The Role of the Amino-Terminal β-Barrel Domain of the α and β Subunits in the Yeast F1-ATPase

被引:0
作者
Bingyi Yao
David M. Mueller
机构
[1] The Chicago Medical School,Department of Biochemistry and Molecular Biology
来源
Journal of Bioenergetics and Biomembranes | 1999年 / 31卷
关键词
F; -ATPase; β-barrel domain; mitochondria; assembly; yeast;
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中图分类号
学科分类号
摘要
The crystal structure of mitochondrial F1-ATPase indicatesthat the α and β subunits fold into a structure defined by threedomains: the top β-barrel domain, the middle nucleotide-binding domain,and the C-terminal α-helix bundle domain (Abraham et al.1994); Bianchet et al., 1998). The β-barrel domains of theα and β subunits form a crown structure at the top ofF1, which was suggested to stabilize it (Abraham et al.1994). In this study. the role of the β-barrel domain in the α andβ subunits of the yeast Saccharomyces cerevisiae F1,with regard to its folding and assembly, was investigated. The β-barreldomains of yeast F1 α and β subunits were expressedindividually and together in Escherichia coli. When expressedseperately, the β-barrel domain of the β subunit formed a largeaggregate structure, while the domain of the α subunit waspredominately a monomer or dimer. However, coexpression of the β-barreldomain of α subunit domain. Furthermore, the two domains copurified incomplexes with the major portion of the complex found in a small molecularweight form. These results indicate that the β-barrel domain of theα and β subunits interact specifically with each other and thatthese interactions prevent the aggregation of the β-barrel domain of theβ subunit. These results mimic in vivo results and suggest thatthe interactions of the β-barrel domains may be critical during thefolding and assembly of F1.
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页码:95 / 104
页数:9
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