Activation of the herpes simplex virus type-1 origin-binding protein (UL9) by heat shock proteins

Nicolas Tanguy Le Gac, Paul E Boehmer

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Heat shock proteins participate in the initiation of DNA replication of different organisms by facilitating the assembly of initiation complexes. We have examined the effects of human heat shock proteins (Hsp40 and Hsp70) on the interaction of the herpes simplex virus type-1 initiator protein (UL9) with oriS, one of the viral origins of replication. Hsp40 and Hsp70 act substoichiometrically to increase the affinity of UL9 for oriS. The major contributor to this effect is Hsp40. Heat shock proteins also stimulate the ATPase activity of UL9 with oriS and increase opening of the origin. In contrast, heat shock proteins have no effect on the origin-independent activities of UL9 suggesting that their role is not merely in refolding denatured protein. These observations are consistent with a role for heat shock proteins in activating UL9 to efficiently initiate viral origin-dependent DNA replication. The action of heat shock proteins in this capacity is analogous to their role in activating the initiator proteins of other organisms.

Original languageEnglish (US)
Pages (from-to)5660-5666
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number7
DOIs
StatePublished - Feb 15 2002
Externally publishedYes

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Human Herpesvirus 1
Heat-Shock Proteins
Chemical activation
DNA Replication
Protein Refolding
Proteins
Replication Origin
DNA
Viruses
Adenosine Triphosphatases
Human herpesvirus 1 UL9 protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

Activation of the herpes simplex virus type-1 origin-binding protein (UL9) by heat shock proteins. / Le Gac, Nicolas Tanguy; Boehmer, Paul E.

In: Journal of Biological Chemistry, Vol. 277, No. 7, 15.02.2002, p. 5660-5666.

Research output: Contribution to journalArticle

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