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 An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: 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 An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone. FEBS letters 2015 imex curation An BC., Lee SS., Jung HS., Kim JY., Lee Y., Lee KW., Lee SY., Tripathi BN., Chung BY. bychung@kaeri.re.kr 03-Dec-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation 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 Accepted 2015-NOV-09 AT 14:19 GMT AT 14:19 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation 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 D42EB998870CA489 q88nw9_psepk Alkyl hydroperoxide reductase C tsaA Peroxiredoxin Thioredoxin peroxidase PP_1084 protein protein psepk psepk MSVLVGKKAPDFTVPAVLGNGEIVDSFNLASAIKGKYGLVFFYPLDFTFVCPSELIALDNRIPDFQARNVEVIGVSIDSHFTHNAWRNTPVNNGGIGQVKYTLAADMTHEICKAYDVESEGGVAFRGAFLIDTNGVVRSQIVNDLPLGRNMDELLRLVDALQFHEEHGEVCPANWKKGDKGMNASPEGVAAYLSENAGKL 9005A8156DD24415 q88nw9_psepk-q88nw9_psepk-1 2 5 unspecified role unspecified role neutral component neutral component purified purified 5 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 C S Wed May 02 15:19:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ser' Tue Jun 30 15:56:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ser' Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain C A Wed May 02 20:17:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ala' Tue Jun 30 17:39:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ala' direct interaction direct interaction 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 2 4 unspecified role unspecified role neutral component neutral component purified purified 4 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 A C Wed May 02 17:44:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 18:11:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction 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-2 1 5 unspecified role unspecified role neutral component neutral component purified purified 5 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction 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 1 5 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 C S Wed May 02 14:56:24 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ser' Tue Jun 30 19:49:59 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ser' Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain C A Wed May 02 15:38:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ala' Tue Jun 30 15:44:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ala' direct interaction direct interaction 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 1 4 unspecified role unspecified role neutral component neutral component purified purified 4 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 A C Wed May 02 18:41:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 19:52:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction f2a f2b q88nw9_psepk-q88nw9_psepk-3 3 5 unspecified role unspecified role neutral component neutral component purified purified 5 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 C S Wed May 02 17:09:38 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ser' Tue Jun 30 20:24:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ser' Q88NW9:p.Cys112Ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain C A Wed May 02 18:30:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys112ala' Tue Jun 30 18:50:26 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys112Ala' direct interaction direct interaction 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 3 4 unspecified role unspecified role neutral component neutral component purified purified 4 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 A C Wed May 02 20:32:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ala112cys' Tue Jun 30 17:43:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala112Cys' direct interaction direct interaction f3