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Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c
被引:11
|作者:
Zhang, Yulin
[1
]
Stevens, Julie M.
[1
]
Ferguson, Stuart J.
[1
]
机构:
[1] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England
来源:
FEBS LETTERS
|
2014年
/
588卷
/
18期
基金:
英国生物技术与生命科学研究理事会;
关键词:
Cytochrome c;
Holocytochrome c synthase;
Heme;
Ccm system;
SITE-DIRECTED MUTAGENESIS;
MATURATION CCM APPARATUS;
HEME-BINDING MOTIF;
ONE THIOETHER BOND;
ESCHERICHIA-COLI;
APOCYTOCHROME-C;
SACCHAROMYCES-CEREVISIAE;
SEQUENCE REQUIREMENTS;
LYASE;
IMPORT;
D O I:
10.1016/j.febslet.2014.07.026
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:
Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N-terminus of the apocytochrome polypeptide are important protein-protein recognition motifs. Here, we explore further the important features of the N-terminal sequence and investigate what variations in the CXXCH residues are productively recognised by HCCS in its substrate. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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页码:3367 / 3374
页数:8
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