MISC

1996年4月

Identification of a 55-kDa endonuclease in rat liver mitochondria with nucleolytic properties similar to endonuclease G

BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL
  • S Ikeda
  • ,
  • T Tanaka
  • ,
  • H Hasegawa
  • ,
  • K Ozaki

38
5
開始ページ
1049
終了ページ
1057
記述言語
英語
掲載種別
出版者・発行元
ACADEMIC PRESS AUST

An endonuclease was extracted from intact rat liver mitochondria with 0.4 M NaCl, and partially purified. A zymographic assay in SDS-polyacrylamide gel containing single-stranded DNA revealed that the enzyme has an apparent molecular mass of 55 kDa. it was different from the molecular mass of the major endonuclease of bovine heart mitochondria (a homodimer of a 29-kDa peptide), that was recently shown to be identical to the endonuclease G. The purified 55-kDa enzyme degraded both DNA and RNA, preferring RNA and single-stranded DNA at a weak alkaline pH, required Mg2+ and Mn2+ but not Ca2+ for activity, and was strongly inhibited by monovalent cations. Nicks generated by the enzyme were resealable with T4 DNA ligase, indicating that the enzyme produces 5'-P and 3'-OH ends. The 55-kDa enzyme, like endonuclease G, displayed a strong preference to nick within a (dG)n .(dC)n sequence tract.

Web of Science ® 被引用回数 : 9

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Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1996UK16500021&DestApp=WOS_CPL

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