RnjB

From SubtiWiki
Revision as of 14:16, 18 November 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
Gene name rnjB
Synonyms ymfA
Essential no
Product RNase J2
Function RNA processing and degradation
Gene expression levels in SubtiExpress: rnjB
Interactions involving this protein in SubtInteract: RNase J2
MW, pI 56 kDa, 9.18
Gene length, protein length 1545 bp, 515 aa
Immediate neighbours dapA, tepA
Sequences Protein DNA DNA_with_flanks
Genetic context
YmfA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RnjB expression.png















Categories containing this gene/protein

Rnases

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU16780

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: endoribonuclease, involved in processing of thrS mRNA
  • Protein family: RNase J subfamily (according to Swiss-Prot)
  • Paralogous protein(s): RnjA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: constitutive expression PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP45 (spc), GP1113 (miniTn10 spc), both available in Stülke lab
  • Expression vector:
  • lacZ fusion: pGP419 (in pAC7), available in Stülke lab
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • FLAG-tag construct: GP1001 (spc, based on pGP1331), available in the Stülke lab
  • Antibody:

Labs working on this gene/protein

Harald Putzer, IBPC Paris, France Homepage

Your additional remarks

References

Reviews

Zbigniew Dominski, Agamemnon J Carpousis, Béatrice Clouet-d'Orval
Emergence of the β-CASP ribonucleases: highly conserved and ubiquitous metallo-enzymes involved in messenger RNA maturation and degradation.
Biochim Biophys Acta: 2013, 1829(6-7);532-51
[PubMed:23403287] [WorldCat.org] [DOI] (P p)

Martin Lehnik-Habrink, Richard J Lewis, Ulrike Mäder, Jörg Stülke
RNA degradation in Bacillus subtilis: an interplay of essential endo- and exoribonucleases.
Mol Microbiol: 2012, 84(6);1005-17
[PubMed:22568516] [WorldCat.org] [DOI] (I p)

David H Bechhofer
Bacillus subtilis mRNA decay: new parts in the toolkit.
Wiley Interdiscip Rev RNA: 2011, 2(3);387-94
[PubMed:21957024] [WorldCat.org] [DOI] (I p)

Jamie Richards, Joel G Belasco
Ribonuclease J: how to lead a double life.
Structure: 2011, 19(9);1201-3
[PubMed:21893280] [WorldCat.org] [DOI] (I p)

Ciarán Condon
What is the role of RNase J in mRNA turnover?
RNA Biol: 2010, 7(3);316-21
[PubMed:20458164] [WorldCat.org] [DOI] (I p)


Original publications