Difference between revisions of "Response regulator aspartate phosphatases"

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These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the [[phosphorelay]] for sporulation initiation by dephosphorylating [[Spo0F]]-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation).
 
These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the [[phosphorelay]] for sporulation initiation by dephosphorylating [[Spo0F]]-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation).
 
The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.
 
The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.
 +
 +
The RAP phosphatases are made up of the C-terminal tetratricopeptide repeat (TPR) domain that is connected by a flexible helix containing linker to the N-terminal 3-helix bundle. Upon binding of the regulating peptide, the 3-helix bundle and the linker helix undergo a conformational change to form a TPR-like fold that merges with the existing C-terminal TPR domain. {{PubMed|23526881}}
  
 
==The RAP proteins of ''B. subtilis'', their cognate peptides and target proteins==
 
==The RAP proteins of ''B. subtilis'', their cognate peptides and target proteins==
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* [[RapH]]: bifuntional protein: dephosphorylates [[Spo0F]]-P and inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapH]]: bifuntional protein: dephosphorylates [[Spo0F]]-P and inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapI]], [[PhrI]]: [[RapI]] inhibits the DNA-binding activity of [[ImmR]]
 
* [[RapI]], [[PhrI]]: [[RapI]] inhibits the DNA-binding activity of [[ImmR]]
* [[RapJ]]: unknown function
+
* [[RapJ]]: dephosphorylates [[Spo0F]]
 
* [[RapK]], [[PhrK]]: [[RapK]] inhibits the DNA-binding activity of [[ComA]]-P
 
* [[RapK]], [[PhrK]]: [[RapK]] inhibits the DNA-binding activity of [[ComA]]-P
  
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* [[phosphoproteins]]
 
* [[phosphoproteins]]
 
* [[protein kinases and phosphatases]]
 
* [[protein kinases and phosphatases]]
 +
==Structural analysis==
 +
<pubmed> 23526881 </pubmed>
 
==Reviews==
 
==Reviews==
 
<pubmed>8730857 11587783 19995980 9689219 20133180 </pubmed>
 
<pubmed>8730857 11587783 19995980 9689219 20133180 </pubmed>

Latest revision as of 17:36, 27 March 2013

These proteins contain the so-called tetratricopeptide repeats (TPRs) protein-protein interaction module. They control the phosphorelay for sporulation initiation by dephosphorylating Spo0F-P or they inhibit transcription factors by protein-protein interaction (without affecting phosphorylation). The activity of these proteins can be controlled by small peptides that are expressed as precursors, exported, and re-imported into the cell.

The RAP phosphatases are made up of the C-terminal tetratricopeptide repeat (TPR) domain that is connected by a flexible helix containing linker to the N-terminal 3-helix bundle. Upon binding of the regulating peptide, the 3-helix bundle and the linker helix undergo a conformational change to form a TPR-like fold that merges with the existing C-terminal TPR domain. PubMed

The RAP proteins of B. subtilis, their cognate peptides and target proteins

Related lists

Structural analysis

Vijay Parashar, Philip D Jeffrey, Matthew B Neiditch
Conformational change-induced repeat domain expansion regulates Rap phosphatase quorum-sensing signal receptors.
PLoS Biol: 2013, 11(3);e1001512
[PubMed:23526881] [WorldCat.org] [DOI] (I p)

Reviews

Ruth E Silversmith
Auxiliary phosphatases in two-component signal transduction.
Curr Opin Microbiol: 2010, 13(2);177-83
[PubMed:20133180] [WorldCat.org] [DOI] (I p)

Daniel Schultz, Peter G Wolynes, Eshel Ben Jacob, José N Onuchic
Deciding fate in adverse times: sporulation and competence in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2009, 106(50);21027-34
[PubMed:19995980] [WorldCat.org] [DOI] (I p)

M Perego, J A Brannigan
Pentapeptide regulation of aspartyl-phosphate phosphatases.
Peptides: 2001, 22(10);1541-7
[PubMed:11587783] [WorldCat.org] [DOI] (P p)

J Reizer, A Reizer, M Perego, M H Saier
Characterization of a family of bacterial response regulator aspartyl-phosphate (RAP) phosphatases.
Microb Comp Genomics: 1997, 2(2);103-11
[PubMed:9689219] [WorldCat.org] [DOI] (P p)

M Perego, P Glaser, J A Hoch
Aspartyl-phosphate phosphatases deactivate the response regulator components of the sporulation signal transduction system in Bacillus subtilis.
Mol Microbiol: 1996, 19(6);1151-7
[PubMed:8730857] [WorldCat.org] [DOI] (P p)