In:
Journal of Virology, American Society for Microbiology, Vol. 59, No. 1 ( 1986-07), p. 50-58
Abstract:
The bottom-component RNA (B-RNA) of cowpea mosaic virus is expressed by the production of a ∼200,000-dalton polyprotein (200K polyprotein), from which the functional proteins are formed by specific proteolytic cleavages. Partial amino-terminal sequences of the various B-RNA-encoded proteins have now been determined. Comparison of the information obtained with the B-RNA sequence allowed the localization of the coding regions for these proteins on B-RNA, the calculation of their precise molecular weights, and the determination of the cleavage sites at which they are released from the polyprotein precursor. Sequence analysis of the 32K protein, which is derived from the amino-terminal end of the 200K polyprotein, indicated that the AUG codon at nucleotide position 207 of the RNA sequence is the translation initiation codon. Sequence analysis of the 170K, 110K, 87K, 84K, 60K, and 58K proteins revealed the existence of three types of cleavage site in the 200K polyprotein: glutamine-serine (two sites), glutamine-methionine (one site), and glutamine-glycine (one site) amino acid pairs. The nature of these cleavage sites suggested that two different viral proteases are involved in the processing of the B-RNA-encoded polyprotein.
Type of Medium:
Online Resource
ISSN:
0022-538X
,
1098-5514
DOI:
10.1128/jvi.59.1.50-58.1986
Language:
English
Publisher:
American Society for Microbiology
Publication Date:
1986
detail.hit.zdb_id:
1495529-5
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