       Document 0273
 DOCN  M95B0273
 TI    Analysis of the nucleic acid annealing activities of nucleocapsid
       protein from HIV-1.
 DT    9511
 AU    Lapadat-Tapolsky M; Pernelle C; Borie C; Darlix JL; Unite de Virologie
       Humaine (INSERM 412), LaboRetro, Ecole; Normale Superieure de Lyon,
       France.
 SO    Nucleic Acids Res. 1995 Jul 11;23(13):2434-41. Unique Identifier :
       AIDSLINE MED/95357151
 AB    Retroviral nucleocapsid (NC) protein is an integral part of the virion
       nucleocapsid where it is in tight association with genomic RNA and the
       tRNA primer. NC protein is necessary for the dimerization and
       encapsidation of genomic RNA, the annealing of the tRNA primer to the
       primer binding site (PBS) and the initial strand transfer event. Due to
       the general nature of NC protein-promoted annealing, its use to improve
       nucleic acid interactions in various reactions can be envisioned.
       Parameters affecting NC-promoted nucleic acid annealing of NCp7 from
       HIV-1 have been analyzed. The promotion of RNA:RNA and RNA:DNA annealing
       by NCp7 is more sensitive to the concentration of MgCl2 than the
       promotion of DNA:DNA hybridization. Stimulation of complex formation for
       all three complexes was efficient at 0-90 mM NaCl, between 23 and 55
       degrees C and at pH values between 6.5 and 9.5, inclusive. Parameters
       affecting NCp7-promoted hybridization of tRNA(Lys,3) to the PBS, which
       appears to be specific for NC protein, will be discussed. Results
       implicate the basic regions of NCp7, but not the zinc fingers, in
       promoting the annealing of complementary nucleic acid sequences.
       Finally, NCp7 strand transfer activity aids the formation of the most
       stable nucleic acid complex.
 DE    Base Sequence  Capsid/*PHARMACOLOGY  DNA/*METABOLISM  Gene Products,
       gag/*PHARMACOLOGY  Hydrogen-Ion Concentration  HIV-1/*CHEMISTRY
       Magnesium Chloride/PHARMACOLOGY  Molecular Sequence Data  Nucleic Acid
       Hybridization  RNA/*METABOLISM  RNA, Transfer, Amino Acyl/METABOLISM
       Sodium Chloride/PHARMACOLOGY  Support, Non-U.S. Gov't  Temperature  Zinc
       Fingers  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

