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]]: | + | * [[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
Contents
The RAP proteins of B. subtilis, their cognate peptides and target proteins
- RapA, PhrA: RapA dephosphorylates Spo0F-P
- RapB: dephosphorylates Spo0F-P
- RapC, PhrC: RapC inhibits the DNA-binding activity of ComA-P
- RapD: RapD inhibits the DNA-binding activity of ComA-P
- RapE, PhrE: RapE dephosphorylates Spo0F-P
- RapF, PhrF: RapF inhibits the DNA-binding activity of ComA-P
- RapG, PhrG: RapG inhibits the DNA-binding activity of DegU-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
- RapJ: dephosphorylates Spo0F
- RapK, PhrK: RapK inhibits the DNA-binding activity of ComA-P
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)
