RnjA

• Description: RNase J1
  
  

Gene name	rnjA
Synonyms	ykqC
Essential	yes PubMed
Product	RNase J1
Function	RNA processing
Gene expression levels in SubtiExpress: rnjA
Interactions involving this protein in SubtInteract: RNase J1
Metabolic function and regulation of this protein in SubtiPathways: rnjA
MW, pI	61 kDa, 5.902
Gene length, protein length	1665 bp, 555 aa
Immediate neighbours	adeC, rpoY
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, essential genes

The gene

Basic information

• Locus tag: BSU14530

Phenotypes of a mutant

• essential PubMed
• a study from the lab of Ciaran Condon reports that rnjA is non-essential and that the mutant is strongly impaired in sporulation, genetic competence and many other phenotypes PubMed

Database entries

• BsubCyc: BSU14530

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: endonuclease and 5'-3' exonuclease

• Protein family: RNase J subfamily (according to Swiss-Prot)

• Paralogous protein(s): RnjB

RNAs affected by rnjA

• hbs
• thrS
• yhxA-glpP (in a RppH-dependent manner) PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • part of the RNA degradosome PubMed
  • RnjA-RnjB PubMed
  • RnjA-PfkA PubMed
  • RnjA-PnpA PubMed, K(D) of the interaction: 250 nM PubMed
  • RnjA-Rny PubMed
  • RnjA-CshA PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU14530

• Structure: 3ZQ4 PubMed

• UniProt: Q45493

• KEGG entry: [2]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed
• required for thrS RNA processing, involved in maturation of the 5’-end of the16S rRNA

Expression and regulation

• Operon: ykzG-rnjA PubMed

• Expression browser: rnjA PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • translation of YkzG and RnjA is coupled, and this coupling is required for efficient expression of RNase J1 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2868 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 4928 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2768 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4125 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5056 PubMed

Biological materials

• Mutant:
  • GP41 (rnjA under control of p(xyl)), available in Jörg Stülke's lab
  • SSB342 (rnjA under pspac), cat, available in Harald Putzer lab

• Expression vector:
  • for chromosomal expression of RNase J1-Strep (spc): GP1034, available in Jörg Stülke's lab
  • for chromosomal expression of RNase J1-Strep (cat): GP1042, available in Jörg Stülke's lab

• lacZ fusion: pGP418 (in pAC7), available in Jörg Stülke's lab

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

• FLAG-tag construct:
  • GP1020 (spc, based on pGP1331), available in Jörg Stülke's lab
  • GP1075 (aphA3), available in Jörg Stülke's lab

• Antibody:

Labs working on this gene/protein

Harald Putzer, IBPC Paris, France Homepage

David Bechhofer, Mount Sinai School, New York, USA Homepage

Ciaran Condon, IBPC, Paris, France Homepage

References

Reviews

Soumaya Laalami, Léna Zig, Harald Putzer
Initiation of mRNA decay in bacteria.
Cell Mol Life Sci: 2014, 71(10);1799-828
[PubMed:24064983] [WorldCat.org] [DOI] (I p)

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, David H Bechhofer
Regulated RNA stability in the Gram positives.
Curr Opin Microbiol: 2011, 14(2);148-54
[PubMed:21334965] [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)