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

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

Yeast bleomycin hydrolase, Ga16p, is a cysteine peptidase that detoxifies the anticancer drug bleomycin. Ga16p is a dual-function protein capable of both nucleic acid binding and peptide cleavage. We now demonstrate that Ga16p 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.

Original languageEnglish (US)
Pages (from-to)3580-3585
Number of pages6
JournalMolecular and cellular biology
Volume18
Issue number6
DOIs
StatePublished - Jun 1998
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification'. Together they form a unique fingerprint.

Cite this