期刊
JOURNAL OF VIROLOGY
卷 78, 期 7, 页码 3704-3709出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.78.7.3704-3709.2004
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资金
- NIGMS NIH HHS [R01 GM053190, R1GM53190] Funding Source: Medline
Cell-to-cell movement of beet yellows closterovirus requires four structural proteins and a 6-kDa protein (p6) that is a conventional, nonstructural movement protein. Here we demonstrate that either virus infection or p6 overexpression results in association of p6 with the rough endoplasmic reticulum. The p6 protein possesses a single-span, transmembrane, N-terminal domain and a hydrophilic, C-terminal domain that is localized on the cytoplasmic face of the endoplasmic reticulum. In the infected cells, p6 forms a disulfide bridge via a cysteine residue located near the protein's N terminus. Mutagenic analyses indicated that each of the p6 domains, as well as protein dimerization, is essential for p6 function in virus movement.
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