mpidb The Microbial Protein Interaction Database daddaoua-2010-1 Compartmentalized glucose metabolism in Pseudomonas putida is controlled by the PtxS repressor. ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Daddaoua A., Krell T., Alfonso C., Morel B., Ramos J.L. J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation daddaoua-2010-2 Compartmentalized glucose metabolism in Pseudomonas putida is controlled by the PtxS repressor. ecolx Escherichia coli solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Daddaoua A., Krell T., Alfonso C., Morel B., Ramos J.L. J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation yun-2010-1 Pmr, a histone-like protein H1 (H-NS) family protein encoded by the IncP-7 plasmid pCAR1, is a key global regulator that alters host function. in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Yun C.S., Suzuki C., Naito K., Takeda T., Takahashi Y., Sai F., Terabayashi T., Miyakoshi M., Shintani M., Nishida H., Yamane H., Nojiri H. J. Bacteriol. (0021-9193) 2010 Only protein-protein interactions imex curation q88rw2_psepk PP_0017 protein protein psepk psepk MSRLAEFRLLEQQLAAQLAELEALKNDSALKQEMEFETKLRSLLNEYGYGLRQVVLILDPQAVASTDMAPKTSRKPREVKVYKNPHSGEVVETKGGNQRTLKAWKNEYGAEVVESWLAN q88n50_psepk PP_1366 protein protein psepk psepk MSLINEYRATEEAIKELQARLANLSQDDKLKKELEFEGKLRTLMGEYSKSLRDVIALLDPESKLSKAPRGSVKTTVTKRARKVKQYKNPHNGEVIETKGGNHKTLKEWKATWGGDVVESWATLLD q88iq2_psepk PP_2947 protein protein psepk psepk MHMSRLAEFRQLEQKLAAQLAELEAMKSSGELQKEIEFETKLRDLLSKYGYSLRDIINILDPQASRRSAAPAATEKAPRRARQVKQYKNPHNGEVIETKGGNHKLLKEWKAQYGAEEVESWVS q88hh7_psepk ptxS PP_3380 protein protein psepk psepk MTDAPAHTRERVTISEVARVAGVSKATVSRYIGGDRQLLAEATAKRLEEVIERLGYRPNQMARGLKRGQTRLIGMLVADILNPYSVAVMHGVETACRQHGYSLVVCNTNRDDEQERHHLVALQSYNVEGLIVNTLGHHPGELLNLQRDIPMVLVDRQLPELNVDLVGLDNADAVEQALDHLQAQGYRDILAVSEPLDGTSSRLERVQAFGASISRRPGMRQQVLEIGAGLQGQLASFLAHSGHGPQAIFTFNGVATLAVTRALLEAGRNLVADVGLIALDDLDWYPLVGKGITALAQPTERIGVAAFESLLGRLRGDSGAARRIDFKANLIIRGSTQPQ q88gf9_psepk PP_3765 protein protein psepk psepk MSRLAEFRAAEKALQEQMAQLEALKKDAGLKREIEFEQKLVGLMKSYDKSLRDIIAILDPKAVARASSTPPKQQRRPRVVKVYQNPHTGERIETKGGNHRGLKAWKEQYGAATVESWVR ptxs-ptxs-2 1337605 not-defined-1335761978 1337607 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false Figure 3 ptxs-ptxs-1 1337606 not-defined-302440478 1337607 unspecified role unspecified role unspecified role unspecified role region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli Stoichiometry: 2.0 physical association physical association false false false Figure 4 q88rw2-q88rw2 1337628 n/a 1337629 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli n/a 1337629 unspecified role unspecified role prey prey region flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli physical association physical association false false false figure 2B q88rw2-q88n60 1337628 n/a 1337629 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli not-defined-424002861 1337630 unspecified role unspecified role prey prey region Q88N50-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli physical association physical association false false false figure 2B q88rw2-q88iq2 1337628 n/a 1337629 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli not-defined-2097971370 1337631 unspecified role unspecified role prey prey q88iq2-- Q88IQ2-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli physical association physical association false false false figure 2B q88rw2-q88gf9 1337628 n/a 1337629 unspecified role unspecified role bait bait region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli not-defined-238988188 1337632 unspecified role unspecified role prey prey q88gf9-- Q88GF9-- flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecolx Escherichia coli physical association physical association false false false figure 2B DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ pineda_molina-2012-1 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Pineda-Molina E., Reyes-Darias JA., Lacal J., Ramos JL., García-Ruiz JM., Gavira JA., Krell T. DIP original experiment: DIP-251830X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Evidence for chemoreceptors with bimodular ligand-binding regions harboring two signal-binding sites. Pineda-Molina E., Reyes-Darias JA., Lacal J., Ramos JL., García-Ruiz JM., Gavira JA., Krell T. Only protein-protein interactions imex curation mcps_psepk Methyl-accepting chemotaxis protein McpS mcpS PP_4658 protein protein psepk psepk MNSWFANISVNLKLGLGFGLVLVLTGLLALTGWTSLGSLIDRSNWMGDIGQLNKDLTDLRIARLQYMIANGDDTAAANTLAKLDAFSKQQAYLATTFKSPENVKLLGELGDTISAYKLSLNKMRQGYDATRAARVSMDSSAIRADQAMDALSQEVMARPEADSVRLAQYQLISKARQQLLQVRIDVRGYIAENSSANEQAALRQLDAALADTDNLKRQLPSEDARLQQFENAVLAYRDAVRQFRDAVANITTSRAEMTVQGADIVKRSDALYQIQLERRDIESTQARSLQAIATLLALLVGVLAAVLITRQITRPLQDTLVAVEKIASGDLTQHMRVTRRDELGVLQQGIARMGTTLRELISGIRDGVTQIASAAEELSAVTEQTSAGANSQKVETDQVATAMHEMAATVQEVARNAEQASHAATGADDEARAGDRVVGEAIGQIERLAEDMHRSTEAMNLLQQESQKIGSVMDVIKSVAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRGLAQRTQKSTEEIEELIASLQHGTQQVANAMQGSRALTDSSVELARKAGSSLESITSTVSSIQSMNQQIAAAAEQQSAVAEEISRSILNVRDVSEQTAAASDETAASSVELARLGGQLQTLVSQFRV mcps-1 3246597 N/A 3246598 unspecified role unspecified role unspecified role unspecified role Region 46-283 Region 46-283 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint knauer-2012-2 The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation knauer-2012-1 The Fe(II)/α-ketoglutarate-dependent taurine dioxygenases from Pseudomonas putida and Escherichia coli are tetramers. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Knauer SH., Hartl-Spiegelhauer O., Schwarzinger S., Hänzelmann P., Dobbek H. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation an-2015-2 in vitro In vitro bn-page blue native page bn-page weight by staining molecular weight estimation by staining weight by staining An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr FEBS letters 2015 Only protein-protein interactions imex curation imex curation an-2015-1 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr FEBS letters 2015 Only protein-protein interactions imex curation imex curation an-2015-3 in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr FEBS letters 2015 Only protein-protein interactions imex curation imex curation sabbatini-2013-2 Evidence for self-association of the alternative sigma factor σ54. yeast Saccharomyces cerevisiae Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid experimental particp experimental participant identification experimental particp Sabbatini M., Vezzoli A., Milani M., Bertoni G. FEBS J. (1742-464X) 2013 sabbatini-2013-3 Evidence for self-association of the alternative sigma factor σ54. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column experimental particp experimental participant identification experimental particp Sabbatini M., Vezzoli A., Milani M., Bertoni G. FEBS J. (1742-464X) 2013 sabbatini-2013-1 Evidence for self-association of the alternative sigma factor σ54. in vitro In vitro bn-page blue native page bn-page experimental particp experimental participant identification experimental particp Sabbatini M., Vezzoli A., Milani M., Bertoni G. FEBS J. (1742-464X) 2013 taud_ecoli Alpha-ketoglutarate-dependent taurine dioxygenase yaiG 2-aminoethanesulfonate dioxygenase tauD ssiD b0368 JW0360 Sulfate starvation-induced protein 3 protein protein ecoli Escherichia coli (strain K12) MSERLSITPLGPYIGAQISGADLTRPLSDNQFEQLYHAVLRHQVVFLRDQAITPQQQRALAQRFGELHIHPVYPHAEGVDEIIVLDTHNDNPPDNDNWHTDVTFIETPPAGAILAAKELPSTGGDTLWTSGIAAYEALSVPFRQLLSGLRAEHDFRKSFPEYKYRKTEEEHQRWREAVAKNPPLLHPVVRTHPVSGKQALFVNEGFTTRIVDVSEKESEALLSFLFAHITKPEFQVRWRWQPNDIAIWDNRVTQHYANADYLPQRRIMHRATILGDKPFYRAG taud_psepk Alpha-ketoglutarate-dependent taurine dioxygenase tauD atsK PP_0230 protein protein psepk psepk MSLTITPLSPALGAQISGVDISRDISAEERDAIEQALLQHQVLFLRDQPINPEQQARFAARFGDLHIHPIYPNVPDTPQVLVLDTAVTDVRDNAVWHTDVTFLPTPALGAVLSAKQLPAYGGDTLWASGIAAFEALSAPLREMLDGLTATHDFTKSFPLERFGTTPQDLARWEATRRNNPPLSHPVVRTHPVSGRKALFVNEGFTTRINELSELESDALLRLLFAHATRPEFSIRWRWQENDVAFWDNRVTQHFAVDDYRPNRRVMHRATILGDAPF mint lt_sv40 Large T antigen protein protein sv40 sv40 SV40 MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLDWLRNSDDDDEDSQENADKNEDGGEKNMEDSGHETGIDSQSQGSFQAPQSSQSVHDHNQPYHICRGFTCFKKPPTPPPEPET rp54_psepk RNA polymerase sigma-54 factor rpoN ntrA PP_0952 protein protein psepk psepk MKPSLVLKMGQQLTMTPQLQQAIRLLQLSTLDLQQEIQEALESNPMLERQEDGEDFDNSDPMADNAENKPAAEVQDNSFQESTVSADNLEDGEWSERIPNELPVDTAWEDIYQTSASSLPSNDDDEWDFTTRTSAGESLQSHLLWQLNLAPMSDTDRLIAVTLIDSINGQGYLEDTLEEICAGFDPELDIELDEVEAVLHRIQQFEPAGVGARNLGECLLLQLRQLPATTPWMTEAKRLVTDFIDLLGSRDYSQLMRRMKIKEDELRQVIELVQSLNPRPGSQIESSEPEYVVPDVIVRKDSDRWLVELNQEAIPRLRVNPQYAGFVRRADTSADNTFMRNQLQEARWFIKSLQSRNETLMKVATQIVEHQRGFLDHGDEAMKPLVLHDIAEAVGMHESTISRVTTQKYMHTPRGIYELKYFFSSHVSTSEGGECSSTAIRAIIKKLVAAENQKKPLSDSKIAGLLEAQGIQVARRTVAKYRESLGIAPSSERKRLM mint rp54_pseae RNA polymerase sigma-54 factor rpoN PA4462 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MKPSLVLKMGQQLTMTPQLQQAIRLLQLSTLDLQQEIQEALESNPMLERQEDGDDFDNSDPLADGAEQAASAPQESPLQESATPSVESLDDDQWSERIPSELPVDTAWEDIYQTSASSLPSNDDDEWDFTARTSSGESLHSHLLWQVNLAPMSDTDRMIAVTIIDSINNDGYLEESLEEILAAIDPELDVELDEVEVVLRRIQQLEPAGIGARNLRECLLLQLRQLPSTTPWLNEALRLVSDYLDLLGGRDYSQLMRRMKLKEDELRQVIELIQCLHPRPGSQIESSEAEYIVPDVIVRKDNERWLVELNQEAMPRLRVNATYAGMVRRADSSADNTFMRNQLQEARWFIKSLQSRNETLMKVATQIVEHQRGFLDYGEEAMKPLVLHDIAEAVGMHESTISRVTTQKYMHTPRGIFELKYFFSSHVSTAEGGECSSTAIRAIIKKLVAAENAKKPLSDSKIAGLLEAQGIQVARRTVAKYRESLGIAPSSERKRLV mint p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD q88nw9_psepk Alkyl hydroperoxide reductase C tsaA Peroxiredoxin Thioredoxin peroxidase PP_1084 protein protein psepk psepk MSVLVGKKAPDFTVPAVLGNGEIVDSFNLASAIKGKYGLVFFYPLDFTFVCPSELIALDNRIPDFQARNVEVIGVSIDSHFTHNAWRNTPVNNGGIGQVKYTLAADMTHEICKAYDVESEGGVAFRGAFLIDTNGVVRSQIVNDLPLGRNMDELLRLVDALQFHEEHGEVCPANWKKGDKGMNASPEGVAAYLSENAGKL q9hy81_pseae Alkyl hydroperoxide reductase C Peroxiredoxin Thioredoxin peroxidase PA3529 protein protein pseae Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) MSVLVGKKAPDFNVAAVLGNGEIVESFTLSEAIKGKYGLVFFYPLDFTFVCPSELIALDHRIPEFQARNVEVIGVSIDSHFTHNAWRNTPVDKGGIGAVKYTLAADTKHEIAKAYDVESDGGVAFRGAFLIDKEGVVRSQIVNDLPLGRNMDELLRLVDALQFHEEHGEVCPANWKKGDKGMTASPEGVAKYLAENASKL taud-1 1251975 taud tauDpp 1251977 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false sf1 sf2 mint taud-1 1251975 taud tauDEc 1251978 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false sf1 sf2 mint taud-taud 1251976 taud tauDpp 1251977 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.2 taud tauDpp 1251977 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.2 direct interaction direct interaction false false false mint t1 f8 f9 q88nw9_psepk-q88nw9_psepk-2 1883090 N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f2a f2b Wild type (WT)-Prxs and Prx mutants displayed considerably different structural patterns as evident from the result of non-reducing and native PAGE gels of these proteins (Fig. 2A and B). Various oligomeric protein complexes containing both HMW complexes and several LMW forms were observed in WT-PpPrx. The C112S- and C112APpPrx mutants primarily generated dimers as well as fewer HMW complexes than WT-PpPrx (Fig. 2A). q88nw9_psepk-3 1883090 N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified Q88NW9:p.Cys112Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false f2a f2b Wild type (WT)-Prxs and Prx mutants displayed considerably different structural patterns as evident from the result of non-reducing and native PAGE gels of these proteins (Fig. 2A and B). Various oligomeric protein complexes containing both HMW complexes and several LMW forms were observed in WT-PpPrx. The C112S- and C112APpPrx mutants primarily generated dimers as well as fewer HMW complexes than WT-PpPrx (Fig. 2A). q9hy81_pseae-q9hy81_pseae-1 1883090 N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2a f2b q88nw9_psepk-q88nw9_psepk-1 1883091 N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified Q88NW9:p.Cys112Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f1 sf2 f2c F-1 (HMW protein complexes) and F-2 (LMW forms) fractions displayed opposite pattern in peroxidase and chaperone activities. The F-1 fraction exhibited high chaperone activity and low peroxidase activity, whereas the F-2 fraction displayed high peroxidase activity with low chaperone activity (Fig. 1B). These results suggested that oligomerization of the protein into HMW complexes promotes chaperone activity while dissociation of the HMW complexes into LMW species enhances peroxidase activity. The SEC profiles of C112S-PpPrx and C112A-PpPrx were compared with those of WT-PpPrx (Fig. 2C). Like native PAGE gel protein patterns, the SEC chromatogram also showed that the protein structures of C112S-PpPrx, C112A-PpPrx, and WT-PaPrx primarily consisted of LMW structures together with a small number of HMW complexes, whereas the predominant forms of WT-PpPrx and A112C-PaPrx were HMW complexes with a small number of LMW species q88nw9_psepk-1 1883091 N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f1 sf2 f2d F-1 (HMW protein complexes) and F-2 (LMW forms) fractions displayed opposite pattern in peroxidase and chaperone activities. The F-1 fraction exhibited high chaperone activity and low peroxidase activity, whereas the F-2 fraction displayed high peroxidase activity with low chaperone activity (Fig. 1B). These results suggested that oligomerization of the protein into HMW complexes promotes chaperone activity while dissociation of the HMW complexes into LMW species enhances peroxidase activity. q88nw9_psepk-q88nw9_psepk-3 1883092 N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified N/A 1883093 unspecified role unspecified role neutral component neutral component purified purified Q88NW9:p.Cys112Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f3 A comparative electron microscopic (EM) analysis demonstrated the prevalence of HMW and LMW complex structures in the F-1 and F-2 fractions, respectively, of the WT and Prx mutants (Fig. 3). The characteristic appearance of HMW complexes in F-1 fractions were resolved by negative staining followed by single particle image processing (Fig. 3A–E). The protein complexes appeared as spherical shapes with a diameter of 20–40 nm (inset averaged images in Fig. 3A–E). These results, in conjunction with the SEC results (Fig. 2C and D), suggest that probably Cys112 in Prxs participates in the instability of LMW oligomeric complexes (Fig. 3F and J), and enhances the formation of HMW complexes (Fig. 3A and E). The SEC and EM results confirmed that PpPrx primarily consists of HMW complex structures, whereas PaPrx consists predominantly of oligomeric structures. q9hy81_pseae-q9hy81_pseae-2 1883092 N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified N/A 1883094 unspecified role unspecified role neutral component neutral component purified purified Q9HY81:p.Ala112Cys mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f3 rpon-rpon-2 1351063 rpon P. aeruginosa σ54 1351066 predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false rpon P. aeruginosa σ54 1351066 predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false f2c mint P. aeruginosa tp53-lt-5 1351063 p53_human p53 1351067 predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false lt_sv40 SV40T 1351068 predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false f2a homomint mint rpon-rpon-3 1351063 rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false mint f2 f3 P. putida rpon-rpon-4 1351063 rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false mint f2 f3 P. putida rpon-rpon-5 1351063 rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false mint f2 f3 P. putida rpon-1 1351064 rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction false false false f1c mint P. putida rpon-1 1351064 rpon σ54 1351069 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 16.0 direct interaction direct interaction false false false f1c mint P. putida rpon-rpon-1 1351065 rpon σ54 1351069 western blot western blot Immuno blot Immuno blot unspecified role unspecified role neutral component neutral component purified purified rpon σ54 1351069 western blot western blot Immuno blot Immuno blot unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f1b mint P. putida