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Crystallisation of the Herpes Simplex Virus single-stranded DNA binding protein Scientific report

By M. Mapelli, M. Muehleisen, H. Van der Zandt, P.A. Tucker and Heidelberg (Germany) Europaeisches Lab. fuer Molekularbiologie

Abstract

ICP8, the UL29 gene product of Herpes Simplex Virus 1, is a 128KDa nuclear zinc metalloprotein. Genetic studies have shown it plays a key role during the viral lytic phase, mainly by virtue of its ability to bind single-stranded DNA (ssDNA) and to mediate several protein-protein interactions. ICP8 is one of the seven beta gene products required for origin dependent replication of the viral DNA, together with an origin binding protein (OBP), a polymerase with its processivity factor and a heterotrimeric helicase-primase complex [1]. ICP8 localizes to discrete nuclear domains, termed prereplication compartments, possibly driving the organization of the whole replication machinery. During initiation, the concerted action of ICP8 and the OBP catalyzes and stabilizes the unwinding of double-stranded DNA. ICP8 [2,3] also stimulates the activity of the viral DNA polymerase and optimizes the activities of the helicase-primase complex, most likely through an interaction with one of the subunits of the complex. (orig.)Available from TIB Hannover: DtF QN1(83,32) / FIZ - Fachinformationszzentrum Karlsruhe / TIB - Technische InformationsbibliothekSIGLEBundesministerium fuer Bildung und Forschung (BMBF), Bonn (Germany)DEGerman

Topics: 06V - Genetics, cytology, molecular biology
Year: 1999
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Provided by: OpenGrey Repository
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