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J. Biol. Chem., Vol. 275, Issue 39, 30487-30495, September 29, 2000
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From the Department of Medical Microbiology and Immunology, Texas
A&M University System Health Science Center, College Station, Texas
77843-1114
Papillomavirus E1 protein is the replication
initiator that recognizes and binds to the viral origin and initiates
DNA strand separation through its ATP-dependent helicase
activity. The E1 protein also functions in viral DNA replication by
recruiting several cellular proteins to the origin, including host DNA
polymerase
Bovine Papillomavirus E1 Protein Is Sumoylated by the Host
Cell Ubc9 Protein*
and replication protein A. To identify other
cellular proteins that interact with bovine papillomavirus E1, an HeLa
cDNA library was screened using a yeast two-hybrid assay. The host
cell sumoylating enzyme, Ubc9, was found to interact specifically with
E1 both in vitro and in vivo. Mapping studies
localized critical E1 sequences for interaction to amino acids 315-459
and strongly implicated leucine 420 as critical for E1·Ubc9
complex formation. In addition to binding E1, Ubc9 catalyzed the
covalent linkage of the ubiquitin-like protein, SUMO-1, to E1. An E1
mutant unable to bind Ubc9 showed normal intracellular stability, but
was impaired for intranuclear distribution. Failure to accumulate in
appropriate nuclear subdomains may account for the previously
demonstrated replication defect of a human papillomavirus 16 E1 protein
that was also unable to bind Ubc9 and suggests that sumoylation is a
functionally important modification with regulatory implications for
papillomavirus replication.
*
This work was supported by American Cancer Society Grant
VM-183.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.: 979-845-5207;
Fax: 979-845-3479; E-mail: v-wilson@tamu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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