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1994-08-27
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Document 0698
DOCN M9480698
TI A stable complex between integrase and viral DNA ends mediates human
immunodeficiency virus integration in vitro.
DT 9410
AU Ellison V; Brown PO; Department of Biochemistry, Stanford University, CA
94305-5428.
SO Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7316-20. Unique Identifier
: AIDSLINE MED/94316686
AB Retroviral replication depends on integration of the viral genome into a
chromosome of the host cell. The steps in this process are orchestrated
in vivo by a large nucleoprotein complex and are catalyzed by the
retroviral enzyme integrase. Several biochemical properties of the in
vivo nucleoprotein complex were reproduced in vitro with purified
integrase of human immunodeficiency virus type 1 and model viral DNA
substrates. A stable complex between integrase and viral DNA was
detected as an early intermediate in the integration reaction. After
formation of this initial complex, the enzyme processively catalyzed the
3' end processing and strand transfer steps in the reaction. Complexes
containing only purified integrase and the model viral DNA end were
stable under a variety of conditions and efficiently used nonviral DNA
molecules as integration targets. These complexes required a divalent
cation for their formation, and their stability was highly dependent on
the 5'-terminal dinucleotide of the viral DNA, for which no functional
role has previously been defined. Thus, interactions between integrase
and the extreme ends of the viral DNA molecule may be sufficient to
account for the stability of the in vivo integration complex.
DE Base Sequence Cations, Divalent DNA
Nucleotidyltransferases/*METABOLISM DNA, Viral/*METABOLISM
HIV-1/GENETICS/*PHYSIOLOGY Molecular Sequence Data Sequence Deletion
Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. *Virus Integration
JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).