LIPID SPECIFICITY FOR MEMBRANE MEDIATED PARTIAL UNFOLDING OF CYTOCHROME-C

被引:34
作者
DEJONGH, HHJ [1 ]
RITSEMA, T [1 ]
KILLIAN, JA [1 ]
机构
[1] UNIV UTRECHT, CTR BIOMEMBRANES & LIPID ENZYMOL, DEPT MEMBRANE BIOCHEM, 3584 CH UTRECHT, NETHERLANDS
来源
FEBS LETTERS | 1995年 / 360卷 / 03期
关键词
PHOSPHOLIPID; CYTOCHROME C; PROTEIN FOLDING; EXCHANGE; PROTEOLYTIC DIGESTION;
D O I
10.1016/0014-5793(95)00115-P
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
In this study we investigated the lipid specificity for destabilization of the native structure of horse heart cytochrome c by model membranes. From (i) the enhanced release of deuterium from deuterium-labelled cytochrome c and (ii) the increased proteolytic digestion of the protein in the presence of anionic lipids, it was concluded that these lipids are able to destabilize the native structure of cytochrome c. Changes in the absorbance at 695 mm indicated that the destabilization was accompanied by a diminished ligation of Met-80 to the heme. Beef heart cardiolipin was found to be more effective than DOPS, DOPG or DOPA, while no protein destabilization was observed in the presence of the zwitterionic lipid DOPC or, surprisingly, in the presence of E. coli cardiolipin. Experiments with mitoplasts showed that the protein can also be destabilized in its native structure by a biological membrane.
引用
收藏
页码:255 / 260
页数:6
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