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J. Biol. Chem., Vol. 278, Issue 18, 15702-15712, May 2, 2003
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From the Department of Cell Biology and Molecular Genetics,
University of Maryland, College Park, Maryland 20742
An in vitro strand transfer
assay that mimicked recombinational events occurring during reverse
transcription in HIV-1 was used to assess the role of nucleocapsid
protein (NC) in strand transfer. Strand transfer in highly structured
nucleic acid species from the U3 3' long terminal repeats,
gag-pol frameshift region, and Rev response element were
strongly enhanced by NC. In contrast, weakly structured templates from
the env and pol-vif regions transferred well
without NC and showed lower enhancement. The lack of strong polymerase
pause sites in the latter regions demonstrated that non-pause driven
mechanisms could also promote transfer. Assays conducted using NC zinc
finger mutants supported a differential role for the two fingers in
strand transfer with finger 1 (N-terminal) being more important on
highly structured RNAs. Overall this report suggests a role for
structural intricacies of RNA templates in determining the extent of
influence of NC on recombination and illustrates that strand transfer
may occur by several different mechanisms depending on the structural
nature of the RNA.
Evidence for the Differential Effects of Nucleocapsid Protein on
Strand Transfer in Various Regions of the HIV Genome*
*
This work was supported by NIGMS, National Institutes of
Health Grant GM51140.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: Dept. of Cell Biology
and Molecular Genetics, University of Maryland, Bldg. 231, College
Park, MD 20742. Tel.: 301-405-5449; Fax: 301-314-9489; E-mail:
jd146@umail.umd.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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