Gutenberg Open Science: Visualizing the disordered nuclear transport machinery in situ

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9682

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DC Field	Value	Language
dc.contributor.author	Yu, Miao	-
dc.contributor.author	Heidari, Maziar	-
dc.contributor.author	Mikhaleva, Sofya	-
dc.contributor.author	Tan, Piau Siong	-
dc.contributor.author	Mingu, Sara	-
dc.contributor.author	Ruan, Hao	-
dc.contributor.author	Reinkemeier, Christopher D.	-
dc.contributor.author	Obarska-Kosinska, Agnieszka	-
dc.contributor.author	Siggel, Marc	-
dc.contributor.author	Beck, Martin	-
dc.contributor.author	Hummer, Gerhard	-
dc.contributor.author	Lemke, Edward A.	-
dc.date.accessioned	2023-11-21T08:20:32Z	-
dc.date.available	2023-11-21T08:20:32Z	-
dc.date.issued	2023	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/9700	-
dc.description.abstract	The approximately 120 MDa mammalian nuclear pore complex (NPC) acts as a gatekeeper for the transport between the nucleus and cytosol1. The central channel of the NPC is filled with hundreds of intrinsically disordered proteins (IDPs) called FG-nucleoporins (FG-NUPs)2,3. Although the structure of the NPC scaffold has been resolved in remarkable detail, the actual transport machinery built up by FG-NUPs—about 50 MDa—is depicted as an approximately 60-nm hole in even highly resolved tomograms and/or structures computed with artificial intelligence4,5,6,7,8,9,10,11. Here we directly probed conformations of the vital FG-NUP98 inside NPCs in live cells and in permeabilized cells with an intact transport machinery by using a synthetic biology-enabled site-specific small-molecule labelling approach paired with highly time-resolved fluorescence microscopy. Single permeabilized cell measurements of the distance distribution of FG-NUP98 segments combined with coarse-grained molecular simulations of the NPC allowed us to map the uncharted molecular environment inside the nanosized transport channel. We determined that the channel provides—in the terminology of the Flory polymer theory12—a ‘good solvent’ environment. This enables the FG domain to adopt expanded conformations and thus control transport between the nucleus and cytoplasm. With more than 30% of the proteome being formed from IDPs, our study opens a window into resolving disorder–function relationships of IDPs in situ, which are important in various processes, such as cellular signalling, phase separation, ageing and viral entry.	de_DE
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	570 Biowissenschaften	de_DE
dc.subject.ddc	570 Life sciences	en_GB
dc.title	Visualizing the disordered nuclear transport machinery in situ	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-9682	-
jgu.type.contenttype	Scientific article	de
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 10 Biologie	de
jgu.organisation.number	7970	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Nature	de
jgu.journal.volume	617	de
jgu.pages.start	162	de
jgu.pages.end	169	de
jgu.publisher.year	2023	-
jgu.publisher.name	Nature Publ. Group	de
jgu.publisher.place	London u.a.	de
jgu.publisher.issn	1476-4687	de
jgu.publisher.issn	0028-0836	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	570	de
jgu.publisher.doi	10.1038/s41586-023-05990-0	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	JGU-Publikationen

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