Functional significance of three basic N-terminal amino acids of alfalfa mosaic virus coat protein.
Infection of tobacco protoplasts with mutant alfalfa mosaic virus (AMV) RNAs indicated that three basic amino acids in the N-terminus of AMV coat protein are important for the biological activity of the coat protein in the beginning of infection. Substitution of alanines for lysines at position 14 or 17 in the coat protein resulted in a 5- or 10-fold reduction in the activity of the protein, respectively. However, substitution of alanine for arginine at position 18 entirely abolished activity. Arginine 18 was also required for the coat protein to bind to the 3' noncoding region of the virus RNA in vitro, whereas lysine 14 or 17 was not required. Thus, these results indicate that arginine 18 is essential for the activity of the coat protein in early infection and that binding of the coat protein to AMV RNA correlates with activity.
Yusibov
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Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907, USA.
Loesch-Fries
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D017794:Alfalfa mosaic virus / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000096:biosynthesis / Q000737:chemistry*; D003001:Cloning, Molecular; D017931:DNA Primers; D008969:Molecular Sequence Data; D010947:Plants, Toxic; D010957:Plasmids; D014176:Protein Biosynthesis; D011523:Protoplasts; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014026:Nicotiana; D014158:Transcription, Genetic
D017931:DNA Primers; D011994:Recombinant Proteins