RnjB

From SubtiWiki
Revision as of 18:46, 13 September 2011 by Jstuelk (talk | contribs) (Reviews)
Jump to: navigation, search
Gene name rnjB
Synonyms ymfA
Essential no
Product RNase J2
Function RNA processing and degradation
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
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YmfA context.gif
This image was kindly provided by SubtiList





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

  • Structure: 3BK1 (RNase J from Thermus thermophilus) 3BK2 (RNase J from Thermus thermophilus, complex with UMP)
  • UniProt: O31760
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • 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


Original publications

Gintaras Deikus, David H Bechhofer
5' End-independent RNase J1 endonuclease cleavage of Bacillus subtilis model RNA.
J Biol Chem: 2011, 286(40);34932-40
[PubMed:21862575] [WorldCat.org] [DOI] (I p)

Nathalie Mathy, Agnès Hébert, Peggy Mervelet, Lionel Bénard, Audrey Dorléans, Inés Li de la Sierra-Gallay, Philippe Noirot, Harald Putzer, Ciarán Condon
Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour.
Mol Microbiol: 2010, 75(2);489-98
[PubMed:20025672] [WorldCat.org] [DOI] (I p)

Shiyi Yao, David H Bechhofer
Processing and stability of inducibly expressed rpsO mRNA derivatives in Bacillus subtilis.
J Bacteriol: 2009, 191(18);5680-9
[PubMed:19633085] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632] [WorldCat.org] [DOI] (I p)

Ulrike Mäder, Léna Zig, Julia Kretschmer, Georg Homuth, Harald Putzer
mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene expression on a global scale.
Mol Microbiol: 2008, 70(1);183-96
[PubMed:18713320] [WorldCat.org] [DOI] (I p)

Inés Li de la Sierra-Gallay, Léna Zig, Ailar Jamalli, Harald Putzer
Structural insights into the dual activity of RNase J.
Nat Struct Mol Biol: 2008, 15(2);206-12
[PubMed:18204464] [WorldCat.org] [DOI] (I p)

Sergine Even, Olivier Pellegrini, Lena Zig, Valerie Labas, Joelle Vinh, Dominique Bréchemmier-Baey, Harald Putzer
Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E.
Nucleic Acids Res: 2005, 33(7);2141-52
[PubMed:15831787] [WorldCat.org] [DOI] (I e)