Biochemical and genetic characterization of a replication protein A dependent DNA helicase from the yeast, Saccharomyces cerevisiae - PubMed (original) (raw)
. 1995 Jan 26;206(3):850-6.
doi: 10.1006/bbrc.1995.1121.
Affiliations
- PMID: 7832796
- DOI: 10.1006/bbrc.1995.1121
Biochemical and genetic characterization of a replication protein A dependent DNA helicase from the yeast, Saccharomyces cerevisiae
E E Biswas et al. Biochem Biophys Res Commun. 1995.
Abstract
We have purified a DNA dependent ATPase/DNA helicase, DNA helicase B, from S. cerevisiae. Helicase B was a 129-kDa polypeptide. The ATPase activity of helicase B was strongly DNA dependent. The DNA helicase activity was stimulated by yeast replication protein A, indicating a probable function in DNA replication. Helicase B showed a 5'-->3' polarity of movement. Protein sequencing indicated that helicase B was identical to a hypothetical 127-kDa polypeptide encoded by yORF61, located 5' upstream of the BMH1 locus in chromosome V. The protein sequence contained a "type I ATP/GTP binding motif" and other helicase-like motifs and the expressed protein exhibited helicase activity. Thus, we concluded that yORF61 is the gene for helicase B and will be referred to as HCSB.
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