Identification of MYO4, a second class V myosin gene in yeast.

Identification of MYO4, a second class V myosin gene in yeast.
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DOI:
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发表时间:
1994-04
影响因子:
4
通讯作者:
B K Haarer;A. Petzold;S. H. Lillie;S. Brown
B K Haarer;A. Petzold;S. H. Lillie;S. Brown
中科院分区:
生物学2区
文献类型:
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作者:
B K Haarer;A. Petzold;S. H. Lillie;S. Brown

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我们在酵母(酿酒酵母)中分离出了第四个肌球蛋白基因(MYO4)。 MYO4 使用 Cheney 等人设计的分类法编码大约 170 kDa(1471 个氨基酸)的 V 类肌球蛋白。 (1993a;Cell Motil.Cytoskel.24, 215-223);运动结构域之后是包含六个假定的钙调蛋白结合位点的颈部区域和具有短的潜在“卷曲螺旋”结构域的尾部。与 GenBank 中其他肌球蛋白的比较表明,Myo4 蛋白与酵母 Myo2 蛋白(另一种 V 类肌球蛋白)关系最密切。 MYO4 的缺失无论是单独的还是与 myo2 或其他肌球蛋白基因、肌动蛋白基因或分泌基因的突变结合,都不会产生可检测的表型。然而,MYO4 或 MYO2 的过度表达会导致几种形态异常,包括在二倍体菌株中形成短串未分离的细胞,或在单倍体菌株中形成细胞簇。 MYO4 或 MYO2 的改变表明,这些肌球蛋白的运动结构域和尾部都不需要赋予过度表达表型,而颈部区域可能是需要的。尽管这种表型与 MYO1 缺失时所见的表型相似,但我们提供的证据表明,Myo4p 或 Myo2p 的过度表达并不简单地干扰 Myo1p 功能。
We have isolated a fourth myosin gene (MYO4) in yeast (Saccharomyces cerevisiae). MYO4 encodes a approximately 170 kDa (1471 amino acid) class V myosin, using the classification devised by Cheney et al. (1993a; Cell Motil. Cytoskel. 24, 215-223); the motor domain is followed by a neck region containing six putative calmodulin-binding sites and a tail with a short potential 'coiled-coil' domain. A comparison with other myosins in GenBank reveals that Myo4 protein is most closely related to the yeast Myo2 protein, another class V myosin. Deletion of MYO4 produces no detectable phenotype, either alone or in conjunction with mutations in myo2 or other myosin genes, the actin gene, or secretory genes. However, overexpression of MYO4 or MYO2 results in several morphological abnormalities, including the formation of short strings of unseparated cells in diploid strains, or clusters of cells in haploid strains. Alterations of MYO4 or MYO2 indicate that neither the motor domains nor tails of these myosins are required to confer the overexpression phenotype, whereas the neck region may be required. Although this phenotype is similar to that seen upon MYO1 deletion, we provide evidence that the overexpression of Myo4p or Myo2p is not simply interfering with Myo1p function.