Identification of C-terminal amino acid residues of cauliflower mosaic virus open reading frame III protein responsible for its DNA binding activity.
We cloned in Escherichia coli truncated versions of the protein p15 encoded by open reading frame III of cauliflower mosaic virus. We then compared the ability of the wild-type p15 (129 amino acids) and the deleted p15 to bind viral double-stranded DNA genome. Deletions of > 11 amino acids in the C-terminal proline-rich region resulted in loss of DNA binding activity of wild-type p15. Moreover, a point mutation of the proline at position 118 sharply reduced the interaction between the viral protein and DNA. These results suggest that cauliflower mosaic virus p15 belongs to the family of DNA binding proteins having a proline-rich motif involved in interaction with double-stranded DNA.
Mougeot
J L
JL
Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique, Université Louis Pasteur, Strasbourg, France.
Guidasci
T
T
Wurch
T
T
Lebeurier
G
G
Mesnard
J M
JM
D000595:Amino Acid Sequence; D001665:Binding Sites; D001937:Brassica; D003062:Codon / Q000235:genetics; D004279:DNA, Viral / Q000235:genetics; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D016679:Genome, Viral; D008969:Molecular Sequence Data; D009029:Mosaic Viruses / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D016366:Open Reading Frames; D010957:Plasmids; D011392:Proline; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000235:genetics* / Q000378:metabolism*; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism
D003062:Codon; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; D011392:Proline; D001616:beta-Galactosidase