Polynucleotide adenylyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a polynucleotide adenylyltransferase (EC 2.7.7.19) is an enzyme that catalyzes the chemical reaction

ATP + RNAn $\rightleftharpoons$ diphosphate + RNAn⁺1

Thus, the two substrates of this enzyme are ATP and RNA, whereas its two products are diphosphate and RNA with an extra adenosine nucleotide at its 3' end.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:polynucleotide adenylyltransferase. Other names in common use include NTP polymerase, RNA adenylating enzyme, AMP polynucleotidylexotransferase, ATP-polynucleotide adenylyltransferase, ATP:polynucleotidylexotransferase, poly(A) polymerase, poly(A) synthetase, polyadenylate nucleotidyltransferase, polyadenylate polymerase, polyadenylate synthetase, polyadenylic acid polymerase, polyadenylic polymerase, terminal riboadenylate transferase, poly(A) hydrolase, RNA formation factors, PF1, and adenosine triphosphate:ribonucleic acid adenylyltransferase.

1 Function
2 Structural studies
3 References
4 External links
- 4.1 Gene Ontology (GO) codes

[edit] Function

This enzyme is responsible for the addition of the 3' polyadenine tail to a newly synthesized pre-messenger RNA (pre-mRNA) molecule during the process of gene transcription. The protein is the final addition to a large protein complex that also contains smaller assemblies known as the cleavage and polyadenylation specificity factor (CPSF) and cleavage stimulatory factor (CtSF) and its binding is a necessary prerequisite to the cleavage of the 3' end of the pre-mRNA. After cleavage of the 3' signaling region that directs the assembly of the complex, PAP adds the polyadenine tail to the new 3' end.

The rate at which PAP adds adenine nucleotides is dependent on the presence of another regulatory protein, PABPII (poly-adenine binding protein II). The first few nucleotides added by PAP are added very slowly, but the short polyadenine tail is then bound by PABPII, which accelerates the rate of adenine addition by PAP. The final tail is about 200-250 adenine nucleotides long.

PAP is phosphorylated by mitosis-promoting factor, a key regulator of the cell cycle. High phosphorylation levels decrease PAP activity.

[edit] Structural studies

As of late 2007, 27 structures have been solved for this class of enzymes, with PDB accession codes 1AV6, 1B42, 1BKY, 1EAM, 1EQA, 1F5A, 1FA0, 1JSZ, 1JTE, 1JTF, 1P39, 1Q78, 1Q79, 1V39, 1VFG, 1VP3, 1VP9, 1VPT, 2GA9, 2GAF, 2HHP, 2O1P, 2Q66, 2VP3, 3MAG, 3MCT, and 4DCG.

[edit] References

IUBMB entry for 2.7.7.19
BRENDA references for 2.7.7.19 (Recommended.)
PubMed references for 2.7.7.19
PubMed Central references for 2.7.7.19
Google Scholar references for 2.7.7.19
AUGUST JT, ORTIZ PJ, HURWITZ J (1962). "Ribonucleic acid-dependent ribonucleotide incorporation. I Purification and properties of the enzyme". J. Biol. Chem. 237: 3786–93. PMID 13965521.
Edmonds M and Abrams R (1960). "Polynucleotide biosynthesis: formation of a sequence of adenylate units from adenosine triphosphate by an enzyme from thymus nuclei". J. Biol. Chem. 235: 1142–1149.
Gottesman ME, Canellakis ES (1966). "The terminal nucleotidyltransferases of calf thymus nuclei". J. Biol. Chem. 241: 4339–52. PMID 4288534.
KRAKOW JS, COUTSOGEORGOPOULOS C, CANELLAKIS ES (1962). "Studies on the incorporation of deoxyribonucleic acid". Biochim. Biophys. Acta. 55: 639–50. doi:10.1016/0006-3002(62)90842-9. PMID 14459258.
Mans RJ, Walter TJ (1971). "Transfer RNA-primed oligoadenylate synthesis in maize seedlings. II Primer, substrate and metal specificities and size of product". Biochim. Biophys. Acta. 247: 113–21. PMID 4946277.
Sheldon R, Jurale C, Kates J (1972). "Detection of polyadenylic acid sequences in viral and eukaryotic RNA(polu(U)-cellulose columns-poly(U) filters-fiberglass-HeLa cells-bacteriophage T4)". Proc. Natl. Acad. Sci. U. S. A. 69: 417–21. PMID 4501121.
Lodish H, Berk A, Matsudaira P, Kaiser CA, Krieger M, Scott MP, Zipursky SL, Darnell J. (2004). Molecular Cell Biology. WH Freeman: New York, NY. 5th ed.
Colgan DF, Murthy KG, Prives C, Manley JL. (1996). Cell-cycle related regulation of poly(A) polymerase by phosphorylation. Nature 384(6606):282-5.