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Nucleic Acids Research, 1992, Vol. 20, No. 6 1379-1385
© 1992

ENZYMOLOGY

Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster

Ke Shuai+, Chanchal K. Das Gupta, R. Scott Hawley, John W. Chase*, Kathryn L. Stone1 and Kenneth R. Williams1

Department of Molecular Biology and Genetics, Albert Einstein College of Medicine Bronx, New York, NY 10461 1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine New Haven, CT 06520, USA

*To whom correspondence should be addressed at Department of Biochemistry, Case Western Reserve University, School of Medicine, Cleveland, OH 44121, USA

Received October 22, 1991. Revised February 17, 1992. Accepted February 17, 1992.

An endo-exonuclease (designated nuclease III) has been purified to near homogeneity from adult flies of Drosophila melanogaster. The enzyme degrades single-and double-stranded DNA and RNA. It has a sedimentation co-efficient of 3.1S and a stokes radius of 27A The native form of the purified enzyme appears to be a monomer of 33,600 dalton. It has a pH optimum of 7–8.5 and requires Mg2+ or Mn2+ but not Ca2+ or Co2+ for its activity. The enzyme activity on double-stranded DNA was inhibited 50% by 30 mM NaCI, while its activity on single-stranded DNA required 100 mM NaCI for 50% inhibition. Under the latter conditions, its activity on double-stranded DNA was inhibited approximately 98%. The enzyme degrades DNA to complete acid soluble products which are a mixture of mono- and oligonucleotides with 5'-P and 3'-OH termini. Supercoiled DNA was converted by the enzyme to nicked and subsequently to linear forms in a stepwise fashion under the condition in which the enzyme works optimally on single-stranded DNA. The amino acid composition and amino acid sequencing of tryptic peptldes from purified nuclease III is also reported.

+Present address: Laboratory of Molecular and Cellular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021-6399, USA


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