Identification of functional domains in Atp11p. Protein required for assembly of the mitochondrial F1-ATPase in yeast.
Identification of functional domains in Atp11p. Protein required for assembly of the mitochondrial F1-ATPase in yeast.
复制标题
Atp11p 功能域的鉴定。
DOI：
10.1074/jbc.271.9.4887
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Ackerman,SH
中科院分区：
文献类型：
--
作者：
Wang,ZG;Ackerman,SH
The Atp11p protein ofSaccharomyces cerevisiaeis required for proper assembly of the F1component of the mitochondrial ATP synthase. The mutantatp11genes were cloned and sequenced from 12 yeast strains, which are respiratory-deficient due to a defect in Atp11p function. Four of the mutations mapped to the mitochondrial targeting domain (amino-terminal 39 amino acids) of Atp11p. All the genetic lesions found in the mature protein sequence were shown to be nonsense mutations. This result is consistent with the idea that Atp11p activity is provided, principally, by the overall structure of a functional domain, and not by specific amino acid residues in a localized active site. Amino-terminal (Edman) sequence analysis of fragments derived from limited proteolysis of purified Atp11p, andin vivofunctional characterization of deletion mutants, were employed to locate the position of the active region in the protein. Three domains, separated by proline-rich sequences, were identified in the mature protein. The active domain of Atp11p was mapped to the sequence between Phe-120 and Asn-174. The domains proximal (Glu-40 through Ser-109) and distal (Arg-183 through Asn-318) to the active region were found to be important for the protein stability inside mitochondria.
