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Nucleic Acids Research, 1989, Vol. 17, No. 11 4047-4060
© 1989

ENZYMOLOGY

Characterization of a novel endonuclease from Crithidia fasciculate

Mary L. Holdsworth, Jane C. Hines and Dan S. Ray*

Molecular Biology Institute and Department of Biology, University of California Los Angeles California 90024, USA

*To whom correspondence should be addressed.

Received March 23, 1989. Revised April 24, 1989. Accepted April 24, 1989.

A new endonuclease activity has been identified in whole cell lysates of the trypanosomatid Crithidia fasciculata. This activity, termed endonuclease A (Endo A), introduces single-strand breaks at highly preferred sites in double stranded DNA substrates Physical analysis of this enzyme indicates that it has a sedimentation coefficent S20 w of 4.9 and a Stokes radius of 59Å and thus, a native molecular weight of 125,000 and a frictional coefficient of 1.8. A monomeric structure is suggested for the enzyme based on the recovery of Endo A activity associated with a polypeptide with a molecular weight of 116,000–120,000, following electrophoresis on sodium dodecyl sulfate polyacrylamide gels. Endo A shows an absolute requirement for Mg2+ or Mn2+ and exhibits activity over a broad pH and temperature range, with optimal conditions for activity at pH 8.0 and 30°C.


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