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dc.contributor.authorBostian, Keith A.
dc.contributor.authorSturgeon, Joyce A.
dc.contributor.authorTipper, Donald J.
dc.date2022-08-11T08:09:18.000
dc.date.accessioned2022-08-23T16:26:03Z
dc.date.available2022-08-23T16:26:03Z
dc.date.issued1980-07-01
dc.date.submitted2019-06-17
dc.identifier.citation<p>J Bacteriol. 1980 Jul;143(1):463-70.<a href="https://jb.asm.org/content/143/1/463" target="_blank" title="Link to article on publisher's site"> Link to article on publisher's site</a></p>
dc.identifier.issn0021-9193 (Linking)
dc.identifier.pmid6995444
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36481
dc.description.abstractVirus-like particles containing either L or M double-stranded ribonucleic acid (dsRNA) were isolated from a killer toxin-producing strains of Saccharomyces cerevisiae (K+ R+). At least 95% of M- and 87% of L-dsRNA were recovered in virus-like particle-containing fractions. The major capsid polypeptides (ScV-P1) of both L and M virus-like particles were shown to be identical, and 95% of the cellular ScV-P1 was found in the virus-like particle-containing fractions. Since L-dsRNA encodes ScV-P1, provision of this protein for encapsidation of M-dsRNA defines at least one functional relationship between these dsRNA genomes and associates the L-dsRNA with the killer character. If encapsidation of M-dsRNA is essential for its replication or expression, then L-dsRNA plays an essential role in maintenance or expression of the killer phenotype. The relationship between the L- and M-dsRNA genomes would be analogous to that between a helper and a defective virus. The presence of only minor quantities or uncomplexed dsRNA and ScV-P1 suggests that their production is stringently coupled.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=6995444&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 1980, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at https://journals.asm.org/content/copyright-transfer-and-supplemental-material-license-agreement-2017.
dc.subjectyeast
dc.subjectSaccharomyces cerevisiae
dc.subjectdsRNA
dc.subjectBacteriology
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectPhysiology
dc.titleEncapsidation of yeast killer double-stranded ribonucleic acids: dependence of M on L
dc.typeJournal Article
dc.source.journaltitleJournal of bacteriology
dc.source.volume143
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1044&amp;context=maps_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/44
dc.identifier.contextkey14751696
refterms.dateFOA2022-08-23T16:26:03Z
html.description.abstract<p>Virus-like particles containing either L or M double-stranded ribonucleic acid (dsRNA) were isolated from a killer toxin-producing strains of Saccharomyces cerevisiae (K+ R+). At least 95% of M- and 87% of L-dsRNA were recovered in virus-like particle-containing fractions. The major capsid polypeptides (ScV-P1) of both L and M virus-like particles were shown to be identical, and 95% of the cellular ScV-P1 was found in the virus-like particle-containing fractions. Since L-dsRNA encodes ScV-P1, provision of this protein for encapsidation of M-dsRNA defines at least one functional relationship between these dsRNA genomes and associates the L-dsRNA with the killer character. If encapsidation of M-dsRNA is essential for its replication or expression, then L-dsRNA plays an essential role in maintenance or expression of the killer phenotype. The relationship between the L- and M-dsRNA genomes would be analogous to that between a helper and a defective virus. The presence of only minor quantities or uncomplexed dsRNA and ScV-P1 suggests that their production is stringently coupled.</p>
dc.identifier.submissionpathmaps_pubs/44
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages463-70


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