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/ http://www.ebi.ac.uk/ hosoya_mats-2005-1 Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. in vitro In vitro affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom edman degradation edman degradation Hosoya-Matsuda N., Motohashi K., Yoshimura H., Nozaki A., Inoue K., Ohmori M., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The method involves mutation of the buried redox-active cysteine of Trx, which favors the formation of stable mixed disulphides with its target proteins. Purified mutated Trx used as bait was bound to CNBR-activated sepharose. The cytosolic fraction fraction of Synechocystis was loaded on the column. Eluates from the chromatography experiment were analyzed by SDS-PAGE. Table 1, fig 1 thisabor@res.titech.ac.jp J. Biol. Chem. (0021-9258) 2005 Only protein-protein interactions imex curation hosoya_mats-2005-2 Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. in vitro In vitro bn-page blue native page bn-page predetermined predetermined participant predetermined Hosoya-Matsuda N., Motohashi K., Yoshimura H., Nozaki A., Inoue K., Ohmori M., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The method involves mutation of the buried redox-active cysteine of Trx, which favors the formation of stable mixed disulphides with its target proteins. Purified mutated Trx used as bait was bound to CNBR-activated sepharose. The cytosolic fraction fraction of Synechocystis was loaded on the column. Eluates from the chromatography experiment were analyzed by SDS-PAGE. Table 1, fig 1 thisabor@res.titech.ac.jp J. Biol. Chem. (0021-9258) 2005 Only protein-protein interactions imex curation hosoya_mats-2005-3 Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Hosoya-Matsuda N., Motohashi K., Yoshimura H., Nozaki A., Inoue K., Ohmori M., Hisabori T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species The method involves mutation of the buried redox-active cysteine of Trx, which favors the formation of stable mixed disulphides with its target proteins. Purified mutated Trx used as bait was bound to CNBR-activated sepharose. The cytosolic fraction fraction of Synechocystis was loaded on the column. Eluates from the chromatography experiment were analyzed by SDS-PAGE. Table 1, fig 1 thisabor@res.titech.ac.jp J. Biol. Chem. (0021-9258) 2005 Only protein-protein interactions imex curation p73489_syny3 ssl2245 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSINAYKLATTLTEDGTLLLQDLPCPAGTSVEVIVLVAPQGMVLPQAERAQGPAPGKVGEAGADYMAATADTMTEWNSEADNSAYRHL thio2_syny3 Thioredoxin-like protein slr1139 slr1139 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MSLLEITDAEFEQETQGQTKPVLVYFWASWCGPCRLMAPAIQAIAKDYGDKLKVLKLEVDPNPAAVAQCKVEGVPALRLFKNNELVMTHEGAIAKPKLLELLKEELDFI p73348_syny3 slr1198 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MALQLGDVVPDFTQESSQGPISFHEWAGDSWVVLFSHPADYTPVCTTELGTVAKLKPEFDKRNVKVIALSVDDVESHKGWICDIDETQNTTVNYPILADGDKKVSDLYGMIHPNALNNLTVRSVFIIDPAKKLRLTFTYPASTGRNFDEILRVIDSLQLTDYHQVATPANWQDGDKCVVVPSISTEDAKVKFPKGVEEIKPYLRLTPQPNK prx5_syny3 Peroxiredoxin sll1621 Glutathione-dependent peroxiredoxin sll1621 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MTPERVPSVVFKTRVRDESVPGPNPYRWEDKTTEQIFGGKKVVLFSLPGAFTPTCSSNHLPRYEQLFEEFQALGVDDIICLSVNDAFVMFQWGKQIGADKVKLLPDGNGEFTRKMGMLVEKSNLGFGMRSWRYSMFVNDGKIEKMFIEPEFGDNCPVDPFECSDADTMLAYLKGAEAPGVSEPVKAFVG phcb_syny3 C-phycocyanin beta subunit cpcB sll1577 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MFDVFTRVVSQADARGEYLSGSQLDALSATVAEGNKRIDSVNRITGNASAIVSNAARALFAEQPQLIQPGGNAYTSRRMAACLRDMEIILRYVTYATFTGDASVLEDRCLNGLRETYVALGVPGASVAAGVQKMKEAALDIVNDPNGITRGDCSAIVAEIAGYFDRAAAAVA apcb_syny3 Allophycocyanin beta chain apcB slr1986 protein protein syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) MQDAITAVINSADVQGKYLDGAAMDKLKSYFASGELRVRAASVISANAATIVKEAVAKSLLYSDVTRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDASILDERVLNGLKETYNSLGVPISSTVQAIQAIKEVTASLVGADAGKEMGVYLDYICSGLS glrx1_ecoli Glutaredoxin 1 grxA grx b0849 JW0833 protein protein ecoli Escherichia coli (strain K12) MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA trxa-sll2245-1 Synechocystis TrxA-linked protein: sll2245 331182 N/A 331185 unspecified role unspecified role prey prey syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) N/A 331186 unspecified role unspecified role bait bait P73263:p.Cys34Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction false false false trxa-slr1998-2 Synechocystis TrxA-linked protein: rehydryn 331182 N/A 331186 unspecified role unspecified role bait bait P73263:p.Cys34Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) N/A 331187 unspecified role unspecified role prey prey syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) direct interaction direct interaction false false false trxa-sll1621-2 Synechocystis TrxA-linked protein: AhpC/TSA family protein 331182 N/A 331188 unspecified role unspecified role prey prey syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) N/A 331186 unspecified role unspecified role bait bait P73263:p.Cys34Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) physical association physical association false false false trxa-cpcb-1 Synechocystis TrxA-linked protein: phycocyanin beta subunit 331182 N/A 331186 unspecified role unspecified role bait bait P73263:p.Cys34Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) N/A 331189 unspecified role unspecified role prey prey syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) direct interaction direct interaction false false false trxa-apcb-1 Synechocystis TrxA-linked protein: Allophycocyanin beta 331182 N/A 331190 unspecified role unspecified role prey prey syny3 Synechocystis sp. (strain PCC 6803 / Kazusa) N/A 331186 unspecified role unspecified role bait bait P73263:p.Cys34Ser mutation increasing mutation increasing interaction mutation increasing certain certain sequence position certain certain certain sequence position certain false ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction false false false y1621-y1621-1 Intermolecular disulfide bond forming sll1621 dimer 331183 N/A 331188 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) N/A 331188 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) disulfide bond disulfide bond disulfide bridge SS-bond false false false Intermolecular disulfide formation under oxidized conditions such as incubation with H2O2. Reduction conditions such as incubation with GSH or Trx disrupt the interaction. y1198-y11198-1 Intermolecular disulfide bond forming slr1198 dimer 331183 N/A 331187 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) N/A 331187 unspecified role unspecified role neutral component neutral component ecobb Escherichia coli (strain B / BL21) disulfide bond disulfide bond disulfide bridge SS-bond false false false Intermolecular disulfide formation under oxidized conditions such as incubation with H2O2. Reduction conditions such as incubation with NADPH, AtNTR and TrxA disrupt the interaction. y1621-thrxa-1 Oxidoreduction reaction between Trx and SLL1621 331184 N/A 331186 electron donor electron donor unspecified role unspecified role ecoli Escherichia coli (strain K12) N/A 331188 electron acceptor electron acceptor unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false SLL1621 could reduce H2O2, t-BOOH, and CHP coupled oxidation of NADPH in the presence of TrxA and AtNTR, although the activity was considerably low. y1621-thrxa-2 Oxidoreduction reaction between GSH and SLL1621 331184 N/A 331191 electron donor electron donor unspecified role unspecified role N/A 331188 electron acceptor electron acceptor unspecified role unspecified role ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false GSH is the best electron donor for SLL1621 studied here. SLL1621 could reduce better the subtrate t-BOOH than H2O2. Acceleration of the peroxidase activity by adding Grx but only 10-20%.