Difference between revisions of "NsrR"

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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=nsrR_1013411_1013851_-1 nsrR] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=nsrR_1013411_1013851_-1 nsrR] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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<pubmed> 22287527 </pubmed>
 
<pubmed> 22287527 </pubmed>
 
==Other original publications==
 
==Other original publications==
<pubmed>16885456,,17293416,21091510 , </pubmed>
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<pubmed>16885456, 24214949,17293416,21091510 , 19006327</pubmed>
Additional publications: {{PubMed|19006327}}
 
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:57, 26 May 2014

  • Description: nitric oxide-responsive regulator

Gene name nsrR
Synonyms yhdE
Essential no
Product transcriptional repressor
Function repression of ResD-ResE-dependent genes in the absence of nitric oxide (NO)
Gene expression levels in SubtiExpress: nsrR
Metabolic function and regulation of this protein in SubtiPathways:
nsrR
MW, pI 16 kDa, 7.75
Gene length, protein length 438 bp, 146 aa
Immediate neighbours lytF, ygxB
Sequences Protein DNA DNA_with_flanks
Genetic context
YhdE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
NsrR expression.png















Categories containing this gene/protein

transcription factors and their control, resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate)

This gene is a member of the following regulons

The NsrR regulon

The gene

Basic information

  • Locus tag: BSU09380

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): [4Fe-4S] cluster, required for DNA-binding PubMed
  • Effectors of protein activity:
    • nitric oxide (NO) acts as molecular inducer and results in NsrR release from its DNA targets PubMed
    • [4Fe-4S]-NsrR binds around the -35 element of the nasD promoter with much higher affinity than apo-NsrR and binding of [4Fe-4S]-NsrR, but not apo-protein, is sensitive to NO PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 122 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Elisabeth Härtig, Dieter Jahn
Regulation of the anaerobic metabolism in Bacillus subtilis.
Adv Microb Physiol: 2012, 61;195-216
[PubMed:23046954] [WorldCat.org] [DOI] (I p)

The NsrR regulon

Sushma Kommineni, Amrita Lama, Benjamin Popescu, Michiko M Nakano
Global transcriptional control by NsrR in Bacillus subtilis.
J Bacteriol: 2012, 194(7);1679-88
[PubMed:22287527] [WorldCat.org] [DOI] (I p)

Other original publications

Bernadette Henares, Sushma Kommineni, Onuma Chumsakul, Naotake Ogasawara, Shu Ishikawa, Michiko M Nakano
The ResD response regulator, through functional interaction with NsrR and fur, plays three distinct roles in Bacillus subtilis transcriptional control.
J Bacteriol: 2014, 196(2);493-503
[PubMed:24214949] [WorldCat.org] [DOI] (I p)

Sushma Kommineni, Erik Yukl, Takahiro Hayashi, Jacob Delepine, Hao Geng, Pierre Moënne-Loccoz, Michiko M Nakano
Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter.
Mol Microbiol: 2010, 78(5);1280-93
[PubMed:21091510] [WorldCat.org] [DOI] (I p)

Erik T Yukl, Mohamed A Elbaz, Michiko M Nakano, Pierre Moënne-Loccoz
Transcription Factor NsrR from Bacillus subtilis Senses Nitric Oxide with a 4Fe-4S Cluster (†).
Biochemistry: 2008, 47(49);13084-92
[PubMed:19006327] [WorldCat.org] [DOI] (I 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)

Michiko M Nakano, Hao Geng, Shunji Nakano, Kazuo Kobayashi
The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.
J Bacteriol: 2006, 188(16);5878-87
[PubMed:16885456] [WorldCat.org] [DOI] (P p)