Arginine repressor ArgR

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Arginine repressor, C-terminal domain
PDB 1xxa EBI.jpg
c-terminal domain of escherichia coli arginine repressor/ l-arginine complex; pb derivative
Identifiers
Symbol Arg_repressor_C
Pfam PF02863
InterPro IPR020899
SCOP 1aoy
SUPERFAMILY 1aoy
Arginine repressor, DNA binding domain
Identifiers
Symbol Arg_repressor
Pfam PF01316
SCOP 1aoy
SUPERFAMILY 1aoy

In molecular biology, the arginine repressor (ArgR) is a repressor of prokaryotic arginine deiminase pathways.

The arginine dihydrolase (AD) pathway is found in many prokaryotes and some primitive eukaryotes, an example of the latter being Giardia lamblia (Giardia intestinalis).[1] The three-enzyme anaerobic pathway breaks down L-arginine to form 1 mol of ATP, carbon dioxide and ammonia. In simpler bacteria, the first enzyme, arginine deiminase, can account for up to 10% of total cell protein.[1]

Most prokaryotic arginine deiminase pathways are under the control of a repressor gene, termed ArgR.[2] This is a negative regulator, and will only release the arginine deiminase operon for expression in the presence of arginine.[3] The crystal structure of apo-ArgR from Bacillus stearothermophilus has been determined to 2.5A by means of X-ray crystallography.[4] The protein exists as a hexamer of identical subunits, and is shown to have six DNA-binding domains, clustered around a central oligomeric core when bound to arginine. It predominantly interacts with A.T residues in ARG boxes. This hexameric protein binds DNA at its N terminus to repress arginine biosyntheis or activate arginine catabolism. Some species have several ArgR paralogs. In a neighbour-joining tree, some of these paralogous sequences show long branches and differ significantly from the well-conserved C-terminal region.

References[edit]

  1. ^ a b Brown DM, Upcroft JA, Edwards MR, Upcroft P (January 1998). "Anaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis". Int. J. Parasitol. 28 (1): 149–64. doi:10.1016/S0020-7519(97)00172-0. PMID 9504342. 
  2. ^ Lu CD, Houghton JE, Abdelal AT (May 1992). "Characterization of the arginine repressor from Salmonella typhimurium and its interactions with the carAB operator". J. Mol. Biol. 225 (1): 11–24. doi:10.1016/0022-2836(92)91022-H. PMID 1583685. 
  3. ^ Maghnouj A, de Sousa Cabral TF, Stalon V, Vander Wauven C (December 1998). "The arcABDC gene cluster, encoding the arginine deiminase pathway of Bacillus licheniformis, and its activation by the arginine repressor argR". J. Bacteriol. 180 (24): 6468–75. PMC 107747. PMID 9851988. 
  4. ^ Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD (May 1999). "Structure of the arginine repressor from Bacillus stearothermophilus". Nat. Struct. Biol. 6 (5): 427–32. doi:10.1038/8229. PMID 10331868. 

This article incorporates text from the public domain Pfam and InterPro IPR020899