Difference between revisions of "Phosphorelay"

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{{CategoryTree
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|Parents=
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* 4. [[Lifestyles]]
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** 4.2. [[Sporulation and Germination]]
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|Neighbours=
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* 4.2.1. [[Sporulation proteins]]
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* 4.2.2. [[Phosphorelay]]
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* 4.2.3. [[Sporulation/ other]]
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* 4.2.4. [[Germination]]
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|Related=
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* [[two-component systems]]
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* [[response regulator aspartate phosphatases]]
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* [[phosphoproteins]]
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* [[protein kinases and phosphatases]]
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|}}
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{{CategoryTree
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|Parents=
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* 3. [[Information processing]]
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** 3.4. [[Regulation of gene expression]]
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|Neighbours=
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* 3.4.1. [[Sigma factors and their control]]
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* 3.4.2. [[Transcription factors and their control]]
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* 3.4.3. [[Trigger enzymes]]
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* 3.4.4. [[RNA binding regulators]]
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* 3.4.5. [[Regulators of core metabolism]]
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* 3.4.6. [[Transition state regulators]]
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* 3.4.7. [[Phosphorelay]]
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* 3.4.8. [[Quorum sensing]]
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* 3.4.9. [[Other regulators]]
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|Related=
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see Table to the right
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|}}
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__TOC__
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<br><br><br><br><br>
 
The phosphorelay is a complex variation of a [[two-component systems|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 phosphorelay is a complex variation of a [[two-component systems|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==
 
==The kinases==
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* [[KinA]]
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* [[KinA]] (controlled by [[Sda]], [[SivA]], [[BslA]], [[KipI]], and [[KipA]])
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* [[KinB]]
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* [[KinB]] (controlled by [[Sda]], [[KbaA]], and [[KapB]])
 
* [[KinC]]
 
* [[KinC]]
 
* [[KinD]]
 
* [[KinD]]
 
* [[KinE]]
 
* [[KinE]]
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==Proteins controlliing the activity of the kinases==
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* [[BslA]]
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* [[KapB]]
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* [[KbaA]]
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* [[KipA]]
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* [[KipI]]
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* [[Sda]]
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* [[SivA]]
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* [[SivC]]
  
 
==The phosphotransferases==
 
==The phosphotransferases==
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* [[RapB]]: dephosphorylation of [[Spo0F]]
 
* [[RapB]]: dephosphorylation of [[Spo0F]]
 
* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
 
* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
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* [[RapH]]: dephosphorylation of [[Spo0F]]
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* [[RapP]]: dephosphorylation of [[Spo0F]] {{PubMed|23524609}}
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== Other protein controlling the activity of the phosphorelay ==
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* the [[YmcA]]- [[YlbF]]-[[YaaT]] complex stimulates phosphotransfer to [[Spo0A]] {{PubMed|23490197}}
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==A mathematical model==
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<pubmed> 20238180 25341802 27122155</pubmed>
  
 
==Reviews==
 
==Reviews==
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<pubmed>8730857 11587783 9778730 1664534 12406209 11489844 10745001 8432743 </pubmed>
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<pubmed>8730857 11587783 9778730 1664534 12406209 11489844 10745001 8432743 19995980 19943903 20133180 20154131 21435030 27501460 26941227 32156829,32156813
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</pubmed>
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==Important original publications==
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<pubmed> 21097618 23169620,22146301 26165942 27216630,30212463,35012345</pubmed>
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=Back to [[categories]]=

Latest revision as of 09:46, 21 January 2022

Parent categories
Neighbouring categories
Related categories
Parent categories
Neighbouring categories
Related categories

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


Reviews


Important original publications

Zhuo Chen, Priyanka Srivastava, Brenda Zarazúa-Osorio, Anuradha Marathe, Masaya Fujita, Oleg A Igoshin
Bacillus subtilis Histidine Kinase KinC Activates Biofilm Formation by Controlling Heterogeneity of Single-Cell Responses.
mBio: 2022, 13(1);e0169421
[PubMed:35012345] [WorldCat.org] [DOI] (I p)

Philip Davidson, Rory Eutsey, Brendan Redler, N Luisa Hiller, Michael T Laub, Dannie Durand
Flexibility and constraint: Evolutionary remodeling of the sporulation initiation pathway in Firmicutes.
PLoS Genet: 2018, 14(9);e1007470
[PubMed:30212463] [WorldCat.org] [DOI] (I e)

Jatin Narula, Anna Kuchina, Fang Zhang, Masaya Fujita, Gürol M Süel, Oleg A Igoshin
Slowdown of growth controls cellular differentiation.
Mol Syst Biol: 2016, 12(5);871
[PubMed:27216630] [WorldCat.org] [DOI] (I e)

Jatin Narula, Anna Kuchina, Dong-Yeon D Lee, Masaya Fujita, Gürol M Süel, Oleg A Igoshin
Chromosomal Arrangement of Phosphorelay Genes Couples Sporulation and DNA Replication.
Cell: 2015, 162(2);328-337
[PubMed:26165942] [WorldCat.org] [DOI] (I p)

Jatin Narula, Seram N Devi, Masaya Fujita, Oleg A Igoshin
Ultrasensitivity of the Bacillus subtilis sporulation decision.
Proc Natl Acad Sci U S A: 2012, 109(50);E3513-22
[PubMed:23169620] [WorldCat.org] [DOI] (I p)

Anna Kuchina, Lorena Espinar, Tolga Çağatay, Alejandro O Balbin, Fang Zhang, Alma Alvarado, Jordi Garcia-Ojalvo, Gürol M Süel
Temporal competition between differentiation programs determines cell fate choice.
Mol Syst Biol: 2011, 7;557
[PubMed:22146301] [WorldCat.org] [DOI] (I e)

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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