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J. Biol. Chem., Vol. 275, Issue 48, 37999-38004, December 1, 2000
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From the The E1 protein is a multifunctional,
origin-binding helicase that is essential for replication of
papillomaviruses. Recently, bovine papillomavirus E1 was shown
to be post-translationally modified by the addition of the SUMO-1
polypeptide. Here we show that the site of sumoylation maps to lysine
residue 514. This lysine and the flanking sequences are well conserved
in human papillomavirus (HPV) E1 proteins. Both HPV1a and HPV18 E1
proteins are substrates for sumoylation in vitro, which is
consistent with this modification being a general property of E1
proteins. Mutations, which impair the sumoylation of bovine
papillomavirus E1, prevent normal nuclear accumulation of E1 with a
concomitant loss of replication capacity. These results suggest that
sumoylation plays a role in nuclear transport and could regulate the E1
replication function by controlling access to the nuclear replication domains.
SUMO-1 Modification of Bovine Papillomavirus E1 Protein Is
Required for Intranuclear Accumulation*
,,¶
Department of Medical Microbiology and
Immunology, College of Medicine, Texas A&M University System Health
Science Center, College Station, Texas 77843-1114 and the
§ Department of Molecular Genetics and Biochemistry,
University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania
15261
*
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.
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