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Plant Physiology 84:1102-1106 (1987)
© 1987 American Society of Plant Biologists

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Metabolism and Enzymology

Partial Purification and Characterization of Uracil-DNA Glycosylase Activity from Chloroplasts of Zea mays Seedlings

Robert J. Bensen1 and Huber R. Warner2

Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, Minnesota 55108

A uracil-DNA glycosylase activity has been purified about 750-fold from the chloroplasts of light-grown Zea mays seedlings. This report represents the first direct demonstration of a DNA-glycosylase repair activity in chloroplasts. The activity, in part, was associated with a chloroplast Triton X-100 sensitive membrane. Its apparent Km was 1.0 micromolar for a poly(dA-dT/U) substrate, and its molecular weight, as determined by gel filtration, was 18,000. The enzyme exhibited optimal activity at pH 7.0 with an atypically narrow pH tolerance. Activity was inhibited greater than 60% by 10 millimolar NaCl, 5 millimolar MgCl2, or 5 millimolar EDTA. Enzyme activity was inhibited 80% by 10 millimolar N-ethylmaleimide, a sulfhydryl group-blocking agent. The activity removed uracil more rapidly from single-stranded DNA than from double-stranded DNA. With this report, uracil-DNA glycosylase activity has now been attributed to all three DNA-containing organelles of eucaryotic cells.

1 Current address: Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.

2 Current address: Building 31, Room 5C19, National Institute on Aging, National Institutes of Health, Bethesda, MD 20205.




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 J. Biol. Chem.Home page
B. L. Gutman and K. K. Niyogi
Evidence for Base Excision Repair of Oxidative DNA Damage in Chloroplasts of Arabidopsis thaliana
J. Biol. Chem., June 19, 2009; 284(25): 17006 - 17012.
[Abstract] [Full Text] [PDF]


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Copyright © 1987 by the American Society of Plant Biologists