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http://dx.doi.org/10.25673/111007
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DC Field | Value | Language |
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dc.contributor.author | Semchonok, Dmitry A. | - |
dc.contributor.author | Kyrilis, Fotis L. | - |
dc.contributor.author | Hamdi, Farzad | - |
dc.contributor.author | Kastritis, Panagiotis L. | - |
dc.date.accessioned | 2023-10-18T08:17:31Z | - |
dc.date.available | 2023-10-18T08:17:31Z | - |
dc.date.issued | 2023 | - |
dc.identifier.uri | https://opendata.uni-halle.de//handle/1981185920/112961 | - |
dc.identifier.uri | http://dx.doi.org/10.25673/111007 | - |
dc.description.abstract | Biomolecular complexes and their interactions govern cellular structure and function. Understanding their architecture is a prerequisite for dissecting the cell's inner workings, but their higher-order assembly is often transient and challenging for structural analysis. Here, we performed cryo-EM on a single, highly heterogeneous biochemical fraction derived from Chaetomium thermophilum cell extracts to visualize the biomolecular content of the multicellular eukaryote. After cryo-EM single-particle image processing, results showed that a simultaneous three-dimensional structural characterization of multiple chemically diverse biomacromolecules is feasible. Namely, the thermophilic, eukaryotic complexes of (a) ATP citrate-lyase, (b) Hsp90, (c) 20S proteasome, (d) Hsp60 and (e) UDP-glucose pyrophosphorylase were characterized. In total, all five complexes have been structurally dissected in a thermophilic eukaryote in a total imaged sample area of 190.64 μm2, and two, in particular, 20S proteasome and Hsp60, exhibit side-chain resolution features. The C. thermophilum Hsp60 near-atomic model was resolved at 3.46 Å (FSC = 0.143) and shows a hinge-like conformational change of its equatorial domain, highly similar to the one previously shown for its bacterial orthologue, GroEL. This work demonstrates that cryo-EM of cell extracts will greatly accelerate the structural analysis of cellular complexes and provide unprecedented opportunities to annotate architectures of biomolecules in a holistic approach. | eng |
dc.language.iso | eng | - |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
dc.subject.ddc | 572 | - |
dc.title | Cryo-EM of a heterogeneous biochemical fraction elucidates multiple protein complexes from a multicellular thermophilic eukaryote | eng |
dc.type | Article | - |
local.versionType | publishedVersion | - |
local.bibliographicCitation.journaltitle | Journal of structural biology: X | - |
local.bibliographicCitation.volume | 8 | - |
local.bibliographicCitation.publishername | Elsevier | - |
local.bibliographicCitation.publisherplace | Amsterdam | - |
local.bibliographicCitation.doi | 10.1016/j.yjsbx.2023.100094 | - |
local.subject.keywords | Native cell extracts, biochemical fraction, Cryo-EM, single-particle image processing, simultaneous 3D reconstructions | - |
local.openaccess | true | - |
dc.identifier.ppn | 1865871710 | - |
cbs.publication.displayform | 2023 | - |
local.bibliographicCitation.year | 2023 | - |
cbs.sru.importDate | 2023-10-18T08:16:43Z | - |
local.bibliographicCitation | Enthalten in Journal of structural biology: X - Amsterdam : Elsevier, 2019 | - |
local.accessrights.dnb | free | - |
Appears in Collections: | Open Access Publikationen der MLU |
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1-s2.0-S2590152423000107-main.pdf | 12.84 MB | Adobe PDF | ![]() View/Open |