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Article

The C-terminal part of the human cytomegalovirus terminase subunit pUL51 is central for terminase complex assembly.

The Journal of general virology - 1 Jan 2018

Neuber Sebastian, Wagner Karen, Messerle Martin, Borst Eva Maria

Abstract excerpt

The cleavage and packaging of the human cytomegalovirus (HCMV) genome is accomplished by the viral terminase, comprising pUL56 and pUL89, and the recently identified pUL51 subunit. Since knowledge about pUL51 is scarce, we aimed at identifying pUL51 domains that are important for terminase assembly. In silico analysis suggested that the N-terminal half of pUL51 is intrinsically disordered, and that α-helices are...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 29205134
DOI: 10.1099/jgv.0.000984

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The C-terminal part of the human cytomegalovirus terminase subunit pUL51 is central for terminase complex assembly.PMID 29205134Read ↗

The Human Cytomegalovirus UL51 Protein Is Essential for Viral Genome Cleavage-Packaging and Interacts with the Terminase Subunits pUL56 and pUL89Semantic proximity Read ↗

Mutual Interplay between the Human Cytomegalovirus Terminase Subunits pUL51, pUL56, and pUL89 Promotes Terminase Complex FormationSemantic proximity Read ↗

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Identification of a short sequence in the HCMV terminase pUL56 essential for interaction with pUL89 subunitSemantic proximity Read ↗

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Interaction of human cytomegalovirus pUL52 with major components of the viral DNA encapsidation network underlines its essential role in genome cleavage-packagingSemantic proximity Read ↗

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