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

نویسندگان

  • A K Abraham
  • S T Jacob
چکیده

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.

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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 75 5  شماره 

صفحات  -

تاریخ انتشار 1978