期刊
MOLECULAR CELL
卷 26, 期 4, 页码 479-489出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.04.010
关键词
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资金
- Intramural NIH HHS [Z01 CT000090-27, Z99 AR999999, Z01 AR027002-29] Funding Source: Medline
- NIAID NIH HHS [R01 AI060836, R56 AI060836, R56 AI041644, AI060836, AI41644-10, R01 AI041644-10, R01 AI041644, R01 AI060836-02] Funding Source: Medline
UL25 and UL17 are two essential minor capsid proteins of HSV-1, implicated in DNA packaging and capsid maturation. We used cryo-electron microscopy to examine their binding to capsids, whose architecture observes T = 16 icosahedral geometry. C-capsids (mature DNA-filled capsids) have an elongated two-domain molecule present at a unique, vertex-adjacent site that is not seen at other quasiequivalent sites or on unfilled capsids. Using SDS-PAGE and mass spectrometry to analyze wild-type capsids, UL25 null capsids, and denaturant-extracted capsids, we conclude that (1) the C-capsid-specific component is a heterodimer of UL25 and UL17, and (2) capsids have additional populations of UL25 and UL17 that are invisible in reconstructions because of sparsity and/or disorder. We infer that binding of the ordered population reflects structural changes induced on the outer surface as pressure builds up inside the capsid during DNA packaging. Its binding may signal that the C-capsid is ready to exit the nucleus.
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