Rizzuto R, Sandonà D, Brini M, Capaldi R A, Bisson R
CNR Centro Studi per la Fisiologia dei Mitocondri, Università di Padova, Italy.
Biochim Biophys Acta. 1991 Dec 2;1129(1):100-4. doi: 10.1016/0167-4781(91)90220-g.
A full-length 515 base pairs cDNA for cytochrome c oxidase subunit V of D. discoideum was isolated from a lambda gt11 expression library. The encoded polypeptide, whose identity was confirmed by partial protein sequencing, is 119 amino acids long (Mr = 13,352) and does not contain a cleavable presequence. The protein, which is homologous to human subunit Vb and yeast subunit IV, exhibits the highest degree of sequence conservation found among nuclear-encoded subunits of cytochrome c oxidase from distantly related organisms. All the invariant residues are clustered in two regions of the C-terminus which include the putative amino acids involved in the coordination of the Zn ion tightly associated to eukaryotic oxidase.
从一个λgt11表达文库中分离出了编码盘基网柄菌细胞色素c氧化酶亚基V的全长515个碱基对的cDNA。通过部分蛋白质测序证实了其编码的多肽，该多肽长度为119个氨基酸（Mr = 13,352），且不包含可裂解的前导序列。该蛋白质与人类亚基Vb和酵母亚基IV同源，在远缘生物的细胞色素c氧化酶的核编码亚基中表现出最高程度的序列保守性。所有不变残基都聚集在C末端的两个区域，其中包括与真核氧化酶紧密相关的锌离子配位中涉及的推定氨基酸。
