Difference between revisions of "PnpA"

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<div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
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Revision as of 15:34, 23 March 2009

  • Description: polynucleotide phosphorylase

Gene name pnpA
Synonyms comR
Essential no
Product polynucleotide phosphorylase (PNPase) (EC 2.7.7.8)
Function necessary for competence development
MW, pI 77 kDa, 4.89
Gene length, protein length 2115 bp, 705 aa
Immediate neighbours rpsO, ylxY
Gene sequence (+200bp) Protein sequence
Genetic context
PnpA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 3'-5' exoribonuclease
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 3CDI (protein from E. coli)
  • Swiss prot entry:
  • KEGG entry: [2]
  • E.C. number:

Additional information

required for the expression of late competence genes comG and comK, requirement bypassed by a mecA disruption; may be necessary for modification of the srfA transcript (stabilization or translation activation)

Expression and regulation

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

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

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

Your additional remarks

References

  1. Bechhofer, D. H. & Wang, W. (1998). Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis. J Bacteriol 180:5968-5977. PubMed
  2. Campos-Guillen, J., Bralley, P., Jones, G. H., Bechhofer, D. H. & Olmedo-Alvarez, G. (2005). Addition of poly(A) and heteropolymeric 3´ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains. J Bacteriol 187:4698-4706. PubMed
  3. Deutscher, M. P. & Reuven, N. B. (1991). Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis. Proc Natl Acad Sci U S A 88:3277-3280. PubMed
  4. Mitra, S., Hue, K. & Bechhofer, D. H. (1996). In vitro processing activity of Bacillus subtilis polynucleotide phosphorylase. Mol Microbiol 19:329-342. PubMed
  5. Wang, W. & Bechhofer, D. H. (1996). Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain. J Bacteriol 178:2375-2382. PubMed
  6. Oussenko, I. A., Abe, T., Ujiie, H., Muto, A. & Bechhofer, D. H. (2005). Participation of 3'-to-5' exoribonucleases in the turnover of Bacillus subtilis mRNA. J Bacteriol 187:2758-2767. PubMed
  7. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press PubMed
  8. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed