| RNA-protein interactions are essential for the life cycle of alfalfa mosaic virus (AlMV), a plant virus with a tripartite, single-stranded RNA genome of positive-polarity. The coat protein (CP) binds specifically to homologous sequences found at the 3;Hydroxyl radical footprinting data indicated that five sites in the 3;Site-directed mutagenesis and in vitro genetic selection were used to investigate the role of the AUGC motifs in specific AlMV CP and peptide recognition. Substituting AAAA for the middle AUGC sequence in AlMV;To identify additional RNA determinants required for coat protein binding, I screened a pool of 39-nucleotide RNAs of random sequence using in vitro genetic selection. From a theoretical pool of 10;The data presented in this thesis: (1) identify a minimal RNA binding site for AlMV CP and peptides, (2) demonstrate the importance of tetranucleotide AUGC elements for specific RNA-protein/peptide interactions, (3) contribute toward defining an RNA-protein complex suitable for high-resolution structural analysis, and (4) suggest strategies for inhibiting the viral life cycle that may have practical application for crop protection. |
