Difference between revisions of "CheY"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* not essential for pellicle biofilm formation, but mutant is outcompeted by the wild-type strain when competed during pellicle formation {{PubMed|26122431}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Mutant:'''
 
* '''Mutant:'''
 
** 1A798 ( ''cheY''::''cat''), {{PubMed|1905718}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A798&Search=1A798 BGSC]
 
** 1A798 ( ''cheY''::''cat''), {{PubMed|1905718}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A798&Search=1A798 BGSC]
 +
** DS6870 (marker-less in NCIB3610) {{PubMed|25313396}}
 +
** TB191 ''amyE''::Phy-''sfgfp'' (marker-less in NCIB3610 with constitutive expressed ''sfgfp'') {{PubMed|26122431}}
 +
** TB207 ''amyE''::Phy-''mKATE2'' (marker-less in NCIB3610 with constitutive expressed ''mKATE2'') {{PubMed|26122431}}
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
−
<pubmed>19494578,,10094672 20122866  16224120 </pubmed>
+
<pubmed>25313396, 26122431, 19494578,,10094672 20122866  16224120 </pubmed>
  
 
==Original Publications==
 
==Original Publications==

Revision as of 13:01, 2 July 2015

  • Description: two-component response regulator, modulation of flagellar switch bias

Gene name cheY
Synonyms cheB
Essential no
Product two-component response regulator
Function modulation of flagellar switch bias
Gene expression levels in SubtiExpress: cheY
Interactions involving this protein in SubtInteract: CheY
MW, pI 13 kDa, 4.746
Gene length, protein length 360 bp, 120 aa
Immediate neighbours fliY, fliZ
Sequences Protein DNA DNA_with_flanks
Genetic context
CheY context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CheY expression.png















Categories containing this gene/protein

transcription factors and their control, motility and chemotaxis, phosphoproteins

This gene is a member of the following regulons

CodY regulon, DegU regulon, SigD regulon, Spo0A regulon

The gene

Basic information

  • Locus tag: BSU16330

Phenotypes of a mutant

  • not essential for pellicle biofilm formation, but mutant is outcompeted by the wild-type strain when competed during pellicle formation PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): YneI

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated by CheA on an Asp residue
    • dephosphorylated by CheC PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 1TMY (CheY from Thermotoga maritima)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:
    • in minimal medium, CheY is present with 7,100 +/- 1,000 molecules per cell PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1164 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 2117 PubMed

Biological materials

  • Mutant:
    • 1A798 ( cheY::cat), PubMed, available at BGSC
    • DS6870 (marker-less in NCIB3610) PubMed
    • TB191 amyE::Phy-sfgfp (marker-less in NCIB3610 with constitutive expressed sfgfp) PubMed
    • TB207 amyE::Phy-mKATE2 (marker-less in NCIB3610 with constitutive expressed mKATE2) PubMed
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Theresa Hölscher, Benjamin Bartels, Yu-Cheng Lin, Ramses Gallegos-Monterrosa, Alexa Price-Whelan, Roberto Kolter, Lars E P Dietrich, Ákos T Kovács
Motility, Chemotaxis and Aerotaxis Contribute to Competitiveness during Bacterial Pellicle Biofilm Development.
J Mol Biol: 2015, 427(23);3695-3708
[PubMed:26122431] [WorldCat.org] [DOI] (I p)

Rebecca A Calvo, Daniel B Kearns
FlgM is secreted by the flagellar export apparatus in Bacillus subtilis.
J Bacteriol: 2015, 197(1);81-91
[PubMed:25313396] [WorldCat.org] [DOI] (I p)

Gerald L Hazelbauer, Wing-Cheung Lai
Bacterial chemoreceptors: providing enhanced features to two-component signaling.
Curr Opin Microbiol: 2010, 13(2);124-32
[PubMed:20122866] [WorldCat.org] [DOI] (I p)

Christopher V Rao, George W Ordal
The molecular basis of excitation and adaptation during chemotactic sensory transduction in bacteria.
Contrib Microbiol: 2009, 16;33-64
[PubMed:19494578] [WorldCat.org] [DOI] (P p)

Christopher V Rao, John R Kirby, Adam P Arkin
Phosphatase localization in bacterial chemotaxis: divergent mechanisms, convergent principles.
Phys Biol: 2005, 2(3);148-58
[PubMed:16224120] [WorldCat.org] [DOI] (I e)

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)


Original Publications

Serena Mordini, Cecilia Osera, Simone Marini, Francesco Scavone, Riccardo Bellazzi, Alessandro Galizzi, Cinzia Calvio
The role of SwrA, DegU and P(D3) in fla/che expression in B. subtilis.
PLoS One: 2013, 8(12);e85065
[PubMed:24386445] [WorldCat.org] [DOI] (I e)

Vincent J Cannistraro, George D Glekas, Christopher V Rao, George W Ordal
Cellular stoichiometry of the chemotaxis proteins in Bacillus subtilis.
J Bacteriol: 2011, 193(13);3220-7
[PubMed:21515776] [WorldCat.org] [DOI] (I p)

Y Pazy, M A Motaleb, M T Guarnieri, N W Charon, R Zhao, R E Silversmith
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
Proc Natl Acad Sci U S A: 2010, 107(5);1924-9
[PubMed:20080618] [WorldCat.org] [DOI] (I p)

Travis J Muff, George W Ordal
The CheC phosphatase regulates chemotactic adaptation through CheD.
J Biol Chem: 2007, 282(47);34120-8
[PubMed:17908686] [WorldCat.org] [DOI] (P p)

Kazuo Kobayashi
Gradual activation of the response regulator DegU controls serial expression of genes for flagellum formation and biofilm formation in Bacillus subtilis.
Mol Microbiol: 2007, 66(2);395-409
[PubMed:17850253] [WorldCat.org] [DOI] (P p)

Travis J Muff, Richard M Foster, Peter J Y Liu, George W Ordal
CheX in the three-phosphatase system of bacterial chemotaxis.
J Bacteriol: 2007, 189(19);7007-13
[PubMed:17675386] [WorldCat.org] [DOI] (P p)

H Werhane, P Lopez, M Mendel, M Zimmer, G W Ordal, L M Márquez-Magaña
The last gene of the fla/che operon in Bacillus subtilis, ylxL, is required for maximal sigmaD function.
J Bacteriol: 2004, 186(12);4025-9
[PubMed:15175317] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Travis J Muff, George W Ordal
Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade.
J Biol Chem: 2004, 279(21);21787-92
[PubMed:14749334] [WorldCat.org] [DOI] (P p)

Virginie Molle, Masaya Fujita, Shane T Jensen, Patrick Eichenberger, José E González-Pastor, Jun S Liu, Richard Losick
The Spo0A regulon of Bacillus subtilis.
Mol Microbiol: 2003, 50(5);1683-701
[PubMed:14651647] [WorldCat.org] [DOI] (P p)

Hendrik Szurmant, Michael W Bunn, Vincent J Cannistraro, George W Ordal
Bacillus subtilis hydrolyzes CheY-P at the location of its action, the flagellar switch.
J Biol Chem: 2003, 278(49);48611-6
[PubMed:12920116] [WorldCat.org] [DOI] (P p)

J R Kirby, M M Saulmon, C J Kristich, G W Ordal
CheY-dependent methylation of the asparagine receptor, McpB, during chemotaxis in Bacillus subtilis.
J Biol Chem: 1999, 274(16);11092-100
[PubMed:10196193] [WorldCat.org] [DOI] (P p)

W Estacio, S S Anna-Arriola, M Adedipe, L M Márquez-Magaña
Dual promoters are responsible for transcription initiation of the fla/che operon in Bacillus subtilis.
J Bacteriol: 1998, 180(14);3548-55
[PubMed:9657996] [WorldCat.org] [DOI] (P p)

J R Kirby, C J Kristich, S L Feinberg, G W Ordal
Methanol production during chemotaxis to amino acids in Bacillus subtilis.
Mol Microbiol: 1997, 24(4);869-78
[PubMed:9194713] [WorldCat.org] [DOI] (P p)

L M Márquez-Magaña, M J Chamberlin
Characterization of the sigD transcription unit of Bacillus subtilis.
J Bacteriol: 1994, 176(8);2427-34
[PubMed:8157612] [WorldCat.org] [DOI] (P p)

D S Bischoff, R B Bourret, M L Kirsch, G W Ordal
Purification and characterization of Bacillus subtilis CheY.
Biochemistry: 1993, 32(35);9256-61
[PubMed:8369293] [WorldCat.org] [DOI] (P p)

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