PnpA

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions: PnpA-RnjA, PnpA-PfkA, PnpA-Rny PubMed

• 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: RelA dependent downregulation (Class I) during stringent response PubMed

• 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

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