Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c.
Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c.
复制标题
DOI：
10.1016/j.febslet.2014.07.026
复制
发表时间：
2014-09-17
期刊：
影响因子：
3.5
通讯作者：
Ferguson SJ
中科院分区：
文献类型：
--
作者：
Zhang Y;Stevens JM;Ferguson SJ
全细胞色素c合酶（HCCS）不将血红素连接到在CXXCH基序中缺乏组氨酸的细胞色素上。HCCS可以识别C-末端截短的细胞色素c。细胞色素c中F15的芳香性或可能的形状互补性对于HCCS的识别是重要的。苯丙氨酸相对于CXXCH的间隔是识别特征。全细胞色素c合酶（HCCS）将血红素共价结合到线粒体呼吸细胞色素c上。尽管最近已经确定CXXCH基序和脱辅基细胞色素多肽的N末端是重要的蛋白质-蛋白质识别基序，但人们对HCCS将血红素附着到脱辅基细胞色素c上的反应知之甚少。在这里，我们进一步探索的N-末端序列的重要功能，并调查在CXXCH残基的变化是生产力认可HCCS在其基板。
Holocytochrome c synthase (HCCS) does not attach heme to cytochromes lacking the histidine in the CXXCH motif. HCCS can recognise C-terminally truncated cytochromes c. The aromatic nature of, or possibly shape complementarity to, F15 in cytochrome c is important for recognition by HCCS. The spacing of the phenylalanine relative to the CXXCH is a recognition feature. 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.
登录
查看更多内容
影响因子：
4.8
作者：
Bernard, DG;Gabilly, ST;Hamel, PP
通讯作者：
Hamel, PP
DOI：
10.1016/0005-2728(86)90234-3
发表时间：
1986-12-03
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
GOODHEW, CF;BROWN, KR;PETTIGREW, GW
通讯作者：
PETTIGREW, GW
影响因子：
4.1
作者：
Allen, James W. A.;Sawyer, Elizabeth B.;Ferguson, Stuart J.
通讯作者：
Ferguson, Stuart J.
影响因子：
3.8
作者：
Silkstone, G;Stanway, G;Wilson, MT
通讯作者：
Wilson, MT
影响因子：
2.9
作者：
BERRY, EA;TRUMPOWER, BL
通讯作者：
TRUMPOWER, BL