IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Nucleic Acids Res. (0305-1048) 2013 imex curation Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de 19-Jun-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de Accepted 2013-JUN-06 by PPORRAS 19-Jun-2013: Contacted by IntAct-Help. Nucleic Acids Res. (0305-1048) 2013 Only protein-protein interactions imex curation Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Nucleic Acids Res. (0305-1048) 2013 imex curation Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de 19-Jun-2013: Contacted by IntAct-Help. Only protein-protein interactions 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 Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de Accepted 2013-JUN-06 by PPORRAS 19-Jun-2013: Contacted by IntAct-Help. Nucleic Acids Res. (0305-1048) 2013 Only protein-protein interactions imex curation Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs. Nucleic Acids Res. (0305-1048) 2013 imex curation Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de 19-Jun-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro emsa electrophoretic mobility shift assay Gel retardation assay band shift band shift Gel retardation assay emsa weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Koehler C., Round A., Simader H., Suck D., Svergun D. Gel was restained with a 0.1% Toluidinium Blue solution to show presence of tRNA Cytoplasmic and mitochondrial versions of both MetRS and GluRS exist, however these have very different sequences. All modelling data described has been based on the cytoplasmic proteins therefore these must have been the constructs used for the experiments. d.svergun@embl-hamburg.de Accepted 2013-JUN-06 by PPORRAS 19-Jun-2013: Contacted by IntAct-Help. Nucleic Acids Res. (0305-1048) 2013 Only protein-protein interactions imex curation syec_yeast Glutamate--tRNA ligase, cytoplasmic GUS1 YGL245W G0583 HRB724 P85 Glutamyl-tRNA synthetase protein protein yeast Saccharomyces cerevisiae Baker's yeast MPSTLTINGKAPIVAYAELIAARIVNALAPNSIAIKLVDDKKAPAAKLDDATEDVFNKITSKFAAIFDNGDKEQVAKWVNLAQKELVIKNFAKLSQSLETLDSQLNLRTFILGGLKYSAADVACWGALRSNGMCGSIIKNKVDVNVSRWYTLLEMDPIFGEAHDFLSKSLLELKKSANVGKKKETHKANFEIDLPDAKMGEVVTRFPPEPSGYLHIGHAKAALLNQYFAQAYKGKLIIRFDDTNPSKEKEEFQDSILEDLDLLGIKGDRITYSSDYFQEMYDYCVQMIKDGKAYCDDTPTEKMREERMDGVASARRDRSVEENLRIFTEEMKNGTEEGLKNCVRAKIDYKALNKTLRDPVIYRCNLTPHHRTGSTWKIYPTYDFCVPIVDAIEGVTHALRTIEYRDRNAQYDWMLQALRLRKVHIWDFARINFVRTLLSKRKLQWMVDKDLVGNWDDPRFPTVRGVRRRGMTVEGLRNFVLSQGPSRNVINLEWNLIWAFNKKVIDPIAPRHTAIVNPVKIHLEGSEAPQEPKIEMKPKHKKNPAVGEKKVIYYKDIVVDKDDADVINVDEEVTLMDWGNVIITKKNDDGSMVAKLNLEGDFKKTKHKLTWLADTKDVVPVDLVDFDHLITKDRLEEDESFEDFLTPQTEFHTDAIADLNVKDMKIGDIIQFERKGYYRLDALPKDGKPYVFFTIPDGKSVNKYGAKK EADAD430A2D98974 EADAD430A2D98974 symc_yeast Methionine--tRNA ligase, cytoplasmic MES1 Methionyl-tRNA synthetase YGR264C protein protein yeast Saccharomyces cerevisiae Baker's yeast MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLYCPVHNSYLADRYVEGECPKCHYDDARGDQCDKCGALLDPFELINPRCKLDDASPEPKYSDHIFLSLDKLESQISEWVEKASEEGNWSKNSKTITQSWLKDGLKPRCITRDLVWGTPVPLEKYKDKVLYVWFDATIGYVSITSNYTKEWKQWWNNPEHVSLYQFMGKDNVPFHTVVFPGSQLGTEENWTMLHHLNTTEYLQYENGKFSKSRGVGVFGNNAQDSGISPSVWRYYLASVRPESSDSHFSWDDFVARNNSELLANLGNFVNRLIKFVNAKYNGVVPKFDPKKVSNYDGLVKDINEILSNYVKEMELGHERRGLEIAMSLSARGNQFLQENKLDNTLFSQSPEKSDAVVAVGLNIIYAVSSIITPYMPEIGEKINKMLNAPALKIDDRFHLAILEGHNINKAEYLFQRIDEKKIDEWRAKYGGQQV 11679C1AB8BB5E39 11679C1AB8BB5E39 trnamet tRNA(Met) trna transfer rna transfer ribonucleic acid tRNA transfer RNA trna yeast Saccharomyces cerevisiae Baker's yeast arc1_yeast tRNA-aminoacylation cofactor ARC1 ARC1 G4P1 P42 Acyl-RNA-complex protein 1 GU4 nucleic-binding protein 1 tRNA-interacting factor ARC1 G3085 YGL105W protein protein yeast Saccharomyces cerevisiae Baker's yeast MSDLVTKFESLIISKYPVSFTKEQSAQAAQWESVLKSGQIQPHLDQLNLVLRDNTFIVSTLYPTSTDVHVFEVALPLIKDLVASSKDVKSTYTTYRHILRWIDYMQNLLEVSSTDKLEINHDLDLPHEVIEKKKKAPAGGAADAAAKADEDVSKKAKKQDHPRGKPDEETLKKLREEAKAKKAAKKAANAKQQQEQQNKAPEKPKPSAIDFRVGFIQKAIKHPDADSLYVSTIDVGDEEGPRTVCSGLVKHFPLDAMQERYVVVVCNLKPVNMRGIKSTAMVLCGSNDDKVEFVEPPKDSKAGDKVFFEGFGDEAPMKQLNPKKKIWEHLQPHFTTNDGLEVIFKDEEEKDHPVRKLTNAKGESFKVASIANAQVR B0CD64AD564900C7 B0CD64AD564900C7 trna transfer RNA trna transfer rna transfer ribonucleic acid tRNA transfer RNA trna yeast Saccharomyces cerevisiae Baker's yeast trnaglu CHEBI:29175 trna transfer rna transfer ribonucleic acid tRNA transfer RNA trna yeast Saccharomyces cerevisiae Baker's yeast arc1-gus1-1 2 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association fig. 2 arc1-gus1-7 2 8 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association fig. 2 The reconstituted complexes were formed using tRNAMet and tRNAGlu but these could not be differentiated in this experiment. arc1-gus1-3 1 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component yeast Saccharomyces cerevisiae Baker's yeast 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component yeast Saccharomyces cerevisiae Baker's yeast physical association physical association Fig. 5, Supp. Fig. 2 arc1-gus1-4 1 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association Fig. 5, Supp. Fig. 2 arc1-gus1-5 1 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 5, Supp. Fig. 2 arc1-gus1-6 1 7 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 5, Supp. Fig. 2 arc1-gus1-8 3 4 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role prey prey yeast Saccharomyces cerevisiae Baker's yeast 6 unspecified role unspecified role bait bait region 32p radiolabel 32p radiolabel P32 32P 32P P32 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined yeast Saccharomyces cerevisiae Baker's yeast 7 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role prey prey ecoli Escherichia coli (strain K12) physical association physical association Fig. 3 A competition assay revealed that a high concentration of tRNAGlu did not influence the binding capacity of tRNAMet to the complex demonstrating that tRNAMet and tRNAGlu both bind to the complex and that both tRNAs were bound independently from each other