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).