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Mol Cell Biol, June 1998, p. 3580-3585, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Nucleic Acid Binding Activity of Bleomycin Hydrolase Is Involved in Bleomycin Detoxification

Wenjin Zheng and Stephen Albert Johnston*

Departments of Medicine and Biochemistry, Graduate Program in Biochemistry and Molecular Biology, University of Texas-Southwestern Medical Center, Dallas, Texas 75235-8573

Received 1 December 1997/Returned for modification 14 January 1998/Accepted 26 February 1998

Yeast bleomycin hydrolase, Gal6p, is a cysteine peptidase that detoxifies the anticancer drug bleomycin. Gal6p is a dual-function protein capable of both nucleic acid binding and peptide cleavage. We now demonstrate that Gal6p exhibits sequence-independent, high-affinity binding to single-stranded DNA, nicked double-stranded DNA, and RNA. A region of the protein that is involved in binding both RNA and DNA substrates is delineated. Immunolocalization reveals that the Gal6 protein is chiefly cytoplasmic and thus may be involved in binding cellular RNAs. Variant Gal6 proteins that fail to bind nucleic acid also exhibit reduced ability to protect cells from bleomycin toxicity, suggesting that the nucleic acid binding activity of Gal6p is important in bleomycin detoxification and may be involved in its normal biological functions.

* Corresponding author. Mailing address: Department of Medicine, UT-Southwestern, 5323 Harry Hines Blvd., Dallas, TX 75235-8573. Phone: (214) 648-1415. Fax: (214) 648-1450. E-mail: johnston{at}ryburn.swmed.edu.

Mol Cell Biol, June 1998, p. 3580-3585, Vol. 18, No. 6
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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