来自大豆叶绿体的一种DNA解旋酶的部分纯化及特性分析

Partial purification and characterization of a DNA helicase from chloroplasts of Glycine max.

作者信息

Cannon G C, Heinhorst S

机构信息

Department of Chemistry and Biochemistry, University of Southern Mississippi, Hattiesburg 39406.

出版信息

Plant Mol Biol. 1990 Sep;15(3):457-64. doi: 10.1007/BF00019162.

DOI:10.1007/BF00019162

PMID:1966489

Abstract

A DNA helicase activity was detected in extracts of purified chloroplasts from the SB-1 cell line of Glycine max and partially purified by column chromatography on DEAE cellulose, phosphocellulose, and single-stranded DNA cellulose. The chloroplast helicase has a DNA-dependent ATPase activity, and its strand displacement activity is strictly dependent upon the presence of a nucleoside triphosphate and Mg2+ or Mn2+. Strand displacement activity does not require a free unannealed single-strand or replication fork-like structure.

摘要

在大豆SB-1细胞系纯化叶绿体提取物中检测到一种DNA解旋酶活性，并通过在DEAE纤维素、磷酸纤维素和单链DNA纤维素上进行柱色谱法进行部分纯化。叶绿体解旋酶具有依赖于DNA的ATP酶活性，其链置换活性严格依赖于三磷酸核苷以及Mg2+或Mn2+的存在。链置换活性不需要游离的未退火单链或复制叉样结构。