DISRUPTION OF THE SINGLE TROPOMYOSIN GENE IN YEAST RESULTS IN THE DISAPPEARANCE OF ACTIN CABLES FROM THE CYTOSKELETON
DISRUPTION OF THE SINGLE TROPOMYOSIN GENE IN YEAST RESULTS IN THE DISAPPEARANCE OF ACTIN CABLES FROM THE CYTOSKELETON
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DOI：
10.1016/0092-8674(89)90961-6
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发表时间：
1989-04-21
期刊：
影响因子：
64.5
通讯作者：
BRETSCHER, A
中科院分区：
文献类型：
--
作者：
LIU, H;BRETSCHER, A
酵母原肌球蛋白基因，命名为TPM 1，存在于每个单倍体基因组的单拷贝中，并编码预测分子量为23.5 kd的蛋白质。该蛋白质序列与高等细胞原肌球蛋白同源，包括特征性疏水-亲水假七肽重复序列。间接免疫荧光显微镜显示，原肌球蛋白是本地化与肌动蛋白电缆在野生型细胞。TPM 1的破坏不是致命的，但会导致生长速率降低和肌动蛋白电缆的消失。携带条件肌动蛋白突变act 1 -2的菌株也缺乏肌动蛋白电缆;在这些菌株中原肌球蛋白的过度表达部分恢复肌动蛋白电缆。这些结果强烈表明，原肌球蛋白与F肌动蛋白在体内相互作用，并可能发挥重要作用，在组装或稳定肌动蛋白电缆在酵母。
The yeast tropomyosin gene, designated TPM1, is present in a single copy per haploid genome and encodes a protein with a predicted molecular weight of 23.5 kd. The protein sequence is homologous to higher cell tropomyosins, including the characteristic hydrophobic-hydrophilic pseudoheptapeptide repeats. Indirect immunofluorescence microscopy reveals that tropomyosin is localized with actin cables in wild-type cells. Disruption of TPM1 is not lethal, but results in a reduced growth rate and disappearance of actin cables. Strains carrying the conditional actin mutation act1-2 also lack actin cables; overexpression of tropomyosin in these strains partially restores actin cables. These results strongly suggest that tropomyosin interacts with F actin in vivo and may play an important role in assembling or stabilizing actin cables in yeast.