Polynucleotide adenylyltransferase
(Redirected from
Polyadenylate polymerase
)polynucleotide adenylyltransferase | |||||||||
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Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In
enzymology, a polynucleotide adenylyltransferase (EC 2.7.7.19) is an enzyme that catalyzes the chemical reaction
- ATP + RNA-3'OH pyrophosphate + RNApA-3'OH
Thus, the two
substrates of this enzyme are ATP and RNA, whereas its two products are pyrophosphate and RNA with an extra adenosine
nucleotide at its 3' end.
Human genes with this activity include TUT1, MTPAP, PAPOLA, PAPOLB, PAPOLG, TENT2, TENT4A, TENT4B, TENT5C, TENT5D.
Function
This enzyme is responsible for the addition of the
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, polyadenylate polymerase (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 in mammals.
PAP is
mitosis-promoting factor, a key regulator of the cell cycle
. High phosphorylation levels decrease PAP activity.
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
.
References
- August JT, Ortiz PJ, Hurwitz J (December 1962). "Ribonucleic acid-dependent ribonucleotide incorporation. I. Purification and properties of the enzyme". J. Biol. Chem. 237 (12): 3786–93. PMID 13965521.
- .
- Gottesman ME, Canellakis ES (1966). "The terminal nucleotidyltransferases of calf thymus nuclei". J. Biol. Chem. 241 (19): 4339–52. PMID 4288534.
- Krakow Js; Coutsogeorgopoulos C; Canellakis ES (1962). "Studies on the incorporation of deoxyribonucleic acid". Biochim. Biophys. Acta. 55 (5): 639–50. 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 (1): 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 (2): 417–21. PMID 4501121.
- Colgan DF, Murthy KG, Prives C, Manley JL (November 1996). "Cell-cycle related regulation of poly(A) polymerase by phosphorylation". Nature. 384 (6606): 282–5. S2CID 4304275.