The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification

被引:25
作者
Zheng, WJ
Johnston, SA
机构
[1] Univ Texas, SW Med Ctr, Dept Med, Grad Program Biochem & Mol Biol, Dallas, TX 75235 USA
[2] Univ Texas, SW Med Ctr, Dept Biochem, Grad Program Biochem & Mol Biol, Dallas, TX 75235 USA
关键词
D O I
10.1128/MCB.18.6.3580
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3580 / 3585
页数:6
相关论文
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