Proton-Magnetic-Resonance Studies on the Coat Protein of Alfalfa Mosaic Virus

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Amino acids of alfalfa mosaic virus coat protein that direct formation of unusually long virus particles.

In contrast to most alfalfa mosaic virus (AMV) strains (YSMV, S, M and 425), AMV strains VRU and 1 5/64 can form abnormally long virus particles, an ability which has been linked to the coat protein (CP). In order to study this phenomenon, the CP-encoding RNAs 3 of AMV strains VRU and 1 5/64 were cloned and fully sequenced. Comparative sequence analyses of AMV RNA 3 sequences derived from diffe...

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Structural elements of the 3'-terminal coat protein binding site in alfalfa mosaic virus RNAs.

The 3'-terminal of the three genomic RNAs of alfalfa mosaic virus (AIMV) and ilarviruses contain a number of AUGC-motifs separated by hairpin structures. Binding of coat protein (CP) to such elements in the RNAs is required to initiate infection of these viruses. Determinants for CP binding in the 3'-terminal 39 nucleotides (nt) of AIMV RNA 3 were analyzed by band-shift assays. From the 5'- to ...

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ژورنال

عنوان ژورنال: European Journal of Biochemistry

سال: 1982

ISSN: 0014-2956,1432-1033

DOI: 10.1111/j.1432-1033.1982.tb06741.x