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PMID: 27783 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Hydrolysis of poly (A) to adenine nucleotides by purified poly (A) polymerase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 5 ·1978-05-00 ·Pages 2085-7

Abraham AK, Jacob ST

Abstract

Highly purified poly(A) polymerase (polynucleotide adenylyltransferase, EC 2.7.7.19), which synthesizes poly(A) from ATP substrate, can also catalyze hydrolysis of poly(A). The enzyme, designated as poly(A) hydrolase, requires either Mn2+ or Mg2+ for activity. Although AMP is the predominant product of the reaction, ADP and ATP are also formed. The enzyme is a 3'-exonuclease that does not degrade poly(A) associated with poly(A) poly(U) helical structure. AMP, ADP, and ATP inhibit the hydrolytic reaction. These data suggest that (i) the levels of adenine nucleotides regulate synthesis and degradation of poly(A), (ii) poly(A) itself is a storage form of adenine nucleotides, (iii) the hydrolytic reaction is responsible for poly(A) shortening or turnover observed in vivo, and (iv) the synthetic and hydrolytic activities are functions of the same protein molecule.

MeSH Terms
Adenine Nucleotides/pharmacology Cations, Divalent/pharmacology Exonucleases/metabolism Hydrogen-Ion Concentration Hydrolysis Kinetics Nucleotidyltransferases/metabolism Poly A/metabolism Polynucleotide Adenylyltransferase/metabolism Substrate Specificity
Chemicals
Adenine Nucleotides Cations, Divalent Poly A Nucleotidyltransferases Polynucleotide Adenylyltransferase Exonucleases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Abraham A K
Jacob S T
References (16)
16 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.75.5.2085
Published
1978-05-00
Pages
2085-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392495
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.5.2085 PMC Full Text View journal details
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