The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding
文献类型:期刊论文
作者 | Liu, JL ; Rigolet, P ; Dou, SX ; Wang, PY ; Xi, XG |
刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
![]() |
出版日期 | 2004 |
卷号 | 279期号:41页码:42794 |
关键词 | BLOOMS-SYNDROME GENE SACCHAROMYCES-CEREVISIAE CRYSTAL-STRUCTURES FAMILY HELICASES DOMAIN MUTATIONS MECHANISM RECOMBINATION REPLICATION NUCLEOTIDES |
ISSN号 | 0021-9258 |
通讯作者 | Xi, XG (reprint author), Ecole Normale Super, CNRS, UMR 8113, Lab Biotechnol & Pharmacol Genet Appl, 61 Ave President Wilson, F-94235 Cachan, France. |
中文摘要 | The RecQ family of DNA helicases has been shown to be important for the maintenance of genomic integrity. Mutations in human RecQ genes lead to genomic instability and cancer. Several RecQ family of helicases contain a putative zinc finger motif of the C-4 type at the C terminus that has been identified in the crystalline structure of RecQ helicase from Escherichia coli. To better understand the role of this motif in helicase from E. coli, we constructed a series of single mutations altering the conserved cysteines as well as other highly conserved residues. All of the resulting mutant proteins exhibited a high level of susceptibility to degradation, making functional analysis impossible. In contrast, a double mutant protein in which both cysteine residues Cys(397) and Cys(400) in the zinc finger motif were replaced by asparagine residues was purified to homogeneity. Slight local conformational changes were detected, but the rest of the mutant protein has a well defined tertiary structure. Furthermore, the mutant enzyme displayed ATP binding affinity similar to the wild-type enzyme but was severely impaired in DNA binding and in subsequent ATPase and helicase activities. These results revealed that the zinc finger binding motif is involved in maintaining the integrity of the whole protein as well as DNA binding. We also showed that the zinc atom is not essential to enzymatic activity. |
收录类别 | SCI |
语种 | 英语 |
公开日期 | 2013-09-23 |
源URL | [http://ir.iphy.ac.cn/handle/311004/45608] ![]() |
专题 | 物理研究所_物理所公开发表论文_物理所公开发表论文_期刊论文 |
推荐引用方式 GB/T 7714 | Liu, JL,Rigolet, P,Dou, SX,et al. The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2004,279(41):42794. |
APA | Liu, JL,Rigolet, P,Dou, SX,Wang, PY,&Xi, XG.(2004).The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding.JOURNAL OF BIOLOGICAL CHEMISTRY,279(41),42794. |
MLA | Liu, JL,et al."The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding".JOURNAL OF BIOLOGICAL CHEMISTRY 279.41(2004):42794. |
入库方式: OAI收割
来源:物理研究所
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。