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: rpoY-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

Monica P Hui, Patricia L Foley, Joel G Belasco
Messenger RNA degradation in bacterial cells.
Annu Rev Genet: 2014, 48;537-59
[PubMed:25292357] [WorldCat.org] [DOI] (I p)

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)