Difference between revisions of "RnjA"

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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1665 bp, 555 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1665 bp, 555 aa  
 
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[adeC]]'', ''[[ykzG]]''
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[adeC]]'', ''[[rpoY]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU14530 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU14530 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU14530 DNA_with_flanks]
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU14530 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU14530 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU14530 DNA_with_flanks]
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=== Additional information===
 
=== Additional information===
 
 
  
  

Revision as of 11:19, 6 August 2014

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
YkqC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RnjA expression.png















Categories containing this gene/protein

Rnases, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU14530

Phenotypes of a mutant

Database entries

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

Additional information

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

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

  • 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

  • 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
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), 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

Your additional remarks

References

Reviews


Original publications