・リリボヌクレオチドヌクレオチジルトランスフェラーゼ
- 関
- polynucleotide phosphorylase
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/26 00:14:30」(JST)
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| Polynucleotide Phosphorylase |
|
Structure of the PNPase trimer from Streptomyces antibioticus. PDB 1e3p.[1]
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| Identifiers |
| EC number |
2.7.7.8 |
| CAS number |
9014-12-4 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
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Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity.[2] That is, it dismantles the RNA chain starting at the 3' end and working toward the 5' end.[1] It also synthesizes long, highly heteropolymeric tails in vivo. It accounts for all of the observed residual polyadenylation in strains of Escherichia coli missing the normal polyadenylation enzyme.[1] Discovered by Ochoa in 1951, the RNA-polymerization activity of PNPase was initially believed to be responsible for DNA-dependent synthesis of messenger RNA, a notion that got disproved by the late 1950s (http://www.jbc.org/content/281/15/e12.full.pdf).
It is involved on mRNA processing and degradation in bacteria, plants,[3] and in humans.[4]
In humans, the enzyme is encoded by the PNPT1 gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two RNase PH domains, an S1 RNA binding domain and a K-homology domain. The protein is present in bacteria and in the chloroplasts[2] and mitochondria[5] of some eukaryotic cells. In eukaryotes and archaea, a structurally and evolutionary related complex exists, called the exosome.[5]
The same abbreviation (PNPase) is also used for another, otherwise unrelated enzyme, Purine nucleoside phosphorylase.
Model organisms
Pnpt1 knockout mouse phenotype
| Characteristic |
Phenotype |
| Homozygote viability |
Abnormal |
| Recessive lethal study |
Abnormal |
| Fertility |
Normal |
| Body weight |
Normal |
| Anxiety |
Normal |
| Neurological assessment |
Normal |
| Grip strength |
Normal |
| Hot plate |
Normal |
| Dysmorphology |
Normal |
| Indirect calorimetry |
Normal |
| Glucose tolerance test |
Normal |
| Auditory brainstem response |
Normal |
| DEXA |
Normal |
| Radiography |
Normal |
| Body temperature |
Normal |
| Eye morphology |
Normal |
| Clinical chemistry |
Normal |
| Plasma immunoglobulins |
Normal |
| Haematology |
Normal |
| Peripheral blood lymphocytes |
Normal |
| Micronucleus test |
Normal |
| Heart weight |
Normal |
| Skin Histopathology |
Normal |
| Brain histopathology |
Normal |
| Salmonella infection |
Normal[6] |
| Citrobacter infection |
Normal[7] |
| All tests and analysis from[8][9] |
Model organisms have been used in the study of PNPT1 function. A conditional knockout mouse line, called Pnpt1tm1a(KOMP)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[12][13][14]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty six tests were carried out on mutant mice and two significant abnormalities were observed.[8] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.[8]
| Human PNPase I |
| Identifiers |
| Symbol |
PNPASE |
| Alt. symbols |
PNPase, OLD35, old-35 |
| Entrez |
87178 |
| HUGO |
23166 |
| OMIM |
610316 |
| PDB |
1E3P |
| RefSeq |
NM_033109 |
| UniProt |
Q8TCS8 |
| Other data |
| EC number |
2.7.7.8 |
| Locus |
Chr. 2 p15 |
References
- ^ a b c Symmons MF, Jones GH, Luisi BF (November 2000). "A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation". Structure 8 (11): 1215–26. doi:10.1016/S0969-2126(00)00521-9. PMID 11080643.
- ^ a b Yehudai-Resheff S, Hirsh M, Schuster G (August 2001). "Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts". Mol. Cell. Biol. 21 (16): 5408–16. doi:10.1128/MCB.21.16.5408-5416.2001. PMC 87263. PMID 11463823.
- ^ Yehudai-Resheff S, Zimmer SL, Komine Y, Stern DB (March 2007). "Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii". Plant Cell 19 (3): 1023–38. doi:10.1105/tpc.106.045427. PMC 1867357. PMID 17351118.
- ^ Sarkar D, Fisher PB (May 2006). "Human polynucleotide phosphorylase (hPNPase old-35): an RNA degradation enzyme with pleiotrophic biological effects" (PDF). Cell Cycle 5 (10): 1080–4. doi:10.4161/cc.5.10.2741. PMID 16687933.
- ^ a b Schilders G, van Dijk E, Raijmakers R, Pruijn GJ (2006). "Cell and molecular biology of the exosome: how to make or break an RNA". Int. Rev. Cytol. 251: 159–208. doi:10.1016/S0074-7696(06)51005-8. PMID 16939780.
- ^ "Salmonella infection data for Pnpt1". Wellcome Trust Sanger Institute.
- ^ "Citrobacter infection data for Pnpt1". Wellcome Trust Sanger Institute.
- ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium".
- ^ "Mouse Genome Informatics".
- ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
External links
- Polynucleotide Phosphorylase at the US National Library of Medicine Medical Subject Headings (MeSH)
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Transferases: phosphorus-containing groups (EC 2.7)
|
|
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
| 2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- Thymidine
- NAD+
- Glycerol
- Pantothenate
- Mevalonate
- Pyruvate
- Deoxycytidine
- PFP
- Diacylglycerol
- Phosphoinositide 3
- Class I PI 3
- Class II PI 3
- Sphingosine
- Glucose-1,6-bisphosphate synthase
|
|
| 2.7.2: COOH acceptor |
- Phosphoglycerate
- Aspartate kinase
|
|
| 2.7.3: N acceptor |
|
|
| 2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
|
|
|
2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
|
|
2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
| Polymerase |
| DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
|
|
| RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
|
|
|
Phosphorolytic
3' to 5' exoribonuclease |
|
|
| Nucleotidyltransferase |
- UTP—glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
|
|
| Guanylyltransferase |
|
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| Other |
- Recombinase (Integrase)
- Transposase
|
|
|
| 2.7.8: miscellaneous |
| Phosphatidyltransferases |
- CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
- CDP-diacylglycerol—serine O-phosphatidyltransferase
- CDP-diacylglycerol—inositol 3-phosphatidyltransferase
- CDP-diacylglycerol—choline O-phosphatidyltransferase
|
|
| Glycosyl-1-phosphotransferase |
- N-acetylglucosamine-1-phosphate transferase
|
|
|
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor) |
| 2.7.10: protein-tyrosine |
|
|
| 2.7.11: protein-serine/threonine |
- see serine/threonine-specific protein kinases
|
|
| 2.7.12: protein-dual-specificity |
- see serine/threonine-specific protein kinases
|
|
| 2.7.13: protein-histidine |
- Protein-histidine pros-kinase
- Protein-histidine tele-kinase
- Histidine kinase
|
|
|
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Proteins: enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
UpToDate Contents
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English Journal
- CsrA Participates in a PNPase Autoregulatory Mechanism by Selectively Repressing Translation of pnp Transcripts That Have Been Previously Processed by RNase III and PNPase.
- Park H1, Yakhnin H1, Connolly M1, Romeo T2, Babitzke P3.
- Journal of bacteriology.J Bacteriol.2015 Dec;197(24):3751-9. doi: 10.1128/JB.00721-15. Epub 2015 Oct 5.
- Csr is a conserved global regulatory system that represses or activates gene expression posttranscriptionally. CsrA of Escherichia coli is a homodimeric RNA binding protein that regulates transcription elongation, translation initiation, and mRNA stability by binding to the 5' untranslated leader or
- PMID 26438818
- Airpnp: Auto- and Integrated Regulation of Polynucleotide Phosphorylase.
- Condon C1.
- Journal of bacteriology.J Bacteriol.2015 Dec;197(24):3748-50. doi: 10.1128/JB.00794-15. Epub 2015 Oct 5.
- The properties and expression of polynucleotide phosphorylase (PNPase), capable of both RNA degradation and polymerization, have been studied for 60 years. In this issue of the Journal of Bacteriology, Park et al. (H. Park, H. Yakhnin, M. Connolly, T. Romeo, and P. Babitzke, J Bacteriol 197:3751-375
- PMID 26438817
- SUV3 helicase is required for correct processing of mitochondrial transcripts.
- Clemente P1, Pajak A1, Laine I1, Wibom R2, Wedell A3, Freyer C4, Wredenberg A4.
- Nucleic acids research.Nucleic Acids Res.2015 Sep 3;43(15):7398-413. doi: 10.1093/nar/gkv692. Epub 2015 Jul 7.
- Mitochondrial gene expression is largely regulated by post-transcriptional mechanisms that control the amount and translation of each mitochondrial mRNA. Despite its importance for mitochondrial function, the mechanisms and proteins involved in mRNA turnover are still not fully characterized. Studie
- PMID 26152302
Related Links
- Polyribonucleotide nucleotidyltransferase Gene pnp Organism Escherichia coli (strain K12) Status Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein level i Function i Involved in mRNA , ] [] ] ...
- RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA ...
Related Pictures
★リンクテーブル★
[★]
- 英
- polyribonucleotide nucleotidyltransferase
- 関
- ・リヌクレオチドホスホリラーゼ
[★]
ポリヌクレオチドホスホリラーゼ
- 関
- polyribonucleotide nucleotidyltransferase
[★]
ヌクレオチジルトランスフェラーゼ、ヌクレオチド転移酵素、ヌクレオチジル転移酵素
- 関
- terminal deoxynucleotide transferase
[★]