Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids.

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Research Abstract Details 

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Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Abstract Text:

Benes L Trus,William W Newcomb,Naiqian Cheng,Giovanni Cardone,Lyuben Marekov,Fred L Homa,Jay C Brown,Alasdair C Steven,

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.

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Publishing Authors By Initials

BL Trus,WW Newcomb,N Cheng,G Cardone,L Marekov,FL Homa,JC Brown,AC Steven,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Molecular cell

VOLUME: 26

Page Numbers: 479-89

Journal Abbreviation: Mol. Cell

ISSN: 1097-2765

DAY: 25

MONTH: May

YEAR: 2007

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Information

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LANGUAGE: eng

NlmUniqueID: 9802571

Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Information

Substance Name: DNA cleavage and packaging proteins, Her

Registry Number: 139381-88-7

Grant and Affiliation Information for Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids.

AFFILIATION: Laboratory of Structural Biology Research, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Country: United States

AGENCY: United States NIAMS

GRANT: Z01 AR027002-29

ACRONYM: AR

MEDLINETA: Mol Cell

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