Response regulator

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 (DBD).

RR CheY is a chemotaxis response regulator in bacteria see Chemotaxis protein.^[1].
RR Spo0 is the sporulation response regulator^[2].
RR PleD is required in loss of motility^[3]. For details see PleD activation, PleD allosteric product inhibition, PleD catalysis and Response regulator PLED in complex with C-di-GMP
RR PhoP is important for survival under conditions of macrophage-induced stress^[4]. For details see PhoP Regulatory Domain and PhoP-PhoQ
Photosynthetic apparatus RR in Rhodobacter sphaeroides is involved in the transduction of signals which monitor oxygen levels. ^[5]. For details see PrrA in Rhodobacter sphaeroides
RR WspR couples the chemosensory Wsp pathway to the overproduction of acetylated cellulase ^[6]. For details see WspR.
Redox RR is DNA-sequence specific. It controls transcription as a result of its phosphorylation by a redox sensor^[7].

For iron response regulator Irr see Irr.

3D Structures of response regulator

Response regulator 3D structure

Se-Met DNA-binding response regulator D complex with thiocyanate, 1kgs

Drag the structure with the mouse to rotate

ReferencesReferences

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Allen JF. Redox control of transcription: sensors, response regulators, activators and repressors. FEBS Lett. 1993 Oct 18;332(3):203-7. PMID:8405457

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

[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

[7] Allen JF. Redox control of transcription: sensors, response regulators, activators and repressors. FEBS Lett. 1993 Oct 18;332(3):203-7. PMID:8405457

[1]

[2]

[3]

[4]

[5]

[6]

[7]