PMID: 6160038Sep 1, 1980Paper

An endonuclease from yeast mitochondrial fractions

European Journal of Biochemistry
R Morosoli, C V Lusena

Abstract

A membrane-bound endonuclease has been isolated from mitochondrial fractions of Saccharomyces cerevisiae. The enzyme is present in a stable complex and has an approximate molecular weight of 14 000. It requires Mg2+ or Mn2+ for activity, and has an optimum pH of 7.0. Its activity with native DNA is five times less than with denatured DNA in 0.05 M KCl and is very low in 0.2 M KCl. The activity with RNA is 40% of that with denatured DNA; the two substrates are competitive. Its mode of action is endonucleolitic, cuts both strands of native lambda DNA at the same or nearby sites. After mild digestion of DNA, analysis of 5'-end groups of the digestion products indicated a marked preference for deoxythymidylic and deoxyguanilic acid residues as the site of enzymatic cleavage. After exhaustive digestion of DNA, mononucleotides (2.4%), dinucleotides (70.5%) and trinucleotides (27%) ending in 5'-phosphate are produced.

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Citations

Jan 1, 1987·The International Journal of Biochemistry·S A KouidouA C Trakatellis
Mar 30, 2004·Biochemical and Biophysical Research Communications·E S Rangarajan, V Shankar
Apr 17, 2002·Biochimica Et Biophysica Acta·Patrick BouexPatricia Laquel-Robert
Dec 18, 2001·FEMS Microbiology Reviews·E S Rangarajan, V Shankar
Apr 26, 2003·Journal of Industrial Microbiology & Biotechnology·Jian Zhao, Graham H Fleet

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