RNA-dependent ATPase from Saccharomyces cerevisiae [Yeasts]

A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence of Mg2+ or Mn2+ ions and requires a single-strand...

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Bibliographic Details
Published in:The Journal of biological chemistry 1980-12, Vol.255 (24), p.11704-11709
Main Authors: Belhadj, O, Sentenac, A, Fromageot, P
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - isolation & purification
Adenosine Triphosphatases - metabolism
Chromatin - enzymology
DNA, Single-Stranded
Kinetics
Molecular Weight
Polynucleotides - pharmacology
Saccharomyces cerevisiae - enzymology
Structure-Activity Relationship
Substrate Specificity
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Summary:A new RNA-dependent ATPase has been isolated from yeast chromatin extracts and partially characterized. The protein has a sedimentation coefficient of about 7 S. The enzyme hydrolyzes specifically ATP (or dATP) to ADP (or dADP) and Pi in the presence of Mg2+ or Mn2+ ions and requires a single-stranded polynucleotide as cofactor. The order of efficiency of synthetic polymers is poly(rU) > poly(rI) greater than or equal to poly(dU) > poly(rA) greater than or equal to poly(rC). Among natural polymers, single-stranded DNA and poly(rA)-containing mRNA from yeast are also active but less so than poly(rU). The enzyme exhibits a pH optimum of 8 and is fully inhibited by 0.25 M NaCl. The Km for ATP is0.2 mM. The resemblance between this ATPase and DNA-dependent ATPases from other sources, as well as the termination factor rho, is discussed.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)70190-2