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Affinity of peptides for the nuclear location signal of the Moloney murine leukemia virus Rev protein.
The Rev protein of the Moloney murine leukemia virus (Mo-MLV) contains two nuclear localization signals (NLS) and three nuclear export signals (NES). A peptide of 35 residues of the Rev protein (amino acid residues 138-172) was shown to be able to enter nuclei of cultured cells, whereas a derivative containing two point mutations of serine to valine at both positions 155 and 159 was not able to enter. The mutation of residue 155, but not of 159, completely inhibited the affinity of the peptide to enter the nuclei. The results show that the location of amino acid residue 155 in the Rev peptide is crucial for efficient nuclear import. A deletion of four residues of amino acid residues 161-164 did not influence the nuclear localization. These results suggest that this region is not critical for the recognition by the nuclear transport machinery of the Rev protein. Furthermore, amino acid residues 140-165 of the Rev protein were divided into 14 overlapping peptides and one peptide encompassing all 14 regions
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