Difference between revisions of "Rph"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ysnA]]'', ''[[gerM]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ysnA]]'', ''[[gerM]]''
 
|-
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28370 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28370 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28370 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28370 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28370 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28370 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:rph_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:rph_context.gif]]

Revision as of 10:55, 14 May 2013

  • Description: RNase PH, 3'-5' exoribonuclease

Gene name rph
Synonyms
Essential no
Product RNase PH (EC 2.7.7.56)
Function 3'-5' exoribonuclease
Gene expression levels in SubtiExpress: rph
MW, pI 26 kDa, 4.888
Gene length, protein length 735 bp, 245 aa
Immediate neighbours ysnA, gerM
Sequences Protein DNA DNA_with_flanks
Genetic context
Rph context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Rph expression.png
























Categories containing this gene/protein

Rnases, translation

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU28370

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • major player in the exonucleolytic maturation of CCA-containing tRNA precursors PubMed
    • responsible for endonucleolytic cleavage of scRNA (scr) PubMed
  • Protein family: RNase PH family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

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

Ciaran Condon, IBPC, Paris, France Homepage

Your additional remarks

References

Yulia Redko, Ciarán Condon
Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-III.
J Bacteriol: 2010, 192(1);356-9
[PubMed:19880604] [WorldCat.org] [DOI] (I p)

Shiyi Yao, Joshua B Blaustein, David H Bechhofer
Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an additional endonuclease cleavage site.
Nucleic Acids Res: 2007, 35(13);4464-73
[PubMed:17576666] [WorldCat.org] [DOI] (I p)

Tingyi Wen, Irina A Oussenko, Olivier Pellegrini, David H Bechhofer, Ciarán Condon
Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis.
Nucleic Acids Res: 2005, 33(11);3636-43
[PubMed:15983136] [WorldCat.org] [DOI] (I e)

Irina A Oussenko, Teppei Abe, Hiromi Ujiie, Akira Muto, David H Bechhofer
Participation of 3'-to-5' exoribonucleases in the turnover of Bacillus subtilis mRNA.
J Bacteriol: 2005, 187(8);2758-67
[PubMed:15805522] [WorldCat.org] [DOI] (P p)

Lene S Harlow, Anders Kadziola, Kaj Frank Jensen, Sine Larsen
Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding.
Protein Sci: 2004, 13(3);668-77
[PubMed:14767080] [WorldCat.org] [DOI] (P p)

M G Craven, D J Henner, D Alessi, A T Schauer, K A Ost, M P Deutscher, D I Friedman
Identification of the rph (RNase PH) gene of Bacillus subtilis: evidence for suppression of cold-sensitive mutations in Escherichia coli.
J Bacteriol: 1992, 174(14);4727-35
[PubMed:1624460] [WorldCat.org] [DOI] (P p)