Response regulator

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*'''RR Spo0''' is the sporulation response regulator<ref>PMID:12829280</ref>. <br />
*'''RR Spo0''' is the sporulation response regulator<ref>PMID:12829280</ref>. <br />
*'''RR PleD''' is required in loss of motility<ref>PMID:7592388</ref>. For details see [[PleD activation]], [[PleD allosteric product inhibition]], [[PleD catalysis]] and [[Response regulator PLED in complex with C-di-GMP]]<br />
*'''RR PleD''' is required in loss of motility<ref>PMID:7592388</ref>. For details see [[PleD activation]], [[PleD allosteric product inhibition]], [[PleD catalysis]] and [[Response regulator PLED in complex with C-di-GMP]]<br />
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*'''RR PhoP''' is important for survival under conditions of macrophage-induced stress<ref>PMID:7592388</ref>. For details see [[PhoP Regulatory Domain]] and [[PhoP-PhoQ]]<br />
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*'''RR PhoP''' is important for survival under conditions of macrophage-induced stress<ref>PMID:21634789</ref>. For details see [[PhoP Regulatory Domain]] and [[PhoP-PhoQ]]<br />
*'''Photosynthetic apparatus RR''' in ''Rhodobacter sphaeroides'' is involved in the transduction of signals which monitor oxygen levels. <ref>PMID:8955382</ref>. For details see [[PrrA in Rhodobacter sphaeroides]] <br />
*'''Photosynthetic apparatus RR''' in ''Rhodobacter sphaeroides'' is involved in the transduction of signals which monitor oxygen levels. <ref>PMID:8955382</ref>. For details see [[PrrA in Rhodobacter sphaeroides]] <br />
*'''RR WspR''' couples the chemosensory Wsp pathway to the overproduction of acetylated cellulase <ref>PMID:17379708</ref>. For details see [[WspR]].<br />
*'''RR WspR''' couples the chemosensory Wsp pathway to the overproduction of acetylated cellulase <ref>PMID:17379708</ref>. For details see [[WspR]].<br />

Revision as of 06:58, 7 August 2016

Template:STRUCTURE 1kgs

Response regulators (RR) are part of the two-component signal transduction systems which enable bacteria to sense and respond to a wide range of environments. Two-component RR is a complex of histidine kinase (sensor protein SP) and RR. The RR act as phosphorylation-activated switches. Most RR consist of N terminal which is the signal receiving domain and C terminal which is the DNA-binding domain.

3D Structures of response regulator

Updated on 07-August-2016

References

  1. Smith JG, Latiolais JA, Guanga GP, Citineni S, Silversmith RE, Bourret RB. Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY. J Bacteriol. 2003 Nov;185(21):6385-91. PMID:14563873
  2. Ladds JC, Muchova K, Blaskovic D, Lewis RJ, Brannigan JA, Wilkinson AJ, Barak I. The response regulator Spo0A from Bacillus subtilis is efficiently phosphorylated in Escherichia coli. FEMS Microbiol Lett. 2003 Jun 27;223(2):153-7. PMID:12829280
  3. Hecht GB, Newton A. Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. J Bacteriol. 1995 Nov;177(21):6223-9. PMID:7592388
  4. Menon S, Wang S. Structure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver Domain. Biochemistry. 2011 Jul 5;50(26):5948-57. Epub 2011 Jun 13. PMID:21634789 doi:10.1021/bi2005575
  5. Eraso JM, Kaplan S. Complex regulatory activities associated with the histidine kinase PrrB in expression of photosynthesis genes in Rhodobacter sphaeroides 2.4.1. J Bacteriol. 1996 Dec;178(24):7037-46. PMID:8955382
  6. Malone JG, Williams R, Christen M, Jenal U, Spiers AJ, Rainey PB. The structure-function relationship of WspR, a Pseudomonas fluorescens response regulator with a GGDEF output domain. Microbiology. 2007 Apr;153(Pt 4):980-94. PMID:17379708 doi:http://dx.doi.org/10.1099/mic.0.2006/002824-0

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