Motif CXCC in nitrile hydratase activator is critical for NHase biogenesis in vivo

被引：54

作者：

Lu, J ^{[1
]}

Zheng, YJ

Yamagishi, H

Odaka, M

Tsujimura, M

Maeda, M

Endo, I

机构：

[1] RIKEN, Bioengn Lab, Wako, Saitama 3510198, Japan

[2] Chinese Acad Sci, Changchun Inst Appl Chem, Key Lab Rare Earth Chem & Phys, Changchun 130022, Peoples R China

[3] Utsunomiya Univ, Fac Agr, Dept Bioprod Sci, Utsunomiya, Tochigi 3218505, Japan

来源：

FEBS LETTERS | 2003年 / 553卷 / 03期

基金：

日本学术振兴会;

关键词：

nitrile hydratase; nitrile hydratase activator; site-directed mutagenesis; protein-protein interaction; iron trafficking;

D O I：

10.1016/S0014-5793(03)01070-6

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：

Nitrile hydratase (NHase) activator from Rhodococcus sp. N-771 is required for NHase functional expression. The motif 73CXCC76 in the NHase activator sequence was here revealed to be vital for its function by site-directed mutagenesis. All three substitutions of the cysteines by serines resulted in a much lower level of expression of active NHase. Furthermore, interaction between NHase activator and NHase was detected and the critical role of NHase activator was not exhibited in the cysteine oxidization process of NHase. These findings suggest NHase activator mainly participates in iron trafficking in NHase biogenesis as an iron type metallochaperone. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：391 / 396

页数：6

共 32 条

[1] Solution structure of the Cu(I) and Apo forms of the yeast metallochaperone, Atx1 [J].