Interactions of the Escherichia coli hydrogenase biosynthetic proteins:: HybG complex formation

被引:27
作者
Butland, G
Zhang, JW
Yang, WH
Sheung, A
Wong, P
Greenblatt, JF
Emili, A
Zamble, DB
机构
[1] Univ Toronto, Dept Chem, Toronto, ON M5S 3H6, Canada
[2] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
hydrogenase; metallocenter assembly; accessory protein interactions; nickel;
D O I
10.1016/j.febslet.2005.12.063
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Assembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway and the coordinated activity of many accessory proteins. To analyze complex formation between these factors in Escherichia coli, they were genomically tagged and native multi-protein complexes were isolated. This method validated multiple interactions reported in separate studies from several organisms and defined a new complex containing the putative chaperone HybG and the large subunit of hydrogenase 1 or 2. The complex also includes HypE and HypD, which interact with each other before joining the larger complex. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:677 / 681
页数:5
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