BIOCHEMICAL AND GENETIC-CHARACTERIZATION OF A REPLICATION PROTEIN-A DEPENDENT DNA HELICASE FROM THE YEAST, SACCHAROMYCES-CEREVISIAE

被引：17

作者：

BISWAS, EE

CHEN, PH

LESZYK, J

BISWAS, SB

机构：

[1] UNIV MARYLAND, SCH MED, DEPT PEDIAT, BALTIMORE, MD 21201 USA

[2] WORCESTER FDN EXPTL BIOL INC, SHREWSBURY, MA 01545 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 206卷 / 03期

关键词：

D O I：

10.1006/bbrc.1995.1121

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：

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. (C) 1995 Academic Press. Inc.

引用

页码：850 / 856

页数：7

共 19 条

[1]

BEAN DW, 1993, J BIOL CHEM, V268, P21783

[2] PURIFICATION AND CHARACTERIZATION OF A YEAST DNA POLYMERASE-ALPHA COMPLEX WITH ASSOCIATED PRIMASE, 5'-]3' EXONUCLEASE, AND DNA-DEPENDENT ATPASE ACTIVITIES [J].