RnjB

• Description: RNase J2
  
  

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

Categories containing this gene/protein

Rnases

The gene

Basic information

• Locus tag: BSU16780

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:
  • associated to the RNA degradosome PubMed
  • RnjA-RnjB PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 3ZQ4 (RNase J1) PubMed

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: rnjB PubMed

• 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

References

Reviews

Additional reviews: PubMed

Lehnik-Habrink M, Lewis RJ, Mäder U, Stülke J    
RNA degradation in Bacillus subtilis: an interplay of
essential endo- and exoribonucleases. 
Mol Microbiol.: 2012, 84(6) 1005-1017. 
PubMed:22568516

Original publications

Additional publications: PubMed