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dc.creatorMi, L
dc.creatorGoryaynov, A
dc.creatorLindquist, A
dc.creatorRexach, M
dc.creatorYang, W
dc.date.accessioned2021-01-31T16:01:09Z
dc.date.available2021-01-31T16:01:09Z
dc.date.issued2015-01-01
dc.identifier.issn2045-2322
dc.identifier.issn2045-2322
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5237
dc.identifier.other25797490 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5255
dc.description.abstract© 2015, Nature Publishing Group. All rights reserved. The nuclear pore complex (NPC) is one of the largest supramolecular structures in eukaryotic cells. Its octagonal ring-scaffold perforates the nuclear envelope and features a unique molecular machinery that regulates nucleocytoplasmic transport. NPCs are composed of ∼30 different nucleoporins (Nups), averaged at 8, 16 or 32 copies per NPC. This estimate has not been confirmed for individual NPCs in living cells due to the inherent difficulty of counting proteins inside single supramolecular complexes. Here we used single-molecule SPEED microscopy to directly count the copy-number of twenty-four different Nups within individual NPCs of live yeast, and found agreement as well as significant deviation from previous estimates. As expected, we counted 8 copies of four peripheral Nups and 16 copies of fourteen scaffold Nups. Unexpectedly, we counted a maximum of 16 copies of Nsp1 and Nic96, rather than 32 as previously estimated; and found only 10-15 copies of six other Nups, rather than 8 or 16 copies as expected. This in situ molecular-counting technology can test structure-function models of NPCs and other supramolecular structures in cells.
dc.format.extent9372-
dc.language.isoen
dc.relation.haspartScientific Reports
dc.relation.isreferencedbySpringer Science and Business Media LLC
dc.rightsCC BY
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectActive Transport, Cell Nucleus
dc.subjectEscherichia coli
dc.subjectGene Expression
dc.subjectGreen Fluorescent Proteins
dc.subjectNuclear Pore
dc.subjectNuclear Pore Complex Proteins
dc.subjectNuclear Proteins
dc.subjectProtein Multimerization
dc.subjectRecombinant Fusion Proteins
dc.subjectSaccharomyces cerevisiae
dc.subjectSaccharomyces cerevisiae Proteins
dc.titleQuantifying Nucleoporin Stoichiometry Inside Single Nuclear Pore Complexes In vivo
dc.typeArticle
dc.type.genreJournal Article
dc.relation.doi10.1038/srep09372
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.creator.orcidYang, Weidong|0000-0002-3554-3035
dc.date.updated2021-01-31T16:01:05Z
refterms.dateFOA2021-01-31T16:01:10Z


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