STRIKING SIMILARITIES IN AMINO-ACID-SEQUENCE AMONG NONSTRUCTURAL PROTEINS ENCODED BY RNA VIRUSES THAT HAVE DISSIMILAR GENOMIC ORGANIZATION
STRIKING SIMILARITIES IN AMINO-ACID-SEQUENCE AMONG NONSTRUCTURAL PROTEINS ENCODED BY RNA VIRUSES THAT HAVE DISSIMILAR GENOMIC ORGANIZATION
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DOI:
10.1073/pnas.81.14.4358
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发表时间:
1984-01-01
期刊:
影响因子:
--
通讯作者:
KAESBERG, P
中科院分区:
文献类型:
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作者:
HASELOFF, J;GOELET, P;KAESBERG, P
The plant viruses alfalfa mosaic virus (AMV) and brome mosaic virus (BMV) each divide their genetic information among 3 RNA while tobacco mosaic virus (TMV) contains a single genomic RNA. Amino acid sequence comparisons suggest that the single proteins encoded by AMV RNA 1 and BMV RNA 1 and by AMV RNA 2 and BMV RNA 2 are related to the NH2-terminal 2/3 and the COOH-terminal 1/3, respectively, of the largest protein encoded by TMV. Separating these 2 domains in the TMV RNA sequence is an amber termination codon, whose partial suppression allows translation of the downstream domain. Many of the residues that the TMV read-through domain and the segmented plant viruses have in common are also conserved in a read-through domain found in the nonstructural polyprotein of the animal alphaviruses Sindbis and Middelburg. Despite substantial differences in gene organization and expression, all of these viruses appear to use related proteins for common functions in RNA replication. Reassortment of functional modules of coding and regulatory sequence from preexisting viral or cellular sources, perhaps via RNA recombination, may be an important mechanism in RNA virus evolution.