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A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein

Identifieur interne : 001753 ( Istex/Corpus ); précédent : 001752; suivant : 001754

A novel open reading frame in tobacco mosaic virus genome coding for a putative small, positively charged protein

Auteurs : S. Yu. Morozov ; O. N. Denisenko ; D. A. Zelenina ; O. N. Fedorkin ; A. G. Solovyev ; E. Maiss ; R. Casper ; J. G. Atabekov

Source :

RBID : ISTEX:0F853F11A62E6AE633D0180060B8AFEEC5185CA3

English descriptors

Abstract

Abstract: From sequence comparisons between the tobamovirus genomes an open reading frame (ORF-X) potentially encoding a small, positively charged protein (33- to 45-amino-acids long) was found to overlap the immediate 3′ and 5′ sides of the transport protein gene and coat protein gene, respectively. In vitro translation of the monocistronic artificial transcripts generated with T7 RNA polymerase yielded a protein of Mr 4000 (p4) and an unexpected trypsin-sensitive complex of Mr 54000 that was resistant to reduction with 2-mercaptoethanol but could be dissociated by 8 M urea. Assembly of this complex was inhibited completely by site-directed mutagenesis within a conserved, positively charged 5-amino-acid long segment of the ORF-X protein. After centrifugation in low salt buffer the 54-kDa complex remained mostly associated with ribosomes. Apparently this complex represents a specific aggregate of the p4 product of ORF-X with a protein of approximate Mr 50000 that is a component of the translation apparatus.

Url:
DOI: 10.1016/0300-9084(93)90096-B

Links to Exploration step

ISTEX:0F853F11A62E6AE633D0180060B8AFEEC5185CA3

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<abstract lang="en">Abstract: From sequence comparisons between the tobamovirus genomes an open reading frame (ORF-X) potentially encoding a small, positively charged protein (33- to 45-amino-acids long) was found to overlap the immediate 3′ and 5′ sides of the transport protein gene and coat protein gene, respectively. In vitro translation of the monocistronic artificial transcripts generated with T7 RNA polymerase yielded a protein of Mr 4000 (p4) and an unexpected trypsin-sensitive complex of Mr 54000 that was resistant to reduction with 2-mercaptoethanol but could be dissociated by 8 M urea. Assembly of this complex was inhibited completely by site-directed mutagenesis within a conserved, positively charged 5-amino-acid long segment of the ORF-X protein. After centrifugation in low salt buffer the 54-kDa complex remained mostly associated with ribosomes. Apparently this complex represents a specific aggregate of the p4 product of ORF-X with a protein of approximate Mr 50000 that is a component of the translation apparatus.</abstract>
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