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• W76888523 abstract "Research Article1 August 1990free access Eukaryotic coupled translation of tandem cistrons: identification of the influenza B virus BM2 polypeptide. C. M. Horvath C. M. Horvath Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author M. A. Williams M. A. Williams Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author R. A. Lamb R. A. Lamb Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author C. M. Horvath C. M. Horvath Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author M. A. Williams M. A. Williams Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author R. A. Lamb R. A. Lamb Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. Search for more papers by this author Author Information C. M. Horvath1, M. A. Williams1 and R. A. Lamb1 1Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500. The EMBO Journal (1990)9:2639-2647https://doi.org/10.1002/j.1460-2075.1990.tb07446.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Previous nucleotide sequence analysis of RNA segment 7 of influenza B virus indicated that, in addition to the reading frame encoding the 248 amino acid M1 protein, there is a second overlapping reading frame (BM2ORF) of 585 nucleotides that has the coding capacity for 195 amino acids. To search for a polypeptide product derived from BM2ORF, a genetically engineered beta-galactosidase-BM2ORF fusion protein was expressed in Escherichia coli and a polyclonal rabbit antiserum was raised to the purified fusion protein. This antiserum was used to identify a polypeptide, designated BM2 protein (Mr approximately equal to 12,000), that is synthesized in influenza B virus-infected cells. To understand the mechanism by which the BM2 protein is generated from influenza B virus RNA segment 7, a mutational analysis of the cloned DNA was performed and the altered DNAs were expressed in eukaryotic cells. The expression patterns of the M1 and BM2 proteins from the altered DNAs indicate that the BM2 protein initiation codon overlaps with the termination codon of the M1 protein in an overlapping translational stop-start pentanucleotide, TAATG, and that the expression of the BM2 protein requires 5′-adjacent termination of M1 synthesis. Our data suggest that a termination-reinitiation scheme is used in translation of a bicistronic mRNA derived from influenza B virus RNA segment 7, and this strategy has some analogy to prokaryotic coupled stop-start translation of tandem cistrons. Previous ArticleNext Article Volume 9Issue 81 August 1990In this issue RelatedDetailsLoading ..." @default.
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• W76888523 date "1990-08-01" @default.
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• W76888523 title "Eukaryotic coupled translation of tandem cistrons: identification of the influenza B virus BM2 polypeptide." @default.
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• W76888523 doi "https://doi.org/10.1002/j.1460-2075.1990.tb07446.x" @default.
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