Donnelly S F, Pocklington M J, Pallotta D, Orr E
Department of Genetics, University of Leicester, UK.
Mol Microbiol. 1993 Nov;10(3):585-96. doi: 10.1111/j.1365-2958.1993.tb00930.x.
A gene (VRP1) encoding a novel proline-rich protein (verprolin) has been isolated from the yeast Saccharomyces cerevisiae as a result of its hybridization to a chick vinculin cDNA probe. The deduced protein sequence contains 24% proline residues present as proline-rich motifs throughout the verprolin sequence. Several of these motifs resemble recently identified sequences shown to bind Src homology 3 (SH3) domains in vitro. Replacement of the wild-type VRP1 allele with a mutant allele results in strains that grow slower than wild-type strains and are temperature sensitive. The vrp1 mutants are impaired in both cell shape and size and display aberrant chitin and actin localization. We propose that verporlin is involved in the maintenance of the yeast actin cytoskeleton, through interactions with other proteins, possibly containing SH3 domains.
通过与鸡纽蛋白cDNA探针杂交，从酿酒酵母中分离出一个编码新型富含脯氨酸蛋白（肌动蛋白结合蛋白）的基因（VRP1）。推导的蛋白质序列含有24%的脯氨酸残基，在整个肌动蛋白结合蛋白序列中以富含脯氨酸的基序形式存在。其中几个基序类似于最近鉴定出的在体外显示能结合Src同源结构域3（SH3）的序列。用突变等位基因替换野生型VRP1等位基因会导致菌株生长比野生型菌株慢且对温度敏感。vrp1突变体在细胞形状和大小方面均有缺陷，并显示几丁质和肌动蛋白定位异常。我们提出，肌动蛋白结合蛋白通过与其他可能含有SH3结构域的蛋白质相互作用，参与酵母肌动蛋白细胞骨架的维持。
