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 The alr2505 (osiS) gene from Anabaena sp. strain PCC7120 encodes a cysteine desulfurase induced by oxidative stress. The alr2505 (osiS) gene from Anabaena sp. strain PCC7120 encodes a cysteine desulfurase induced by oxidative stress. FEBS J. (1742-464X) 2010 imex curation Ruiz M., Bettache A., Janicki A., Vinella D., Zhang CC., Latifi A. Only protein-protein interactions ecoli Escherichia coli (strain K12) 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 predetermined predetermined participant predetermined Ruiz M., Bettache A., Janicki A., Vinella D., Zhang CC., Latifi A. FEBS J. (1742-464X) 2010 Only protein-protein interactions imex curation q8yu51_noss1 Cysteine desulfurase alr2505 protein protein noss1 Nostoc sp. (strain PCC 7120 / UTEX 2576) MSNRPIYLDCHATTPLDEQVLAVMLPYFTEKFGNPASIGHIYGWEAEAAVKQAREILAAEINASPEEIIFTSGATEANNLAIKGVAEAYFQKGQHIITVATEHHAVIDPCEYLKTLGFEITILSVQADGLIDLAQLEKALRPETILVSVMAANNEIGVLQPLAEIGEMCRTHNIIFHTDAAQAIGKIPLDVQAMNIDLMSLTAHKVYGPKGIGALYVRRRNPRVQLAPQQHGGGHERGMRSGTLYTPQIVGFAKAVEIALAEQTTENQRLTQLRDRLWSQLAQLEGIHLNGHPTQRLAGNLNISIEGVDGAALQLGLQPVVAVSSGSACSSTKTAPSHVLTALGSPEKLAYASIRFGIGRFNTAEEIDIVAKHAIATIQSLRKQATLV mint 8787DBC2B4FF9CD2 q8yu51-q8yu51 1 osiS 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component 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 osis 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component 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 physical association physical association f2b mint The interactions between OsiS monomers were analyzed using a bacterial two-hybrid system that exploits the fact that the catalytic domain of adenylate cyclase of Bordetella pertussis consists of two complementary fragments T25 and T18. These fragments are not active when physically separated. However, if these fragments are fused to interacting proteins homo or heterodimerization of the resultant hybrid proteins reconstitutes an active adenylate cyclase.