Difference between revisions of "RnjA"

From SubtiWiki
Jump to: navigation, search
(Reviews)
(Original publications)
Line 178: Line 178:
  
 
==Original publications==
 
==Original publications==
<pubmed>18079181, 19553197, 17981983, 19458035, 15831787, 18204464, 18713320, 19193632, 17005971, 18445592, 17512403, 17229210, 17576666, 19210617 19633085 19638340 19850915 19880604 20025672 20418391 20572937 ,21803996 21862575 21925382 22198292 22412379 23504012 21893285,21893286,21908660 24187087</pubmed>
+
<pubmed>25940620 18079181, 19553197, 17981983, 19458035, 15831787, 18204464, 18713320, 19193632, 17005971, 18445592, 17512403, 17229210, 17576666, 19210617 19633085 19638340 19850915 19880604 20025672 20418391 20572937 ,21803996 21862575 21925382 22198292 22412379 23504012 21893285,21893286,21908660 24187087</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:17, 14 July 2015

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