Difference between revisions of "Phosphorelay"

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(The kinases)
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* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
 
* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
 
* [[RapH]]: dephosphorylation of [[Spo0F]]
 
* [[RapH]]: dephosphorylation of [[Spo0F]]
 +
 +
== Other protein controlling the activity of the phosphorelay ==
 +
* the [[YmcA]]- [[YlbF]]-[[YaaT]] complex stimulates phosphotransfer to [[Spo0A]] {{PubMed|23490197}}
  
 
==A mathematical model==
 
==A mathematical model==

Revision as of 13:05, 27 March 2013

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see Table to the right






The phosphorelay is a complex variation of a two-component regulatory system. It includes phosphotransferases that transfer the phosphoryl group from the sensor kinases to the ultimate target. The sporulation initiation phosphorelay is the paradigm of this class of signal transduction systems.

The kinases

Proteins controlliing the activity of the kinases

The phosphotransferases

The ultimate target

Phosphatases controlling the phosphorelay (and peptides that modulate their activity)

Other protein controlling the activity of the phosphorelay

A mathematical model

Sara Jabbari, John T Heap, John R King
Mathematical modelling of the sporulation-initiation network in Bacillus subtilis revealing the dual role of the putative quorum-sensing signal molecule PhrA.
Bull Math Biol: 2011, 73(1);181-211
[PubMed:20238180] [WorldCat.org] [DOI] (I p)

Reviews

Additional reviews: PubMed

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Heterochronic phosphorelay gene expression as a source of heterogeneity in Bacillus subtilis spore formation.
J Bacteriol: 2010, 192(8);2053-67
[PubMed:20154131] [WorldCat.org] [DOI] (I p)

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)

Daelynn R Buelow, Tracy L Raivio
Three (and more) component regulatory systems - auxiliary regulators of bacterial histidine kinases.
Mol Microbiol: 2010, 75(3);547-66
[PubMed:19943903] [WorldCat.org] [DOI] (I p)

Keith Stephenson, James A Hoch
Evolution of signalling in the sporulation phosphorelay.
Mol Microbiol: 2002, 46(2);297-304
[PubMed:12406209] [WorldCat.org] [DOI] (P 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 A Hoch, K I Varughese
Keeping signals straight in phosphorelay signal transduction.
J Bacteriol: 2001, 183(17);4941-9
[PubMed:11489844] [WorldCat.org] [DOI] (P p)

J A Hoch
Two-component and phosphorelay signal transduction.
Curr Opin Microbiol: 2000, 3(2);165-70
[PubMed:10745001] [WorldCat.org] [DOI] (P p)

M Perego
Kinase-phosphatase competition regulates Bacillus subtilis development.
Trends Microbiol: 1998, 6(9);366-70
[PubMed:9778730] [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)

J A Hoch
The phosphorelay signal transduction pathway in the initiation of Bacillus subtilis sporulation.
J Cell Biochem: 1993, 51(1);55-61
[PubMed:8432743] [WorldCat.org] [DOI] (P p)

K Trach, D Burbulys, M Strauch, J J Wu, N Dhillon, R Jonas, C Hanstein, P Kallio, M Perego, T Bird
Control of the initiation of sporulation in Bacillus subtilis by a phosphorelay.
Res Microbiol: 1991, 142(7-8);815-23
[PubMed:1664534] [WorldCat.org] [DOI] (P p)


Important original publications

Additional original publications: PubMed

Anna L McLoon, Ilana Kolodkin-Gal, Shmuel M Rubinstein, Roberto Kolter, Richard Losick
Spatial regulation of histidine kinases governing biofilm formation in Bacillus subtilis.
J Bacteriol: 2011, 193(3);679-85
[PubMed:21097618] [WorldCat.org] [DOI] (I p)


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