期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 8, 页码 5829-5835出版社
ELSEVIER
DOI: 10.1074/jbc.M008547200
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资金
- NIGMS NIH HHS [GM39068] Funding Source: Medline
Cells infected by herpes simplex virus type 1 in the G(2) phase of the cell cycle become stalled at an unusual stage of mitosis defined as pseudoprometaphase, This block correlates with the viral immediate-early protein ICP0-induced degradation of the centromere protein CENP-C. However, the observed pseudoprometaphase phenotype of infected mitotic cells suggests that the stability of other centromere proteins may also be affected. Here, we demonstrate that ICP0 also induces the proteasome-dependent degradation of the centromere protein CENP-A. By a series of Western blot and immunofluorescence experiments we show that the endogenous 17-kDa CENP-A and an exogenous tagged version of CENP A are lost from centromeres and degraded in infected and transfected cells as a result of ICP0 expression. CENP-A is a histone H3-like protein associated with nucleosome structures in the inner plate of the kinetochore. Unlike fully transcribed lytic viral DNA, the transcriptionally repressed latent herpes simplex virus type 1 genome has been reported to have a nucleosomal structure similar to that of cellular chromatin, Because ICP0 plays an essential part in controlling the balance between the lytic and latent outcomes of infection, the ICP0-induced degradation of CENP-A is an intriguing feature connecting different aspects of viral and/or cellular genome regulation.
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