Difference between revisions of "Phosphorelay"

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* 3.4.7. [[Phosphorelay]]
 
* 3.4.7. [[Phosphorelay]]
 
* 3.4.8. [[Quorum sensing]]
 
* 3.4.8. [[Quorum sensing]]
 +
* 3.4.9. [[Other regulators]]
 
|Related=
 
|Related=
 
see Table to the right  
 
see Table to the right  
Line 36: Line 37:
  
 
==The kinases==
 
==The kinases==
−
* [[KinA]] (controlled by [[Sda]], [[KipI]], and [[KipA]])
+
* [[KinA]] (controlled by [[Sda]], [[SivA]], [[BslA]], [[KipI]], and [[KipA]])
 
* [[KinB]] (controlled by [[Sda]], [[KbaA]], and [[KapB]])
 
* [[KinB]] (controlled by [[Sda]], [[KbaA]], and [[KapB]])
 
* [[KinC]]
 
* [[KinC]]
 
* [[KinD]]
 
* [[KinD]]
 
* [[KinE]]
 
* [[KinE]]
 +
 +
==Proteins controlliing the activity of the kinases==
 +
* [[BslA]]
 +
* [[KapB]]
 +
* [[KbaA]]
 +
* [[KipA]]
 +
* [[KipI]]
 +
* [[Sda]]
 +
* [[SivA]]
 +
* [[SivC]]
  
 
==The phosphotransferases==
 
==The phosphotransferases==
Line 57: Line 68:
 
* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
 
* [[RapE]], [[PhrE]]: dephosphorylation of [[Spo0F]]
 
* [[RapH]]: dephosphorylation of [[Spo0F]]
 
* [[RapH]]: dephosphorylation of [[Spo0F]]
 +
* [[RapP]]: dephosphorylation of [[Spo0F]] {{PubMed|23524609}}
 +
 +
== 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==
−
<pubmed> 20238180 </pubmed>
+
<pubmed> 20238180 25341802 27122155</pubmed>
 +
 
 
==Reviews==
 
==Reviews==
−
'''Additional reviews:''' {{PubMed|21435030}}
+
<pubmed>8730857 11587783 9778730 1664534 12406209 11489844 10745001 8432743 19995980 19943903 20133180 20154131 21435030 27501460 26941227 32156829,32156813
−
<pubmed>8730857 11587783 9778730 1664534 12406209 11489844 10745001 8432743 19995980 19943903 20133180 20154131</pubmed>
+
</pubmed>
  
 
==Important original publications==
 
==Important original publications==
−
'''Additional original publications:''' {{PubMed|23169620,22146301}}
+
<pubmed> 21097618 23169620,22146301 26165942 27216630,30212463,35012345</pubmed>
−
<pubmed> 21097618 </pubmed>
 
  
 
=Back to [[categories]]=
 
=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

Heiko Babel, Ilka B Bischofs
Molecular and cellular factors control signal transduction via switchable allosteric modulator proteins (SAMPs).
BMC Syst Biol: 2016, 10;35
[PubMed:27122155] [WorldCat.org] [DOI] (I e)

Adaoha E C Ihekwaba, Ivan Mura, Gary C Barker
Computational modelling and analysis of the molecular network regulating sporulation initiation in Bacillus subtilis.
BMC Syst Biol: 2014, 8;119
[PubMed:25341802] [WorldCat.org] [DOI] (I e)

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

Richard Losick
Concerns about Continuing Claims that a Protein Complex Interacts with the Phosphorelay.
mBio: 2020, 11(2);
[PubMed:32156829] [WorldCat.org] [DOI] (I e)

David Dubnau
Reply to Losick, "Concerns about Continuing Claims that a Protein Complex Interacts with the Phosphorelay".
mBio: 2020, 11(2);
[PubMed:32156813] [WorldCat.org] [DOI] (I e)

Jatin Narula, Masaya Fujita, Oleg A Igoshin
Functional requirements of cellular differentiation: lessons from Bacillus subtilis.
Curr Opin Microbiol: 2016, 34;38-46
[PubMed:27501460] [WorldCat.org] [DOI] (I p)

Daniel Schultz
Coordination of cell decisions and promotion of phenotypic diversity in B. subtilis via pulsed behavior of the phosphorelay.
Bioessays: 2016, 38(5);440-5
[PubMed:26941227] [WorldCat.org] [DOI] (I p)

Peter Dürre
Ancestral sporulation initiation.
Mol Microbiol: 2011, 80(3);584-7
[PubMed:21435030] [WorldCat.org] [DOI] (I p)

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

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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