SGD Paper 
Zheng W and Johnston SA (1998) The nucleic acid binding activity of bleomycin hydrolase is involved in bleomycin detoxification. Mol Cell Biol 18(6):3580-5
Abstract: 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.
| Status: Published | Type: Journal Article | PubMed ID: 9584198 |
Topics addressed in this paper
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
| Topics | Genes linked to topics |
|---|---|
| LAP3 | |
| Alias |  |
| Cellular Location | |
| Function/Process | |
| Mutants/Phenotypes | |
| Primary Literature | |
| Protein-Nucleic Acid Interactions | |
| Strains/Constructs | |
