Difference between revisions of "SlrR"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 125: Line 125:
 
** induction by sequestration of [[SinR]] by [[SinI]],  [[SlrA]] {{PubMed|15661000,19788541}} or by SlrR itself {{PubMed|20351052}}
 
** induction by sequestration of [[SinR]] by [[SinI]],  [[SlrA]] {{PubMed|15661000,19788541}} or by SlrR itself {{PubMed|20351052}}
 
** the ''[[slrR]]'' gene is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}}  
 
** the ''[[slrR]]'' gene is not expressed in a ''[[ymdB]]'' mutant {{PubMed|21856853}}  
 +
** the amount of the mRNA is substantially decreased upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
  
 
=Biological materials =
 
=Biological materials =
  
 
* '''Mutant:'''
 
* '''Mutant:'''
** GP955 (''slrR''-''[[pnbA]]''::''cat''), available in [[Stülke]] lab   
+
** GP955 (''slrR''-''[[pnbA]]''::''cat''), available in [[Jörg Stülke]]'s lab   
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''
Line 150: Line 151:
 
==Original publications==
 
==Original publications==
 
'''Additional publications:''' {{PubMed|20817675}}  
 
'''Additional publications:''' {{PubMed|20817675}}  
 +
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
 +
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
 +
<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 +
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 +
 
  <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J''  </big>
 
  <big>''Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J''  </big>
 
  <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big>
 
  <big>'''A Novel Factor Controlling Bistability in ''Bacillus subtilis'': The YmdB Protein Affects</big>

Revision as of 20:07, 19 November 2011

  • Description: transcriptional activator of competence development and sporulation genes, represses SigD-dependent flagellar genes, antagonist of SlrA and SinR, has LexA-like autocleavage activity

Gene name slrR
Synonyms yveJ, slr
Essential no
Product transcription regulator, SlrA antagonist
Function regulation of initiation of biofilm formation and of autolysis
Interactions involving this protein in SubtInteract: SlrR
Regulation of this protein in SubtiPathways:
Biofilm
MW, pI 17 kDa, 9.63
Gene length, protein length 456 bp, 152 aa
Immediate neighbours epsA, pnbA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Slr context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

transcription factors and their control, transition state regulators, biofilm formation

This gene is a member of the following regulons

Abh regulon, AbrB regulon, SinR regulon

The SlrR regulon:

The gene

Basic information

  • Locus tag: BSU34380

Phenotypes of a mutant

Database entries

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

Additional information

  • overexpression of slrR suppresses the phenotype of a ymdB mutant PubMed

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • SlrR binds to and inhibits the activity of SlrA, SlrA indirectly stimulates the synthesis of SlrR by interacting with SinR. SlrR can bind to SinR and SinR directly represses the transcription of SlrR. SlrR indirectly derepresses its own gene. The heterocomplex of SlrR-SinR is a repressor of autolysin and motility genes and inhibits the repressor function of SinR. PubMed
    • repression of transcription of lytA-lytB-lytC and lytF PubMed
    • autocleavage PubMed
  • Protein family:
  • Paralogous protein(s): SinR

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • subject to self-cleavage via a LexA-like autopeptidase, this involves ClpC PubMed
  • Cofactor(s):
  • Effectors of protein activity: interaction with SinR triggers binding of SlrR to the promoters of lytA-lytB-lytC and lytF, resulting in their repression PubMed

Database entries

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

Additional information

Expression and regulation

  • Operon:
  • Regulation:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Patrick Piggot
Epigenetic switching: bacteria hedge bets about staying or moving.
Curr Biol: 2010, 20(11);R480-2
[PubMed:20541494] [WorldCat.org] [DOI] (I p)

Original publications

Additional publications: PubMed

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947
Diethmaier C, Pietack N, Gunka K, Wrede C, Lehnik-Habrink M, Herzberg C, Hübner S, Stülke J  
A Novel Factor Controlling Bistability in Bacillus subtilis: The YmdB Protein Affects
Flagellin Expression and Biofilm Formation. 
J Bacteriol.: 2011, 193(21):5997-6007. 
PubMed:21856853