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M9490412.TXT
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1994-09-19
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Document 0412
DOCN M9490412
TI DNA strand exchange and selective DNA annealing promoted by the human
immunodeficiency virus type 1 nucleocapsid protein.
DT 9411
AU Tsuchihashi Z; Brown PO; Howard Hughes Medical Institute, Standford,
California.
SO J Virol. 1994 Sep;68(9):5863-70. Unique Identifier : AIDSLINE
MED/94335103
AB Nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1)
was expressed in Escherichia coli and purified. The protein displayed a
variety of activities on DNA structure, all reflecting an ability to
promote transition between double-helical and single-stranded
conformations. We found that, in addition to its previously described
ability to accelerate renaturation of complementary DNA strands, the
HIV-1 NC protein could substantially lower the melting temperature of
duplex DNA and could promote strand exchange between double-stranded and
single-stranded DNA molecules. Moreover, in the presence of HIV-1 NC,
annealing of a single-stranded DNA molecule to a complementary DNA
strand that would yield a more stable double-stranded product was
favored over annealing to alternative complementary DNA strands that
would form less stable duplex products (selective annealing). NC thus
appears to lower the kinetic barrier so that double-strand <==>
single-strand equilibrium is rapidly reached to favor the lowest
free-energy nucleic acid conformation. This activity of NC may be
important for correct folding of viral genomic RNA and may have
practical applications.
DE Base Sequence *Capsid DNA/*CHEMISTRY DNA-Binding Proteins/*PHYSIOLOGY
Gene Products, gag/*PHYSIOLOGY HIV-1/*GENETICS In Vitro Molecular
Sequence Data Nucleic Acid Conformation Nucleic Acid Denaturation
Nucleic Acid Renaturation Oligodeoxyribonucleotides/CHEMISTRY
Recombinant Proteins Support, Non-U.S. Gov't Support, U.S. Gov't,
P.H.S. Thermodynamics JOURNAL ARTICLE
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).