Alfalfa mosaic virus temperature-sensitive mutants. V. The nucleotide sequence of TBTS 7 RNA 3 shows limited nucleotide changes and evidence for heterologous recombination.

Abstract:

:Nucleotide sequence determination of the coat protein cistron of the alfalfa mosaic virus (AIMV) temperature-sensitive mutant, Tbts 7 (uv) revealed a small number of point mutations of which only one results in the replacement of an amino acid: the asparagine residue at position 126 is replaced by an aspartate residue. RNA transcribed in vitro from a Tbts 7 cDNA 4 clone directed the production in vitro of a polypeptide which shows the same altered electrophoretic mobility in SDS-polyacrylamide gels as the Tbts 7 coat protein. Nucleotide sequence analysis of the 32-kDa open reading frame revealed some base changes, but none of these lead to changes in the primary structure of the protein. The 5'-terminal sequence of Tbts 7 RNA 3 was analyzed by cDNA cloning. At least three different types of nontranslated leader sequences were found, indicating considerable heterogeneity at the 5' end of the mutant RNA 3. The results indicated that the low abundance of RNA 3-containing particles in Tbts 7 virus preparations might be due to malfunctioning of the 5' terminus of Tbts 7 RNA 3 during replication.

journal_name

Virology

journal_title

Virology

authors

Huisman MJ,Cornelissen BJ,Groenendijk CF,Bol JF,van Vloten-Doting L

doi

10.1016/0042-6822(89)90609-0

subject

Has Abstract

pub_date

1989-08-01 00:00:00

pages

409-16

issue

2

eissn

0042-6822

issn

1096-0341

journal_volume

171

pub_type

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