ポリヌクレオチドホスホリラーゼ
- 関
- polyribonucleotide nucleotidyltransferase
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/01/01 05:35:53」(JST)
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| Polynucleotide Phosphorylase |
Structure of the PNPase trimer from Streptomyces antibioticus. PDB 1e3p.[1]
|
| 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 |
|
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 polyadenylylation in strains of Escherichia coli missing the normal polyadenylylation enzyme.[1]
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[disambiguation needed]. 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[edit]
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 (RCSB PDB PDBe PDBj) |
| RefSeq |
NM_033109 |
| UniProt |
Q8TCS8 |
| Other data |
| Locus |
Chr. 2 p15 |
References[edit]
- ^ 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". Cell Cycle 5 (10): 1080–4. 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[edit]
- Polynucleotide Phosphorylase at the US National Library of Medicine Medical Subject Headings (MeSH)
|
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
|
|
| 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 |
|
|
| Uridylyltransferase |
- Glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
|
|
| Guanylyltransferase |
|
|
| 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
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
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English Journal
- Expression of multiple Bacillus subtilis genes is controlled by decay of slrA mRNA from Rho-dependent 3' ends.
- Liu B1, Kearns DB2, Bechhofer DH3.
- Nucleic acids research.Nucleic Acids Res.2016 Feb 8. pii: gkw069. [Epub ahead of print]
- Timely turnover of RNA is an important element in the control of bacterial gene expression, but relatively few specific targets of RNA turnover regulation are known. Deletion of the Bacillus subtilis pnpA gene, encoding the major 3' exonuclease turnover enzyme, polynucleotide phosphorylase (PNPase),
- PMID 26857544
- Interaction of Bacillus subtilis Polynucleotide Phosphorylase and RNase Y: Structural Mapping and Effect on mRNA Turnover.
- Salvo E1, Alabi S1, Liu B1, Schlessinger A1, Bechhofer DH2.
- The Journal of biological chemistry.J Biol Chem.2016 Jan 21. pii: jbc.M115.711044. [Epub ahead of print]
- Polynucleotide phosphorylase (PNPase), a 3'-to-5' phosphorolytic exoribonuclease, is thought to be the primary enzyme responsible for turnover of Bacillus subtilis mRNA. The role of PNPase in B. subtilis mRNA decay has been analyzed previously by comparison of mRNA profiles in a wild-type strain vs.
- PMID 26797123
- The ribonuclease polynucleotide phosphorylase can interact with small regulatory RNAs in both protective and degradative modes.
- Bandyra KJ1, Sinha D2, Syrjanen J1, Luisi BF1, De Lay NR3.
- RNA (New York, N.Y.).RNA.2016 Jan 12. [Epub ahead of print]
- In all bacterial species examined thus far, small regulatory RNAs (sRNAs) contribute to intricate patterns of dynamic genetic regulation. Many of the actions of these nucleic acids are mediated by well-characterized chaperones such as the Hfq protein, but genetic screens have also recently identifie
- PMID 26759452
Japanese Journal
- Multiple inhibitory factor removal from an Escherichia coli cell extract improves cell-free protein synthesis(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Seki Eiko,Matsuda Natsuko,Kigawa Takanori
- Journal of bioscience and bioengineering 108(1), 30-35, 2009-07-00
- … coli strains were generated by inserting a streptavidin binding peptide (SBP) tag sequence at the 3' termini of the genes encoding polynucleotide phosphorylase (PNPase) and/or Exodeoxyribonuclease V alpha chain (RecD) on the chromosomal DNA. …
- NAID 110007359705
- 早川 浩
- 福岡歯科大学学会雑誌 33(3), 109-117, 2007-09-30
- … coli polynucleotide phosphorylase (Pnp) protein has been identified as being a good candidate for such a role. …
- NAID 110006436917
- Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
Related Links
- Polynucleotide Phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity. That is, it dismantles the RNA chain starting at the 3' end and ...
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- polynucleotide phosphorylase