Mutations in the tether region of the iron-sulfur protein affect the activity and assembly of the cytochrome bc(1) complex of yeast mitochondria.
Mutations in the tether region of the iron-sulfur protein affect the activity and assembly of the cytochrome bc(1) complex of yeast mitochondria.
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铁硫蛋白系链区域的突变会影响酵母线粒体细胞色素 bc(1) 复合物的活性和组装。
DOI：
10.1016/s0005-2728(99)00116-4
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
Beattie,DS
中科院分区：
文献类型：
--
作者：
Obungu,VH;Wang,Y;Amyot,SM;Gocke,CB;Beattie,DS
Resolution of the crystal structure of the mitochondrial cytochrome bc1complex has indicated that the extra-membranous extrinsic domain of the iron–sulfur protein containing the 2Fe2S cluster is connected by a tether to the transmembrane helix that anchors the iron–sulfur protein to the complex. To investigate the role of this tether in the cytochrome bc1complex, we have mutated the conserved amino acid residues Ala-86, Ala-90, Ala-92, Lys-93 and Glu-95 and constructed deletion mutants ΔVLA(88–90) and ΔAMA(90–92) and an insertion mutant I87AAA88 in the iron–sulfur protein of the yeast, Saccharomyces cerevisiae. In cells grown at 30°C, enzymatic activities of the bc1complex were reduced 22–56% in mutants A86L, A90I, A92C, A92R and E95R, and the deletion mutants, ΔVLA(88–90) and ΔAMA(90–92), while activity of the insertion mutant was reduced 90%. No loss of cytochromes b or c–c1, detected spectrally, or the iron–sulfur protein, determined by quantitative immunoblotting, was observed in these mutants with the exception of the mutants of Ala-92 in which the loss of activity paralleled a loss in the amount of the iron–sulfur protein. EPR spectroscopy revealed no changes in the iron–sulfur cluster of mutants A86L, A90I, A92R or the deletion mutant ΔVLA(88–90). Greater losses of both protein and activity were observed in all of the mutants of Ala-92 as well as in A90F grown at 37°C. suggesting that these conserved alanine residues may be involved in maintaining the stability of the iron–sulfur protein and its assembly into the bc1complex. By contrast, no significant loss of iron–sulfur protein was observed in the mutants of Ala-86 in cells grown at either 30°C or 37°C despite the 50–70% loss of enzymatic activity suggesting that Ala-86 may play a critical role in catalysis in the bc1complex.
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线粒体细胞色素 bc1 复合物功能的结构基础。
DOI：
10.1016/s0005-2728(98)00055-3
发表时间：
1998
期刊：
Biochimica et biophysica acta
影响因子：
--
作者：
Yu,CA;Xia,D;Kim,H;Deisenhofer,J;Zhang,L;Kachurin,AM;Yu,L
通讯作者：
Yu,L
荚膜红杆菌 bc1 复合体的泛氢醌氧化位点上细胞色素 b、细胞色素 c1 和 Fe-S 蛋白亚基之间的相互作用。
DOI：
10.1021/bi973146s
发表时间：
1998
期刊：
Biochemistry.
影响因子：
--
作者：
Saribas,AS;Valkova-Valchanova,M;Tokito,MK;Zhang,Z;Berry,EA;Daldal,F
通讯作者：
Daldal,F
酿酒酵母线粒体 Rieske 铁硫蛋白的突变分析。
DOI：
--
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Graham,LA;Trumpower,BL
通讯作者：
Trumpower,BL
牛心脏线粒体 bc1 复合物 Rieske 铁硫蛋白水溶性片段的分离、表征和结晶。
DOI：
--
发表时间：
1996
期刊：
European Journal of Biochemistry
影响因子：
--
作者：
T. Link;M. Saynovits;C. Aßmann;S. Iwata;T. Ohnishi;G. von Jagow
通讯作者：
G. von Jagow
影响因子：
64.5
作者：
DUNN, B;SZAUTER, P;SZOSTAK, JW
通讯作者：
SZOSTAK, JW