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dc.contributor.authorBostian, Keith A.
dc.contributor.authorHopper, James E.
dc.contributor.authorRogers, Davis T.
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.issued1980-02-01
dc.date.submitted2019-06-17
dc.identifier.citation<p>Cell. 1980 Feb;19(2):403-14.<a href="https://doi.org/10.1016/0092-8674(80)90514-0" target="_blank" title="Link to article on publisher's website"> Link to article on publisher's website</a></p>
dc.identifier.issn0092-8674 (Linking)
dc.identifier.doi10.1016/0092-8674(80)90514-0
dc.identifier.pmid6986991
dc.identifier.urihttp://hdl.handle.net/20.500.14038/36480
dc.description.abstractThe M species (medium sized) dsRNA (1.1-1.4 x 10(6) daltons) isolated from a toxin-producing yeast killer strain (K+R+) and three related, defective interfering (suppressive) S species dsRNAs of the yeast killer-associated cytoplasmic multicomponent viral-like particle system were analyzed by in vitro translation in a wheat germ cell-free protein synthesis system. Heat-denatured M species dsRNA programmed the synthesis of two major polypeptides, M-P1 (32,000 daltons) and M-P2 (30,000 daltons). M-P1 has been shown by the criteria of proteolytic peptide mapping and cross-antigenicity to contain ihe 12,000 dalton polypeptide corresponding to the in vivo produced killer toxin, thus establishing thiat it is the M species dsRNA which carries the toxin gene. An M species dsRNA obtained from a neutral strain (K-R+) also programmed the in vitro synthesis of a polypeptide identical in molecular weight to M-P1, thus indicating that the cytoplasmic determinant of the mutant neutral phenotype is either a simple point mutation in the dsRNA toxin gene or a mutation in a dsRNA gene which is required for functional toxin production. In vitro translation of each of the three different suppressive S dsRNAs resulted in the production of a polypeptide (S-P1) of approximately 8000 daltons instead of the 32,000 dalton M-P1 polypeptide programmed by M dsRNA. This result is consistent with the heteroduplex analysis of these dsRNAs by Fried and Fink (1978), which shows retention of M dsRNA ends, accompanied by large internal deletions in each of the S dsRNAs translated.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=6986991&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1016/0092-8674(80)90514-0
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectMicrobiology
dc.subjectPhysiology
dc.titleTranslational analysis of the killer-associated virus-like particle dsRNA genome of S. cerevisiae: M dsRNA encodes toxin
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume19
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/maps_pubs/43
dc.identifier.contextkey14751695
html.description.abstract<p>The M species (medium sized) dsRNA (1.1-1.4 x 10(6) daltons) isolated from a toxin-producing yeast killer strain (K+R+) and three related, defective interfering (suppressive) S species dsRNAs of the yeast killer-associated cytoplasmic multicomponent viral-like particle system were analyzed by in vitro translation in a wheat germ cell-free protein synthesis system. Heat-denatured M species dsRNA programmed the synthesis of two major polypeptides, M-P1 (32,000 daltons) and M-P2 (30,000 daltons). M-P1 has been shown by the criteria of proteolytic peptide mapping and cross-antigenicity to contain ihe 12,000 dalton polypeptide corresponding to the in vivo produced killer toxin, thus establishing thiat it is the M species dsRNA which carries the toxin gene. An M species dsRNA obtained from a neutral strain (K-R+) also programmed the in vitro synthesis of a polypeptide identical in molecular weight to M-P1, thus indicating that the cytoplasmic determinant of the mutant neutral phenotype is either a simple point mutation in the dsRNA toxin gene or a mutation in a dsRNA gene which is required for functional toxin production. In vitro translation of each of the three different suppressive S dsRNAs resulted in the production of a polypeptide (S-P1) of approximately 8000 daltons instead of the 32,000 dalton M-P1 polypeptide programmed by M dsRNA. This result is consistent with the heteroduplex analysis of these dsRNAs by Fried and Fink (1978), which shows retention of M dsRNA ends, accompanied by large internal deletions in each of the S dsRNAs translated.</p>
dc.identifier.submissionpathmaps_pubs/43
dc.contributor.departmentDepartment of Microbiology and Physiological Systems
dc.contributor.departmentDepartment of Microbiology
dc.source.pages403-14


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