Phosphorelay

Parent categories	4. Lifestyles 4.2. Sporulation and Germination
Neighbouring categories	4.2.1. Sporulation proteins 4.2.2. Phosphorelay 4.2.3. Sporulation/ other 4.2.4. Germination
Related categories	two-component systems response regulator aspartate phosphatases phosphoproteins protein kinases and phosphatases
Overview on the categories (Excel file) All genes and their categories (Excel file)

Parent categories	3. Information processing 3.4. Regulation of gene expression
Neighbouring categories	3.4.1. Sigma factors and their control 3.4.2. Transcription factors and their control 3.4.3. Trigger enzymes 3.4.4. RNA binding regulators 3.4.5. Regulators of core metabolism 3.4.6. Transition state regulators 3.4.7. Phosphorelay 3.4.8. Quorum sensing 3.4.9. Other regulators
Related categories	see Table to the right
Overview on the categories (Excel file) All genes and their categories (Excel file)

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

• KinA (controlled by Sda, SivA, BslA, KipI, and KipA)
• KinB (controlled by Sda, KbaA, and KapB)
• KinC
• KinD
• KinE

Proteins controlliing the activity of the kinases

• BslA
• KapB
• KbaA
• KipA
• KipI
• Sda
• SivA
• SivC

The phosphotransferases

• Spo0F
• Spo0B

The ultimate target

• Spo0A

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

• Spo0E: dephosphorylation of Spo0A
• YisI: dephosphorylation of Spo0A
• YnzD: dephosphorylation of Spo0A
• RapA, PhrA: dephosphorylation of Spo0F
• RapB: dephosphorylation of Spo0F
• RapE, PhrE: dephosphorylation of Spo0F
• RapH: dephosphorylation of Spo0F
• RapP: dephosphorylation of Spo0F PubMed

Other protein controlling the activity of the phosphorelay

• the YmcA- YlbF-YaaT complex stimulates phosphotransfer to Spo0A PubMed

Reviews

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

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)