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M9630243.TXT
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1996-02-27
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Document 0243
DOCN M9630243
TI Human immunodeficiency virus nucleocapsid protein stimulates strand
transfer from internal regions of heteropolymeric RNA templates.
DT 9603
AU DeStefano JJ; Department of Microbiology, University of Maryland,
College Park,; USA.
SO Arch Virol. 1995;140(10):1775-89. Unique Identifier : AIDSLINE
MED/96105336
AB We have examined the influence of HIV nucleocapsid protein (NCp) on
strand transfer from internal regions of a heteropolymeric RNA template.
The system consisted of a DNA-primed 225 nucleotide RNA donor template,
on which reverse transcriptase initiated primer extension, and a 189
nucleotide RNA acceptor template, to which extended primers could
transfer. The last 133 nucleotides on the 3' end of the acceptor were
homologous to an internal region on the donor, limiting homologous
strand transfer to this region. Primers extended to the end of the donor
were 212 nucleotides while those transferred to, and extended on the
acceptor were 259 nucleotides in length. The rate of strand transfer and
the level of transfer products increased several-fold when nucleocapsid
was included in the reactions. The increase was due, at least in part,
to the transfer to, and extension on the acceptor, of incompletely
elongated primer-extension products that were chased into transfer
products in the presence of nucleocapsid. Nucleocapsid did not directly
influence reverse transcriptase elongation as the enzyme processivity
(number of nucleotides incorporated before the enzyme dissociates from
the primer-template) was approximately the same in the presence and
absence of nucleocapsid.
DE Capsid/*METABOLISM Cell-Free System DNA, Viral/METABOLISM Gene
Products, gag/*METABOLISM HIV-1/*GENETICS Recombinant Proteins
RNA-Directed DNA Polymerase/METABOLISM RNA, Viral/*METABOLISM Support,
U.S. Gov't, P.H.S. Templates *Virus Replication JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).