NsrR

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

The gene

Basic information

• Locus tag: BSU09380

Database entries

• BsubCyc: BSU09380

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU09380

• Structure:

• UniProt: O07573

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: nsrR PubMed

• Expression browser: nsrR PubMed

• Sigma factor:

• 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:

References

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)

Nicholas P Tucker, Matthew G Hicks, Thomas A Clarke, Jason C Crack, Govind Chandra, Nick E Le Brun, Ray Dixon, Matthew I Hutchings
The transcriptional repressor protein NsrR senses nitric oxide directly via a [2Fe-2S] cluster.
PLoS One: 2008, 3(11);e3623
[PubMed:18989365] [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)