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Characterization of a nuclear localization sequence in the polyomavirus capsid protein VP1.

作者信息

Moreland R B, Garcea R L

机构信息

Division of Pediatric Oncology, Dana-Farber Cancer Institute, Children's Hospital, Boston, Massachusetts 02115.

出版信息

Virology. 1991 Nov;185(1):513-8. doi: 10.1016/0042-6822(91)90811-o.

DOI:10.1016/0042-6822(91)90811-o
PMID:1656604
Abstract

Expression of VP1-beta-galactosidase fusion proteins in the yeast Saccharomyces cerevisiae was used to identify a domain of the polyomavirus VP1 capsid protein which targets this protein to the nucleus. Fusion of the first 17 amino acids of VP1 to beta-galactosidase was sufficient for nuclear localization, whereas fusion of the first 12 amino acids gave a "mixed" cytoplasmic-nuclear phenotype. Mutation of a putative targeting sequence MAPKR(5)K from R to S changed the localization of a 21 amino acid fusion protein from the nucleus to cytoplasm. These results define a nuclear location signal in the amino terminus of polyomavirus VP1 and separate this function from the high-affinity DNA binding function previously defined for this region.

摘要

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