Difference between revisions of "YjbH"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* increased thermotolerance due to increased stabiliy of [[Spx]] and thus increased expression of ''[[trxA]]'' {{PubMed|24417481}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
+
* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''contains Zn atoms (coordinated by the N-terminal His-rich region) [http://www.ncbi.nlm.nih.gov/sites/entrez/19074380 PubMed]
+
* '''[[Cofactors]]:'''
 +
** contains Zn atoms (coordinated by the N-terminal His-rich region) [http://www.ncbi.nlm.nih.gov/sites/entrez/19074380 PubMed]
  
 
* '''Effectors of protein activity:'''  
 
* '''Effectors of protein activity:'''  
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
'''Additional reviews:''' {{PubMed|23479438,19609260}}
+
<pubmed> 23375660 23479438,19609260</pubmed>
<pubmed> 23375660 </pubmed>
 
 
==Original Publications==
 
==Original Publications==
'''Additional publications:''' {{PubMed|21378193,21947404}}
+
<pubmed>17293416, 19074380 17908206, 20525796 21378193,21947404 24417481</pubmed>
<pubmed>17293416, 19074380 17908206, 20525796 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:33, 16 January 2014

  • Description: adaptor protein for ClpX-ClpP-catalyzed Spx degradation, confers resistance against nitrosating agents

Gene name yjbH
Synonyms
Essential no
Product adaptor protein
Function stimulation of Spx degradation
Gene expression levels in SubtiExpress: yjbH
Interactions involving this protein in SubtInteract: YjbH
MW, pI 31 kDa, 5.206
Gene length, protein length 825 bp, 275 aa
Immediate neighbours yizD, yjbI
Sequences Protein DNA DNA_with_flanks
Genetic context
YjbH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YjbH expression.png















Categories containing this gene/protein

proteolysis, resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate)

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU11550

Phenotypes of a mutant

  • increased thermotolerance due to increased stabiliy of Spx and thus increased expression of trxA PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: adaptor protein for ClpX-ClpP-catalyzed Spx degradation PubMed
  • Protein family: UPF0413 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Cofactors:
    • contains Zn atoms (coordinated by the N-terminal His-rich region) PubMed
  • Effectors of protein activity:
    • Zn atom is released upon treatment with strong oxidants PubMed
    • interaction with YirB inhibits the formation of a complex with Spx PubMed

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Peter Zuber, Oregon Health and Science University, USA Homepage

Claes von Wachenfeldt, Lund University, Sweden Homepage

Your additional remarks

References

Reviews

Original Publications

Stephanie Runde, Noël Molière, Anja Heinz, Etienne Maisonneuve, Armgard Janczikowski, Alexander K W Elsholz, Ulf Gerth, Michael Hecker, Kürşad Turgay
The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis.
Mol Microbiol: 2014, 91(5);1036-52
[PubMed:24417481] [WorldCat.org] [DOI] (I p)

Nadine Göhring, Iris Fedtke, Guoqing Xia, Ana M Jorge, Mariana G Pinho, Ute Bertsche, Andreas Peschel
New role of the disulfide stress effector YjbH in β-lactam susceptibility of Staphylococcus aureus.
Antimicrob Agents Chemother: 2011, 55(12);5452-8
[PubMed:21947404] [WorldCat.org] [DOI] (I p)

Sushma Kommineni, Saurabh K Garg, Chio Mui Chan, Peter Zuber
YjbH-enhanced proteolysis of Spx by ClpXP in Bacillus subtilis is inhibited by the small protein YirB (YuzO).
J Bacteriol: 2011, 193(9);2133-40
[PubMed:21378193] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Saurabh K Garg, Sushma Kommineni, Luke Henslee, Ying Zhang, Peter Zuber
The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of Spx.
J Bacteriol: 2009, 191(4);1268-77
[PubMed:19074380] [WorldCat.org] [DOI] (I p)

Jonas T Larsson, Annika Rogstam, Claes von Wachenfeldt
YjbH is a novel negative effector of the disulphide stress regulator, Spx, in Bacillus subtilis.
Mol Microbiol: 2007, 66(3);669-84
[PubMed:17908206] [WorldCat.org] [DOI] (P p)

Annika Rogstam, Jonas T Larsson, Peter Kjelgaard, Claes von Wachenfeldt
Mechanisms of adaptation to nitrosative stress in Bacillus subtilis.
J Bacteriol: 2007, 189(8);3063-71
[PubMed:17293416] [WorldCat.org] [DOI] (P p)