IDENTIFICATION AND MOLECULAR CHARACTERIZATION OF A YEAST MYOSIN-I
IDENTIFICATION AND MOLECULAR CHARACTERIZATION OF A YEAST MYOSIN-I
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DOI：
10.1002/cm.970300109
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发表时间：
1995-01-01
影响因子：
--
通讯作者：
SPUDICH, JA
中科院分区：
文献类型：
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作者：
GOODSON, HV;SPUDICH, JA
肌球蛋白马达家族由分布在不同生物体和细胞类型中的许多类别组成。我们已经确定了一个非常规的肌球蛋白基因（MYO 3）的酵母酿酒酵母，并表明它是一个亚类的非常规肌球蛋白蛋白的成员最初只发现在变形虫生物Dictyosteelium和阿米巴。在这些遗传和形态学上不同的生物体中鉴定这种蛋白质表明它将在真核生物中普遍存在，并且它在真核细胞的基本功能中起作用。我们已经构建了一种缺失99% MYO 3编码序列的酵母菌株。这种突变没有可观察到的表型效应，将MYO 3置于一个不断增长的酵母基因类别中，这些基因在实验室条件下是不稳定的，这可能是由于遗传冗余。MYO 3与其他非常规肌球蛋白的比对表明，它与它们的一个子集共享一个以前未被识别的尾部同源区域;该区域福尔斯属于一个被鉴定为对介导与膜的非特异性静电相互作用很重要的结构域。该区域的存在表明它可能参与介导特定的蛋白质-蛋白质相互作用，可能有助于将该肌球蛋白定位于特定的膜或膜区域。此外，我们发现，“经典”的肌球蛋白I蛋白共享一个区域的超脯氨酸丰富的10个氨基酸之前的SH 3结构域。脯氨酸丰富的区域最近被认为是SH 3结合位点，这表明该区域可能参与调节或以其他方式与SH 3结构域相互作用。(C)1995 Wiley-Liss，Inc.
The family of myosin motors is comprised of numerous classes distributed among a diverse set of organisms and cell types. We have identified an unconventional myosin gene (MYO3) in the yeast Saccharomyces cerevisiae and show that it is member of a subclass of unconventional myosin proteins originally found only in the amoeboid organisms Dictyostelium and Acanthamoeba. Identification of this protein in these genetically and morphologically divergent organisms suggests that it will be ubiquitous in eukaryotes and that it has a role in the basic functions of the eukaryotic cell. We have constructed a strain of yeast missing 99% of the MYO3 coding sequence. This mutation has no observable phenotypic effect, placing MYO3 into a growing class of yeast genes which are dispensable under laboratory conditions, perhaps due to genetic redundancy. Alignment of MYO3 with other unconventional myosins shows that it shares with a subset of them a previously unrecognized region of homology in the tail; this region falls within a domain identified as important for mediating nonspecific electrostatic interactions with membranes. The existence of this region suggests that it may be involved in mediating specific protein-protein interactions, possibly helping to localize this myosin to specific membranes or membrane regions. In addition, we show that ''classic'' myosin I proteins share a region of hyper-proline-richness 10 amino acids before the SH3 domain. Proline-rich regions have recently been implicated as SH3 binding sites, which suggests that this region might be involved with regulating or in other ways interacting with SH3 domains.(C) 1995 Wiley-Liss, Inc.