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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) - ΙΑΤ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/20512
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dc.contributor.authorGeorgatos, S. D.en
dc.contributor.authorMaroulakou, I.en
dc.contributor.authorBlobel, G.en
dc.date.accessioned2015-11-24T19:08:16Z-
dc.date.available2015-11-24T19:08:16Z-
dc.identifier.issn0021-9525-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20512-
dc.rightsDefault Licence-
dc.subjectAnimalsen
dc.subjectCell Fractionationen
dc.subjectCell Nucleus/*ultrastructureen
dc.subjectCytoplasm/immunologyen
dc.subjectImmunoblottingen
dc.subjectLamin Type Aen
dc.subjectLamin Type Ben
dc.subjectLaminsen
dc.subjectMolecular Weighten
dc.subjectNuclear Envelope/immunology/*metabolismen
dc.subjectNuclear Proteins/*immunology/metabolismen
dc.subjectReceptors, Cell Surface/*immunology/metabolismen
dc.subjectSaccharomyces cerevisiae/*physiologyen
dc.subjectSpecies Specificityen
dc.subjectTurkeysen
dc.titleLamin A, lamin B, and lamin B receptor analogues in yeasten
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/2544600-
heal.identifier.secondaryhttp://jcb.rupress.org/content/108/6/2069.full.pdf-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1989-
heal.abstractPrevious studies have shown that turkey erythrocyte lamin B is anchored to the nuclear envelope via a 58-kD integral membrane protein termed p58 or lamin B receptor (Worman H. J., J. Yuan, G. Blobel, and S. D. Georgatos. 1988. Proc. Natl. Acad. Sci. USA. 85:8531-8534). We now identify a p58 analogue in the yeast Saccharomyces cerevisiae. Turkey erythrocyte lamin B binds to yeast urea-extracted nuclear envelopes with high affinity, associating predominantly with a 58-kD polypeptide. This yeast polypeptide is recognized by polyclonal antibodies against turkey p58, partitions entirely with the nuclear fraction, remains membrane bound after urea extraction of the nuclear envelopes, and is structurally similar to turkey p58 by peptide mapping criteria. Using polyclonal antibodies against turkey erythrocyte lamins A and B, we also identify two yeast lamin forms. The yeast lamin B analogue has a molecular mass of 66 kD and is structurally related to erythrocyte lamin B. Moreover, the yeast lamin B analogue partitions exclusively with the nuclear envelope fraction, is quantitatively removed from the envelopes by urea extraction, and binds to turkey lamin A and vimentin. As many higher eukaryotic lamin B forms, the yeast analogue is chemically heterogeneous comprising two serologically related species with different charge characteristics. Antibodies against turkey lamin A detect a 74-kD yeast protein, slightly larger than the turkey lamin A. It is more abundant than the yeast lamin B analogue and partitions between a soluble cytoplasmic fraction and a nuclear envelope fraction. The yeast lamin A analogue can be extracted from the nuclear envelope by urea, shows structural similarity to turkey and rat lamin A, and binds to isolated turkey lamin B. These data indicate that analogues of typical nuclear lamina components (lamins A and B, as well as lamin B receptor) are present in yeast and behave as their vertebrate counterparts.en
heal.journalNameJ Cell Biolen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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