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ECOLI:PNP
Contents |
| Species (Taxon ID) | Escherichia coli (strain K12). ([1]) | |
| Gene Name(s) | pnp | |
| Protein Name(s) | Polyribonucleotide nucleotidyltransferase
Polynucleotide phosphorylase PNPase | |
| External Links | ||
| EMBL | J02638 U18997 U00096 AP009048 X00761 M14425 | |
| PIR | H65106 | |
| RefSeq | NP_417633.4 | |
| PDB | 1SRO 3CDI 3CDJ 3H1C | |
| PDBsum | 1SRO 3CDI 3CDJ 3H1C | |
| ProteinModelPortal | P05055 | |
| SMR | P05055 | |
| DIP | DIP-10522N | |
| IntAct | P05055 | |
| MINT | MINT-244786 | |
| PhosSite | P05055 | |
| SWISS-2DPAGE | P05055 | |
| ECO2DBASE | C078.0 | |
| PRIDE | P05055 | |
| EnsemblBacteria | EBESCT00000002007 EBESCT00000002008 EBESCT00000002009 EBESCT00000002010 EBESCT00000015515 | |
| GeneID | 947672 | |
| GenomeReviews | AP009048_GR U00096_GR | |
| KEGG | ecj:JW5851 eco:b3164 | |
| EchoBASE | EB0736 | |
| EcoGene | EG10743 | |
| eggNOG | COG1185 | |
| GeneTree | EBGT00050000009530 | |
| HOGENOM | HBG382411 | |
| OMA | YGETVVL | |
| ProtClustDB | PRK11824 | |
| BioCyc | EcoCyc:EG10743-MONOMER MetaCyc:EG10743-MONOMER | |
| BRENDA | 2.7.7.8 | |
| Genevestigator | P05055 | |
| GO | GO:0005829 GO:0016020 GO:0000175 GO:0004654 GO:0003723 GO:0006402 GO:0006950 GO:0006396 | |
| HAMAP | MF_01595 | |
| InterPro | IPR001247 IPR015847 IPR004087 IPR009019 IPR004088 IPR018111 IPR012340 IPR016027 IPR012162 IPR015848 IPR003029 IPR020568 IPR022967 | |
| Gene3D | G3DSA:2.40.50.140 G3DSA:1.10.10.400 | |
| PANTHER | PTHR11252 | |
| Pfam | PF00013 PF03726 PF01138 PF03725 PF00575 | |
| PIRSF | PIRSF005499 | |
| SMART | SM00322 SM00316 | |
| SUPFAM | SSF46915 SSF55666 SSF54814 SSF50249 SSF54211 | |
| TIGRFAMs | TIGR03591 | |
| PROSITE | PS50084 PS50126 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0000175 |
3'-5'-exoribonuclease activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0003723 |
RNA binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0004654 |
polyribonucleotide nucleotidyltransferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
C |
Seeded From UniProt |
||||
| GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-0086 |
C |
Seeded From UniProt |
|||
| GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
|
C |
Seeded From UniProt |
|||
| GO:0006396 |
RNA processing |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006396 |
RNA processing |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006402 |
mRNA catabolic process |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0006950 |
response to stress |
IEA: Inferred from Electronic Annotation |
P |
Seeded From UniProt |
||||
| GO:0016020 |
membrane |
IDA: Inferred from Direct Assay |
|
C |
Seeded From UniProt |
|||
| GO:0016740 |
transferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0016779 |
nucleotidyltransferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded From UniProt |
||||
| GO:0042802 |
identical protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded From UniProt |
||||
| GO:0006402 |
mRNA catabolic process |
IMP: Inferred from Mutant Phenotype |
P |
Fig. 2 and Fig. 3 |
complete | |||
| GO:0006402 |
mRNA catabolic process |
IMP: Inferred from Mutant Phenotype |
P |
As shown in Table 2, RNase II and PNPase were used in a pulse-chase to measure the half-life of the radioactive labeled mRNA. RNase II was a mutant strain that would grow at 44 degrees Celsius. First, the mRNA and the RNase II/PNPase were incubated at 30 degrees Celsius then shifted to 44 degrees Celsius. At 44 degrees Celsius PNPase cannot function, but RNase II is still able to function. The table shows that there was a decrease in the degradation of mRNA when the temperature was raised to 44 degrees Celsius which corresponds to a loss of PNPase function. These results demonstrate that PNPase is important to the catabolic process of mRNA. |
complete | |||
| edit table |
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Callaghan AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J Mol Biol 340: 965-79 PubMed GONUTS page
- ↑ 2.0 2.1 Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed GONUTS page
- ↑ Yamanaka K & Inouye M (2001) Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coli. J Bacteriol 183: 2808-16 PubMed GONUTS page
- ↑ Donovan WP & Kushner SR (1986) Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc Natl Acad Sci U S A 83: 120-4 PubMed GONUTS page
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m cont.npr |
r cont.t |
