Nelson N
Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
J Bioenerg Biomembr. 1992 Aug;24(4):407-14. doi: 10.1007/BF00762533.
The vacuolar system of eukaryotic cells contains a large number of organelles that are primary energized by an H(+)-ATPase that was named V-ATPase. The structure and function of V-ATPases from various sources was extensively studied in the last few years. Several genes encoding subunits of the enzyme were cloned and sequenced. The sequence information revealed the relations between V-ATPases and F-ATPases that evolved from common ancestral genes. The two families of proton pumps share structural and functional similarity. They contain distinct peripheral catalytic sectors and hydrophobic membrane sectors. Genes encoding subunits of V-ATPase in yeast cells were interrupted to yield mutants that are devoid of the enzyme and are sensitive to pH and calcium concentrations in the medium. The mutants were used to study structure, function, molecular biology, and biogenesis of the V-ATPase. They also shed light on the functional assembly of the enzyme in the vacuolar system.
真核细胞的液泡系统包含大量由一种名为V-ATPase的H(+)-ATP酶提供主要能量的细胞器。在过去几年中，对来自各种来源的V-ATP酶的结构和功能进行了广泛研究。编码该酶亚基的几个基因被克隆并测序。序列信息揭示了V-ATP酶与从共同祖先基因进化而来的F-ATP酶之间的关系。这两个质子泵家族在结构和功能上具有相似性。它们包含不同的外周催化区和疏水膜区。酵母细胞中编码V-ATP酶亚基的基因被中断，以产生缺乏该酶且对培养基中的pH值和钙浓度敏感的突变体。这些突变体被用于研究V-ATP酶的结构、功能、分子生物学和生物发生。它们还揭示了该酶在液泡系统中的功能组装情况。
