Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum.
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.
Peremyslov
Valera V
VV
Department of Botany and Plant Pathology and Center for Gene Research and Biotechnology, Oregon State University, Corvallis, Oregon 97331, USA.
Pan
Yung-Wei
YW
Dolja
Valerian V
VV
D000409:Alanine / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D002460:Cell Line; D017790:Closterovirus / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D019281:Dimerization; D018870:Endoplasmic Reticulum, Rough / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009068:Movement; D009154:Mutation; D053830:Plant Viral Movement Proteins; D011487:Protein Conformation; D014026:Nicotiana / Q000821:virology; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D008565:Membrane Proteins; D053830:Plant Viral Movement Proteins; D014764:Viral Proteins; D000409:Alanine