Domains of tobacco mosaic virus movement protein essential for its membrane association
Domains of tobacco mosaic virus movement protein essential for its membrane association
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DOI：
10.1099/vir.0.81936-0
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发表时间：
2006-09-01
影响因子：
3.8
通讯作者：
Beachy, Roger N.
中科院分区：
文献类型：
--
作者：
Fujiki, Masaaki;Kawakami, Shigeki;Beachy, Roger N.
利用烟草花叶病毒运动蛋白（TMV-MP）的一系列缺失突变体，对膜结合所必需的蛋白质结构域进行了鉴定。从用野生型和突变型TMV感染的烟草BY-2原生质体中分离膜部分，所述突变型TMV产生携带3as缺失的MP。影响膜缔合的缺失聚集在MP的两个主要疏水区域周围，这两个区域被预测为跨膜。其他疏水区域的缺失也减少了膜结合。此外，MP的非功能突变体，其中一个已知的磷酸化位点被消除，不与细胞膜，而功能的第二个网站回复突变恢复膜协会。这表明MP功能需要与膜相互作用;然而，膜缔合不足以发挥功能。结果是一致的假设，TMV-MP是一个完整的或紧密相关的膜蛋白，包括两个疏水跨膜结构域。
A series of deletion mutants of tobacco mosaic virus movement protein (TMV-MP) was used to identify domains of the protein necessary for membrane association. A membrane fraction was isolated from tobacco BY-2 protoplasts infected with wild-type and mutant TMV that produce MP carrying a 3 as deletion. Deletions that affected membrane association were clustered around the two major hydrophobic regions of MP that are predicted to be transmembrane. Deletions in other hydrophobic regions also reduced membrane association. In addition, a non-functional mutant of MP, in which one of the known phosphorylation sites was eliminated, was not associated with cellular membranes, while a functional second site revertant restored membrane association. This indicates that MP function requires interaction with membrane; however, membrane association was not sufficient for function. Results are consistent with the hypothesis that TMV-MP is an integral or tightly associated membrane protein that includes two hydrophobic transmembrane domains.