De Vries S, Van Witzenburg R, Grivell L A, Marres C A
Department of Molecular Cell Biology, University of Amsterdam, The Netherlands.
Eur J Biochem. 1992 Feb 1;203(3):587-92. doi: 10.1111/j.1432-1033.1992.tb16587.x.
The gene encoding the yeast mitochondrial rotenone-insensitive internal NADH: ubiquinone-6 oxidoreductase has been sequenced. The DNA sequence indicates the presence of an open reading frame of 1539 bp predicted to encode a protein of 513 amino acid residues (57.2 kDa). The NADH dehydrogenase is synthesized as a precursor protein containing a signal sequence of 26 residues. In vitro import experiments show that the precursor NADH dehydrogenase is cleaved to the mature size by the matrix processing peptidase. Both cleavage and translocation across the mitochondrial membrane(s) are dependent on the membrane potential component of the proton-motive force. Comparison of the protein sequence of the yeast NADH dehydrogenase with the data bank indicates that the enzyme from yeast is homologous to the NADH dehydrogenase of Escherichia coli (22.2% identical residues). Both NADH dehydrogenases contain in the central part of the protein a sequence predicted to fold into a beta alpha beta structure involved in the binding of NADH or FAD(H2). Various aspects of the protein structure are discussed.
编码酵母线粒体鱼藤酮不敏感型内部NADH：泛醌-6氧化还原酶的基因已被测序。DNA序列表明存在一个1539 bp的开放阅读框，预计编码一个由513个氨基酸残基组成的蛋白质（57.2 kDa）。NADH脱氢酶作为一种含有26个残基信号序列的前体蛋白被合成。体外导入实验表明，前体NADH脱氢酶被基质加工肽酶切割成成熟大小。切割和跨线粒体膜转运均依赖于质子动力的膜电位成分。酵母NADH脱氢酶的蛋白质序列与数据库数据的比较表明，酵母中的该酶与大肠杆菌的NADH脱氢酶同源（相同残基为22.2%）。两种NADH脱氢酶在蛋白质的中央部分都含有一个预计会折叠成参与NADH或FAD(H2)结合的β-α-β结构的序列。文中讨论了蛋白质结构的各个方面。
