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http://purl.uniprot.org/citations/20153451http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20153451http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20153451http://www.w3.org/2000/01/rdf-schema#comment"Many bacterial oxidoreductases depend on the Tat translocase for correct cell localization. Substrates for the Tat translocase possess twin-arginine leaders. System specific chaperones or redox enzyme maturation proteins (REMPs) are a group of proteins implicated in oxidoreductase maturation. DmsD is a REMP discovered in Escherichia coli, which interacts with the twin-arginine leader sequence of DmsA, the catalytic subunit of DMSO reductase. In this study, we identified several potential interacting partners of DmsD by using several in vitro protein-protein interaction screening approaches, including affinity chromatography, co-precipitation, and cross-linking. Candidate hits from these in vitro findings were analyzed by in vivo methods of bacterial two-hybrid (BACTH) and bimolecular fluorescence complementation (BiFC). From these data, DmsD was confirmed to interact with the general molecular chaperones DnaK, DnaJ, GrpE, GroEL, Tig and Ef-Tu. In addition, DmsD was also found to interact with proteins involved in the molybdenum cofactor biosynthesis pathway. Our data suggests that DmsD may play a role as a "node" in escorting its substrate through a cascade of chaperone assisted protein-folding maturation events."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2010.01.022"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2010.01.022"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Chang L."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Chang L."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Howell J.M."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Howell J.M."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Turner R.J."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/author"Turner R.J."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/pages"1301-1309"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/pages"1301-1309"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/title"DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/title"DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis."xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/volume"1804"xsd:string
http://purl.uniprot.org/citations/20153451http://purl.uniprot.org/core/volume"1804"xsd:string
http://purl.uniprot.org/citations/20153451http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20153451
http://purl.uniprot.org/citations/20153451http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20153451