Nucleic Acids Research, 1993, Vol. 21, No. 4 823-829
© 1993
MOLECULAR BIOLOGY |
Two short basic sequences surrounding the zinc finger of nucleocapsid protein NCp10 of Moloney murine leukemia virus are critical for RNA annealing activity
Unite de Pharmacochimie moléculaire et structurale, U266 INSERM, URA D1500 CNRS, Université René Descartes 4, Avenue de I'Observatoire, 75270 Paris cedex 06 1Laboretro INSERM, Ecole Normale Supérieure de Lyon 46, allée d'Italie, 69364 Lyon, France
*To whom correspondence should be addressed
Received December 17, 1992. Revised January 22, 1993. Accepted January 22, 1993.
The 56 amino acid nucieocapsid protein (NCp10) of Moioney Murine Leukemia Virus, contains a CysX2CysX4HlsX4Cys zinc finger flanked by basic residues. In vitro NCp10 promotes genomic RNA dimerization, a process most probabiy linked to genomic RNA packaging, and replication primer tRNAPro annealing to the initiation site of reverse transcription. To characterize the amino-acid sequences involved in the various functions of NCp10, we have synthesized by solid phase method the native protein and a series of derived peptides shortened at the N- or C-terminus with or without the zinc finger domain. In the latter case, the two parts of the protein were iinked by a Glycine - Giycine spacer. The in vitro studies of these peptides show that nucleic acid annealing activities of NCp10 do not require a zinc finger but are critically dependent on the presence of specific sequences located on each side of the CCHC domain and containing proline and basic residues. Thus, deletion of 11R or 49PRPQT, of the fully active 29 residue peptide 11RQGGERRRSQLDRDGGKKPRGPRGPRPQT53 leads to a complete loss of NCp10 activity. Therefore it is proposed that in NCp10, the zinc finger directs the spatial recognition of the target RNAs by the basic domains surrounding the zinc finger.
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