Isolation and characterization of a cDNA clone for bovine cytochrome c oxidase subunit IV.
Isolation and characterization of a cDNA clone for bovine cytochrome c oxidase subunit IV.
复制标题
牛细胞色素 c 氧化酶亚基 IV cDNA 克隆的分离和表征。
DOI:
10.1073/pnas.81.20.6295
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发表时间:
1984
影响因子:
11.1
通讯作者:
Grossman,LI
中科院分区:
文献类型:
--
作者:
Lomax,MI;Bachman,NJ;Nasoff,MS;Caruthers,MH;Grossman,LI
We have isolated a cDNA clone for the precursor to subunit IV of bovine cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1). A cDNA library was constructed from poly(A)+ RNA of adult beef liver by insertion of cDNA into the plasmid vector pBR322. Transformants were screened by colony hybridization with two mixtures of [32P]-labeled synthetic oligodeoxyribonucleotides. We screened 20,000 transformants with a mixture of heptadecamers complementary to all 16 possible sequences encoding amino acids 98-103 and obtained two cDNA clones encoding subunit IV amino acid sequences. We determined the DNA sequence of the larger (416 base-pair) insert, which contains the coding sequence for amino acids 1-107 of the mature protein and an NH2-terminal extension (presequence). The deduced amino acid sequence of the mature protein is identical with the previously determined protein sequence: the sequence of the NH2-terminal extension contains a potential initiator methionine at amino acid -22 from the NH2-terminus of the processed protein. The presequence is quite basic and contains several arginines, including one at the processing site. No hydrophobic region analogous to that found in bacterial and eukaryotic signal peptides is present, but there are homologies with other mitochondrial protein presequences, which may include a common signal for their destination and processing.
DOI:
--
发表时间:
1983
期刊:
影响因子:
--
作者:
B. Roques
通讯作者:
B. Roques