HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Constantin, N. Articles by Dodson, M. S. Search for Related Content PubMed PubMed Citation Articles by Constantin, N. Articles by Dodson, M. S. Agricola Articles by Constantin, N. Articles by Dodson, M. S.

Two-hybrid analysis of the interaction between the UL52 and UL8 subunits of the herpes simplex virus type 1 helicase–primase

Department of Biochemistry, University of Arizona, Biological Sciences West Building, 1041 E. Lowell Street, Tucson, AZ 85721-0088, USA¹

Author for correspondence: Mark Dodson.Fax +1 520 621 9288. e-mail dodson{at}u.arizona.edu

Herpes simplex virus type 1 expresses a heterotrimeric helicase–primase, the subunits of which are encoded by the viral UL5, UL8 and UL52 genes. The interactions of the UL52 protein with the UL8 and UL5 proteins were analysed by using the yeast two-hybrid system. The UL52–UL5 interaction gave a specific but weak signal in the two-hybrid system. In contrast, the UL52–UL8 interaction gave a strong signal in the two-hybrid system. Deletion analysis showed that a 548 amino acid fragment of UL52 (amino acids 366–914) retains the ability to interact with UL8 and that the N-terminal 349 amino acids are dispensable for the interaction. A fragment library screen and co-immunoprecipitation experiments confirmed the deletion analysis results.