PnpA
- Description: polynucleotide phosphorylase, RNase
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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU16690
Phenotypes of a mutant
- The pnpA mutant is cold sensitive and sensitive to tetracyclin, it shows multiseptate filamentous growth.
- The mutant is deficient in genetic competence (no expression of the late competence genes)
- The mutant overexpresses the trp and ycgM-ycgN-ycgO operons.
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
Categories containing this gene/protein
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 3'-5' exoribonuclease, RNase, PNPase degrades the trp mRNA from the RNA-TRAP complex
- 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), 3GCM (protein from E. coli, PNPase/RNase E micro-domain/RNA tetragonal crystal form )
- UniProt: P50849
- KEGG entry: [2]
- E.C. number:
Additional information
required for the expression of late competence genes comGA and comK, requirement bypassed by a mecA disruption; may be necessary for modification of the srfAA transcript (stabilization or translation activation)
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP584 (aphA3), available in Stülke lab
- 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
Reviews
A J Carpousis, N F Vanzo, L C Raynal
mRNA degradation. A tale of poly(A) and multiprotein machines.
Trends Genet: 1999, 15(1);24-8
[PubMed:10087930]
[WorldCat.org]
[DOI]
(P p)
Original publications