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标题：Primary structure, import, and assembly of the yeast homolog of succinate dehydrogenase flavoprotein
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作者：N Schülke ; G Blobel ; D Pain 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1992
卷号：89
期号：17
页码：8011-8015
DOI：10.1073/pnas.89.17.8011
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：We have isolated a homolog for the flavoprotein subunit of succinate dehydrogenase [succinate:(acceptor) oxidoreductase, EC 1.3.99.1 ] from Saccharomyces cerevisiae and used the obtained peptide sequences to clone and characterize the corresponding gene. It contained an open reading frame of 1923 base pairs and encoded a protein of 640 amino acids (M(r), 70,238) that showed approximately 49% and approximately 28% identity with the Escherichia coli and Bacillus subtilis enzymes, respectively. All features of the FAD cofactor binding site were completely conserved. Comparison of the deduced protein sequence with the N-terminal sequence determined from the isolated protein revealed an N-terminal extension of 28 amino acids that presumably represents a mitochondrial signal sequence. After in vitro transcription and translation, the preprotein was efficiently imported into isolated yeast mitochondria, cleaved to its mature form, and assembled into the membrane-bound succinate dehydrogenase complex.