Nucleic Acids Research, 1995, Vol. 23, No. 13 2434-2441
© 1995
MOLECULAR BIOLOGY |
Analysis of the nucleic acid annealing activites of nucleocapsid protein from HIV-1
Unité de Vircologie Humanine (INSERM 412),LaboRétro,Ecole Normale Supérieure de Lyon 46, Allée D'Italie, 69364 Lyon Cedex 07, France 1Rhone-Poulenic Rorer, Research and Development 13 Quai JUles Guesde, BP 14, 94403 Vitry-sur-Seine Cedex, France
*To whom corespondence should be addressed
Received April 5, 1995. Accepted May 24, 1995.
Retrovlral 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 encapsldation 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 MgCI2 than the promotion of DNA:DNA hybridization. Stimulation of complex formation for all three complexes was efficient at 0-90 mM NaCI, between 23 and 55°C and at pH values between 6.5 and 9.5, inclusive. Parameters affecting NCp7-promoted hybridization of tRNALys,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.
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