DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis

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 i...

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Veröffentlicht in:	Biochimica et biophysica acta 2010-06, Vol.1804 (6), p.1301-1309
Hauptverfasser:	Li, Haiming, Chang, Limei, Howell, Jenika M., Turner, Raymond J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Chaperones Coenzymes - biosynthesis Coenzymes - chemistry Coenzymes - genetics DmsD Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Intracellular Signaling Peptides and Proteins Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - genetics Iron-Sulfur Proteins - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Metalloproteins - biosynthesis Metalloproteins - chemistry Metalloproteins - genetics Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - metabolism Molybdenum cofactor biosynthesis pathway Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - metabolism Protein Folding Protein–protein interactions Pteridines - chemistry Tat
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