Difference between revisions of "Two-component systems"
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Two component systems are signal transduction systems that consist of a sensor kinase and a response regulator (usually a [[transcription factors|transcription factor]]). The kinase autophosphorylates on a His residue (more preciely, one subunit of the dimeric kinase phosphorylates the His residue of the other subunit), and the phosphate group can then be transferred to an aspartate residue in the cognate response regulator. Some response regulators can also autophosphorylate using acety-phosphate as the phosphate donor. | Two component systems are signal transduction systems that consist of a sensor kinase and a response regulator (usually a [[transcription factors|transcription factor]]). The kinase autophosphorylates on a His residue (more preciely, one subunit of the dimeric kinase phosphorylates the His residue of the other subunit), and the phosphate group can then be transferred to an aspartate residue in the cognate response regulator. Some response regulators can also autophosphorylate using acety-phosphate as the phosphate donor. | ||
| − | More complex signal transduction systems of this class are called phosphorelay. The paradigm for a phosphorelay is the pathway leading to the phosphorylation of [[Spo0A]]. | + | More complex signal transduction systems of this class are called [[phosphorelay]]. The paradigm for a [[phosphorelay]] is the pathway leading to the phosphorylation of [[Spo0A]]. |
==Two-component systems in ''B. subtilis'' (kinase, regulator)== | ==Two-component systems in ''B. subtilis'' (kinase, regulator)== | ||
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** [[LytS]], [[LytT]] | ** [[LytS]], [[LytT]] | ||
** [[YesM]], [[YesN]] | ** [[YesM]], [[YesN]] | ||
| − | ** [[YwpD]] (orphan) | + | ** [[YwpD]] (orphan kinase) |
| − | ==The phosphorelay== | + | ==The [[phosphorelay]]== |
* Kinases | * Kinases | ||
** [[KinA]] | ** [[KinA]] | ||
Revision as of 09:39, 28 November 2009
Two component systems are signal transduction systems that consist of a sensor kinase and a response regulator (usually a transcription factor). The kinase autophosphorylates on a His residue (more preciely, one subunit of the dimeric kinase phosphorylates the His residue of the other subunit), and the phosphate group can then be transferred to an aspartate residue in the cognate response regulator. Some response regulators can also autophosphorylate using acety-phosphate as the phosphate donor. More complex signal transduction systems of this class are called phosphorelay. The paradigm for a phosphorelay is the pathway leading to the phosphorylation of Spo0A.
Two-component systems in B. subtilis (kinase, regulator)
- NarL-family
- OmpR family
The phosphorelay
- The ultimate target
Reviews
Rong Gao, Ann M Stock
Biological insights from structures of two-component proteins.
Annu Rev Microbiol: 2009, 63;133-54
[PubMed:19575571]
[WorldCat.org]
[DOI]
(I p)
Martijn Bekker, M Joost Teixeira de Mattos, Klaas J Hellingwerf
The role of two-component regulation systems in the physiology of the bacterial cell.
Sci Prog: 2006, 89(Pt 3-4);213-42
[PubMed:17338439]
[WorldCat.org]
[DOI]
(P p)
Thorsten Mascher, John D Helmann, Gottfried Unden
Stimulus perception in bacterial signal-transducing histidine kinases.
Microbiol Mol Biol Rev: 2006, 70(4);910-38
[PubMed:17158704]
[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)
A H West, A M Stock
Histidine kinases and response regulator proteins in two-component signaling systems.
Trends Biochem Sci: 2001, 26(6);369-76
[PubMed:11406410]
[WorldCat.org]
[DOI]
(P p)
A M Stock, V L Robinson, P N Goudreau
Two-component signal transduction.
Annu Rev Biochem: 2000, 69;183-215
[PubMed:10966457]
[WorldCat.org]
[DOI]
(P p)
V L Robinson, D R Buckler, A M Stock
A tale of two components: a novel kinase and a regulatory switch.
Nat Struct Biol: 2000, 7(8);626-33
[PubMed:10932244]
[WorldCat.org]
[DOI]
(P p)
C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672]
[WorldCat.org]
[DOI]
(P p)
