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Two forms of the major barley stripe mosaic virus nonstructural protein are synthesized in vivo from alternative initiation codons.

Abstract：

:Barley stripe mosaic virus (BSMV) has a tripartite genome comprising RNAs designated alpha, beta, and gamma, which collectively encode seven polypeptides. We show here that an antiserum raised against an abundant disease-specific protein from BSMV-infected plants reacts specifically with the viral beta b gene product expressed as part of a beta-galactosidase fusion protein in Escherichia coli. Two predominant forms of the protein, beta b and beta b', are synthesized in vivo. Infectious in vitro transcripts derived from wild-type and mutant BSMV cDNA clones have been used to map the initiation site for translation of the beta b protein in vivo. The results of our mutagenesis experiments are consistent with a model in which translation of the beta b' protein is initiated by ribosomes that scan past the 5'-proximal beta b initiation site. A mutant which is able to synthesize only the shorter beta b' protein was indistinguishable from the wild-type with respect to all of the phenotypes tested. Thus, the beta b form of the protein is dispensable in planta, and whether the two forms of the protein have different functions in vivo is unclear at present.

journal_name

Virology

journal_title

Virology

authors

Petty IT,Jackson AO

doi

10.1016/0042-6822(90)90559-a

subject

Has Abstract

pub_date

1990-08-01 00:00:00

pages

829-32

issue

2

eissn

0042-6822

issn

1096-0341

journal_volume

177

pub_type

杂志文章

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