Difference between revisions of "Two-component systems"
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** [[NatK]], [[NatR]] | ** [[NatK]], [[NatR]] | ||
** [[PhoR]], [[PhoP]] | ** [[PhoR]], [[PhoP]] | ||
+ | ** [[PsdS]], [[PsdR]] | ||
** [[ResE]], [[ResD]] | ** [[ResE]], [[ResD]] | ||
** [[WalK]], [[WalR]]: the only essential two-component system! | ** [[WalK]], [[WalR]]: the only essential two-component system! | ||
Line 25: | Line 26: | ||
** [[YclK]], [[YclJ]] | ** [[YclK]], [[YclJ]] | ||
** [[YkoH]], [[YkoG]] | ** [[YkoH]], [[YkoG]] | ||
− | ** [[ | + | ** [[YrkQ]], [[YrkP]] |
− | |||
** [[YvrG]], [[YvrHb]] | ** [[YvrG]], [[YvrHb]] | ||
** [[YxdK]], [[YxdJ]] | ** [[YxdK]], [[YxdJ]] | ||
Line 43: | Line 43: | ||
** [[YesM]], [[YesN]] | ** [[YesM]], [[YesN]] | ||
** [[YwpD]] (orphan kinase) | ** [[YwpD]] (orphan kinase) | ||
+ | |||
+ | * Orphan response regulator | ||
+ | ** [[YneI]] | ||
==The [[phosphorelay]]== | ==The [[phosphorelay]]== | ||
Line 52: | Line 55: | ||
** [[KinE]] | ** [[KinE]] | ||
− | * | + | * Phosphotransferases |
** [[Spo0F]] | ** [[Spo0F]] | ||
** [[Spo0B]] | ** [[Spo0B]] | ||
Line 58: | Line 61: | ||
* The ultimate target | * The ultimate target | ||
** [[Spo0A]] | ** [[Spo0A]] | ||
+ | |||
+ | ==Related lists== | ||
+ | * [[phosphorelay]] | ||
+ | * [[response regulator aspartate phosphatases]] | ||
+ | * [[phosphoproteins]] | ||
+ | * [[protein kinases and phosphatases]] | ||
+ | |||
+ | ==Important original publications== | ||
+ | <pubmed>21665979</pubmed> | ||
==Reviews== | ==Reviews== | ||
− | <pubmed>17338439 19575571 11406410 10966457 10932244 | + | <pubmed>17338439 19575571 17158704 17433693 17913492 18832064 19943903 20117042 18076326 20080056 20133181 20133179 21051349 23279101 23352354 22746333 24494032 27519796</pubmed> |
+ | '''Reviews that appeared before 2005''': {{PubMed|11406410,10966457,10932244,10094672,11489844,10745001,1664534}} |
Latest revision as of 08:05, 25 August 2016
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.
Contents
Two-component systems in B. subtilis (kinase, regulator)
- NarL-family
- OmpR family
- Orphan response regulator
The phosphorelay
- The ultimate target
Related lists
- phosphorelay
- response regulator aspartate phosphatases
- phosphoproteins
- protein kinases and phosphatases
Important original publications
Reviews
Christopher P Zschiedrich, Victoria Keidel, Hendrik Szurmant
Molecular Mechanisms of Two-Component Signal Transduction.
J Mol Biol: 2016, 428(19);3752-75
[PubMed:27519796]
[WorldCat.org]
[DOI]
(I p)
Anna I Podgornaia, Michael T Laub
Determinants of specificity in two-component signal transduction.
Curr Opin Microbiol: 2013, 16(2);156-62
[PubMed:23352354]
[WorldCat.org]
[DOI]
(I p)
Hendrik Szurmant, James A Hoch
Statistical analyses of protein sequence alignments identify structures and mechanisms in signal activation of sensor histidine kinases.
Mol Microbiol: 2013, 87(4);707-12
[PubMed:23279101]
[WorldCat.org]
[DOI]
(I p)
Emily J Capra, Michael T Laub
Evolution of two-component signal transduction systems.
Annu Rev Microbiol: 2012, 66;325-47
[PubMed:22746333]
[WorldCat.org]
[DOI]
(I p)
Benjamin G Bobay, James A Hoch, John Cavanagh
Dynamics and activation in response regulators: the β4-α4 loop.
Biomol Concepts: 2012, 3(2);175-182
[PubMed:24494032]
[WorldCat.org]
[DOI]
(I p)
Mohamed Barakat, Philippe Ortet, David E Whitworth
P2CS: a database of prokaryotic two-component systems.
Nucleic Acids Res: 2011, 39(Database issue);D771-6
[PubMed:21051349]
[WorldCat.org]
[DOI]
(I p)
Hendrik Szurmant, James A Hoch
Interaction fidelity in two-component signaling.
Curr Opin Microbiol: 2010, 13(2);190-7
[PubMed:20133181]
[WorldCat.org]
[DOI]
(I p)
Kristin Wuichet, Brian J Cantwell, Igor B Zhulin
Evolution and phyletic distribution of two-component signal transduction systems.
Curr Opin Microbiol: 2010, 13(2);219-25
[PubMed:20133179]
[WorldCat.org]
[DOI]
(I p)
Richard C Stewart
Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.
Curr Opin Microbiol: 2010, 13(2);133-41
[PubMed:20117042]
[WorldCat.org]
[DOI]
(I p)
Rong Gao, Ann M Stock
Molecular strategies for phosphorylation-mediated regulation of response regulator activity.
Curr Opin Microbiol: 2010, 13(2);160-7
[PubMed:20080056]
[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)
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)
Alexander Y Mitrophanov, Eduardo A Groisman
Signal integration in bacterial two-component regulatory systems.
Genes Dev: 2008, 22(19);2601-11
[PubMed:18832064]
[WorldCat.org]
[DOI]
(P p)
Michael T Laub, Mark Goulian
Specificity in two-component signal transduction pathways.
Annu Rev Genet: 2007, 41;121-45
[PubMed:18076326]
[WorldCat.org]
[DOI]
(P p)
Hendrik Szurmant, Robert A White, James A Hoch
Sensor complexes regulating two-component signal transduction.
Curr Opin Struct Biol: 2007, 17(6);706-15
[PubMed:17913492]
[WorldCat.org]
[DOI]
(P p)
Rong Gao, Timothy R Mack, Ann M Stock
Bacterial response regulators: versatile regulatory strategies from common domains.
Trends Biochem Sci: 2007, 32(5);225-34
[PubMed:17433693]
[WorldCat.org]
[DOI]
(P 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)
Reviews that appeared before 2005: PubMed