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J Biol Chem, Vol. 275, Issue 11, 8226-8232, March 17, 2000
From the Departments of Here we report the co-factor requirements for DNA
fragmentation factor (DFF) endonuclease and characterize its cleavage
sites on naked DNA and chromatin substrates. The endonuclease exhibits a pH optimum of 7.5, requires Mg2+, not
Ca2+, and is inhibited by Zn2+. The enzyme
generates blunt ends or ends with 1-base 5'-overhangs possessing
5'-phosphate and 3'-hydroxyl groups and is specific for double- and not
single-stranded DNA or RNA. DFF endonuclease has a moderately greater
sequence preference than micrococcal nuclease or DNase I, and the sites
attacked possess a dyad axis of symmetry with respect to purine and
pyrimidine content. Using HeLa cell nuclei or chromatin reconstituted
on a 5 S rRNA gene tandem array, we prove that the enzyme attacks
chromatin in the internucleosomal linker, generating oligonucleosomal
DNA ladders sharper than those created by micrococcal nuclease.
Histone H1, high mobility group-1, and topoisomerase II activate
DFF endonuclease activity on naked DNA substrates but much less so on
chromatin substrates. We conclude that DFF is a useful reagent for
chromatin research.
Cleavage Preferences of the Apoptotic Endonuclease DFF40
(Caspase-activated DNase or Nuclease) on Naked DNA and Chromatin
Substrates*
§,
**, and
Molecular Biology and
Biochemistry and the ** Howard Hughes Medical Institute,
University of Texas Southwestern Medical Center,
Dallas, Texas 75235
*
This work was supported in part by the Polish State
Committee for Scientific Research Grant 6P04A01317 (to P. W.),
American Cancer Society Grant RE258, National Institutes of Health
Grant GMRO1-55942, Robert A. Welch Foundation Grant I-1412 (to
X. W.), National Institutes of Health Grant GMRO1-29935, and Robert A. Welch Foundation Grant I-0823 (to W. T. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence and reprint requests should be
addressed: Dept. of Molecular Biology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9148. Tel.:
214-648-1924; Fax: 214-648-1909; E-mail: garrard@utsw.swmed.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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