Purification and characterisation of a soluble N-terminal fragment of the breast cancer susceptibility protein BRCA1

被引：15

作者：

Sturdy, A ^{[1
]}

Naseem, R ^{[1
]}

Webb, M ^{[1
]}

机构：

[1] Univ Sheffield, Dept Chem, Sheffield S3 7HF, S Yorkshire, England

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2004年 / 340卷 / 03期

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

breast cancer; BRCA1; DNA binding; four-way junction;

D O I：

10.1016/j.jmb.2004.05.005

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：

The BRCA1 gene encodes a large multidomain protein of 1863 residues, mutations in which lead to breast cancer. Studies to elucidate the mechanisms by which BRCA1 prevents tumour formation have been restricted by the size of the protein. Unable to purify large amounts of the full-length protein, we have identified a fragment of BRCA1, amino acid residues 230-534, that when cloned into the expression vector pET 22b and expressed in Escherichia coli is found predominantly in the soluble portion of the cell lysate. The resulting protein was purified to homogeneity and studies reveal that BRCA1 230-534 binds specifically to four-way junction DNA when compared to duplex and single-stranded DNA. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：469 / 475

页数：7

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