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postdoctoral position in HSV

weller weller at PANDA.UCHC.EDU
Thu Jun 6 11:45:18 EST 1996

Postdoctoral position available.  Herpes Simplex Virus DNA Replication.  

A postdoctoral research position is available with Dr. Sandra K. Weller 
in the Department of Microbiology, University of Connecticut School of 
Medicine, Farmington Connecticut.  This research is funded by a 5-year 
NIH grant to study DNA replication in Herpes Simplex Virus type 1.  
Specifically we are in the process of carrying out structure-function 
analyses of two viral helicases: UL9, a multifunctional protein of HSV-1 
which exhibits origin specific DNA binding, dimer formation, helicase 
and ATPase activities and UL5 a subunit of a heterotrimeric 
helicase-primase composed of the products of the UL5, UL52, and UL8 
genes.  The helicase/primase exhibits ATPase, ss and ds DNA binding, 
helicase and primase activities.  Both UL9 and UL5 contain six sequence 
motifs found in DNA and RNA helicases of superfamilies I and II.  Motifs 
I and II comprise an NTP binding site consensus sequence; however, the 
role(s) of the other helicase motifs are unknown for any helicase.  
Single amino acid substitutions created in each motif abolish the 
ability of UL5 and UL9 to support viral DNA replication in vivo  [Zhu, 
L. and Weller, S.K. (1992) J. Virol. 66: 469; Martinez et al. (1992) J. 
Virol. 66:6735].  Wild-type UL5 and several motif variant proteins have 
been individually overexpressed and purified from a recombinant 
baculovirus system (Graves-Woodward, K. L. and Weller, S. K. (1996) J. 
Biol. Chem., 271:13629; Graves-Woodward K.L. and Weller, S.K. (1996) J. 
Biol. Chem. in preparation).  Future projects include further 
structure-function analysis of both UL9 and the helicase/primase.  For 
instance, UL52 which specifies the primase of the heterotrimeric complex 
contains a zinc finger domain, and we wish to determine the role of this 
domain in primase activity, ss and ds DNA binding and helicase activity 
of the complex.  Other lines of investigation in the laboratory involve 
analysis of the structure of replicating viral DNA, intranuclear 
localization of viral replication proteins and protein-protein 
interactions with viral and cellular proteins.  The successful applicant 
will have experience with protein biochemistry.  Preference will be 
given to applicants who also have experience with molecular biology 
and/or virology, but this is not necessary.  The starting dates and 
salaries are flexible;  the latter depends on experience. Benefits are 
provided.  Interested applicants should fax or e-mail a CV including 
names and contact addresses of 3 referees to: Dr. Sandra K. Weller, 
Professor of Microbiology, MC3205, University of Connecticut Health 
Center, 263 Farmington Ave., Farmington, CT 06030.  Fax: (860) 679-1239.  
Weller at panda.uchc.edu.  

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