UniProt UniProt http://www.uniprot.org Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro peptide array peptide array antibody detection identification by antibody antibody detection Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro oxidoreduct assay oxidoreductase assay oxidoreduct assay predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. Protein complexes purified on an immobilized metal affinity column prior to gel filtration. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro emsa electrophoretic mobility shift assay Gel retardation assay band shift band shift Gel retardation assay emsa weight by staining molecular weight estimation by staining weight by staining Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nuclease assay nuclease assay predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. Cleavage product analyzed by denaturing PAGE wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. Protein complexes purified on an immobilized metal affinity column prior to gel filtration. Participant detection by HPLC wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro methyltransferase as methyltransferase assay methyltransferase as predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. To ensure that scattering data were measured on single molecular species without aggregates, size-exclusion chromatographic separations were connected in-line to a SAXS flow cell wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. Protein complexes purified on an immobilized metal affinity column prior to gel filtration. Participant detection by multiangle light scattering. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro dsc differential scanning calorimetry dsc predetermined predetermined participant predetermined Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. There is a discrepnacy between results in Fig. 1C and the text. It is assumed that the text is correct, as this correlates with subsequent data in the paper. Fluorescence intensity of SYPRO ORANGE was measured from 25 to 96 °C wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes. The Journal of biological chemistry 2018 imex curation Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Oerum S., Roovers M., Rambo RP., Kopec J., Bailey HJ., Fitzpatrick F., Newman JA., Newman WG., Amberger A., Zschocke J., Droogmans L., Oppermann U., Yue WW. wyatt.yue@sgc.ox.ac.uk Accepted 2019-DEC-02 AT 15:31 GMT AT 15:31 GMT by PPORRAS The Journal of biological chemistry 2018 Only protein-protein interactions imex curation imex curation tm10c_human tRNA methyltransferase 10 homolog C TRMT10C HBV pre-S2 trans-regulated protein 2 MRPP1 RG9MTD1 RNA (guanine-9-)-methyltransferase domain-containing protein 1 Renal carcinoma antigen NY-REN-49 Mitochondrial ribonuclease P protein 1 mRNA methyladenosine-N(1)-methyltransferase tRNA (adenine(9)-N(1))-methyltransferase tRNA (guanine(9)-N(1))-methyltransferase protein protein human Homo sapiens Human MAAFLKMSVSVNFFRPFTRFLVPFTLHRKRNNLTILQRYMSSKIPAVTYPKNESTPPSEELELDKWKTTMKSSVQEECVSTISSSKDEDPLAATREFIEMWRLLGREVPEHITEEELKTLMECVSNTAKKKYLKYLYTKEKVKKARQIKKEMKAAAREEAKNIKLLETTEEDKQKNFLFLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQEKWDKLLLTSTEKSHVDLFPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILLCLKNNGNWQEALQFVPKRKHTGFLEISQHSQEFINRLKKAKT 28CBD97B4114819F hcd2_human 3-hydroxyacyl-CoA dehydrogenase type-2 HSD17B10 SCHAD XH98G2 HADH2 3-hydroxyacyl-CoA dehydrogenase type II Type II HADH 3-hydroxy-2-methylbutyryl-CoA dehydrogenase Endoplasmic reticulum-associated amyloid beta-peptide-binding protein Short-chain type dehydrogenase/reductase XH98G2 Mitochondrial ribonuclease P protein 2 2-methyl-3-hydroxybutyryl-CoA dehydrogenase ERAB MRPP2 SDR5C1 Short chain dehydrogenase/reductase family 5C member 1 17-beta-estradiol 17-dehydrogenase 3-alpha-(17-beta)-hydroxysteroid dehydrogenase (NAD(+)) 3alpha(or 20beta)-hydroxysteroid dehydrogenase 7-alpha-hydroxysteroid dehydrogenase protein protein human Homo sapiens Human MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP 9E74F242E3E6FEF1 brexanolone brexanolone (3alpha,5alpha)-3-hydroxypregnan-20-one 3alpha,5alpha-tetrahydroprogesterone 3alpha,5alpha-THP 3alpha-hydroxy-5alpha-dihydroprogesterone 3alpha-hydroxy-5alpha-pregnan-20-one 3alpha-OH DHP 5alpha-pregnan-3alpha-ol-20-one allopregnan-3alpha-ol-20-one allopregnanolone allotetrahydroprogesterone brexanolona brexanolone brexanolonum SAGE-547 SGE-102 Zulresso 3alpha-hydroxy-5alpha-pregnan-20-one small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) s-adenosyl-l-methioninate S-adenosyl-L-methioninate AdoMet S-Adenosylmethionine SAM [(3S)-3-amino-3-carboxylatopropyl](5'-deoxyadenosin-5'-yl)(methyl)sulfonioacetate small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) s-adenosyl-s-carboxymethyl-l-homocysteine S-adenosyl-S-carboxymethyl-L-homocysteine carboxy-SAM Cx-SAM carboxy-S-adenosyl-L-methionine small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) mt-tv_human_rna pre-(mt)tRNAVal trna transfer rna transfer ribonucleic acid tRNA transfer RNA trna human Homo sapiens Human adenosine 3'-monophosphate adenosine 3'-monophosphate (3'-AMP) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) mt-ti_human_rna pre-(mt)tRNAIle trna transfer rna transfer ribonucleic acid tRNA transfer RNA trna human Homo sapiens Human nadh Nicotinamide adenine dinucleotide, reduced form small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) mrpp3_human Mitochondrial ribonuclease P catalytic subunit PRORP KIAA0391 MRPP3 Mitochondrial ribonuclease P protein 3 Protein only RNase P catalytic subunit protein protein human Homo sapiens Human MTFYLFGIRSFPKLWKSPYLGLGPGHSYVSLFLADRCGIRNQQRLFSLKTMSPQNTKATNLIAKARYLRKDEGSNKQVYSVPHFFLAGAAKERSQMNSQTEDHALAPVRNTIQLPTQPLNSEEWDKLKEDLKENTGKTSFESWIISQMAGCHSSIDVAKSLLAWVAAKNNGIVSYDLLVKYLYLCVFHMQTSEVIDVFEIMKARYKTLEPRGYSLLIRGLIHSDRWREALLLLEDIKKVITPSKKNYNDCIQGALLHQDVNTAWNLYQELLGHDIVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFAHSIKTWFESVPGKQWKGQFTTVRKSGQCSGCGKTIESIQLSPEEYECLKGKIMRDVIDGGDQYRKTTPQELKRFENFIKSRPPFDVVIDGLNVAKMFPKVRESQLLLNVVSQLAKRNLRLLVLGRKHMLRRSSQWSRDEMEEVQKQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHKACLPDAKTQRLFFKWQQGHQLAIVNRFPGSKLTFQRILSYDTVVQTTGDSWHIPYDEDLVERCSCEVPTKWLCLHQKT 6AB17E7E8820D818 trmt10c-1 4 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 3A, Supp Figs. 3 & 5 trmt10c-2 10 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1B s_adenosyl_l_methioninate-trmt10c-1 11 16 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1C s_adenosyl_s_carboxymethyl_l_homocysteine-trmt10c-1 11 17 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Fig. 1B adenosine 3'_monophosphate-trmt10c-1 11 19 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Fig. 1B s_adenosyl_l_methioninate-trmt10c-2 1 16 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1 R work = 0.1946 R free = 0.2173 hsd17b10-trmt10c-1 10 13 unspecified role unspecified role neutral component neutral component purified purified region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 3B hsd17b10-trmt10c-2 2 13 unspecified role unspecified role bait bait purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 14 unspecified role unspecified role prey prey purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 3C Additional binding regions were identified at end of the N domain and start of the methyltransferase domains, within the methyltransferase domain, and in the C terminal but exact coordinates were not given. hsd17b10-trmt10c-3 10 20 unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Fig. 4A hsd17b10-mt_ti_human_rna-1 5 20 unspecified role unspecified role bait bait purified purified in vitro In vitro 13 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role prey prey purified purified ecoli Escherichia coli (strain K12) physical association physical association Fig. 4B, 4C hsd17b10-trmt10c-4 5 13 unspecified role unspecified role prey prey purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 20 unspecified role unspecified role bait bait purified purified direct interaction direct interaction Fig.4C hsd17b10-mt_ti_human_rna-2 8 20 enzyme target enzyme target substrate substrate neutral component neutral component purified purified in vitro In vitro 13 enzyme enzyme neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q7L0Y3:p.Asp314Asn mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D N Tue Jun 30 19:32:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp314Asn' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Q7L0Y3:p.Gln226Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain Q A Tue Jun 30 19:28:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln226Ala' region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) methylation methylation reaction methylation Fig. 4D hsd17b10-mt_tv_human_rna-1 8 18 enzyme target enzyme target substrate substrate neutral component neutral component purified purified in vitro In vitro 13 enzyme enzyme neutral component neutral component purified purified Q7L0Y3:p.Asp314Asn mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D N Tue Jun 30 20:14:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp314Asn' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Q7L0Y3:p.Gln226Ala mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain Q A Tue Jun 30 18:33:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln226Ala' region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) methylation methylation reaction methylation Fig. 4D brexanolone-hsd17b10-1 3 15 enzyme target enzyme target substrate substrate neutral component neutral component 14 enzyme enzyme neutral component neutral component purified purified ecoli Escherichia coli (strain K12) redox reaction oxidoreductase activity electron transfer reaction redox reaction Fig. 4E hsd17b10-kiaa0391-3 4 22 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 20 unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Fig. 5B, Supp. Fig. 5 hsd17b10-kiaa0391-4 4 22 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Fig. 5B,Supp. Fig. 5 hsd17b10-mt_ti_human_rna-3 6 22 enzyme enzyme neutral component neutral component purified purified region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 20 enzyme target enzyme target substrate substrate neutral component neutral component purified purified in vitro In vitro 13 ancillary ancillary neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) rna cleavage rna cleavage Fig. 5C, 5D Reaction is divalent metal cation dependent hsd17b10-kiaa0391-5 9 22 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 20 unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Table 2 hsd17b10-mt_ti_human_rna-4 9 20 unspecified role unspecified role neutral component neutral component purified purified in vitro In vitro 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Table 2 hsd17b10-trmt10c-5 11 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Fig. 1F hsd17b10-nadh-1 11 21 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Fig. 1F hsd17b10-s_adenosyl_l_methioninate-1 11 16 unspecified role unspecified role neutral component neutral component 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 13 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp. Fig. 1F hsd17b10-trmt10c-6 4 13 unspecified role unspecified role neutral component neutral component purified purified region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp Fig. 3A, 3B hsd17b10-trmt10c-7 12 13 unspecified role unspecified role neutral component neutral component purified purified region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Supp Fig. 3C hsd17b10-trmt10c-8 7 13 unspecified role unspecified role neutral component neutral component purified purified region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 4A hsd17b10-trmt10c-9 9 13 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 14 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) physical association physical association Table 2