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TitleProteasomes. A molecular census of 26S proteasomes in intact neurons.
Journal, issue, pagesScience, Vol. 347, Issue 6220, Page 439-442, Year 2015
Publish dateJan 23, 2015
AuthorsShoh Asano / Yoshiyuki Fukuda / Florian Beck / Antje Aufderheide / Friedrich Förster / Radostin Danev / Wolfgang Baumeister /
PubMed AbstractThe 26S proteasome is a key player in eukaryotic protein quality control and in the regulation of numerous cellular processes. Here, we describe quantitative in situ structural studies of this highly ...The 26S proteasome is a key player in eukaryotic protein quality control and in the regulation of numerous cellular processes. Here, we describe quantitative in situ structural studies of this highly dynamic molecular machine in intact hippocampal neurons. We used electron cryotomography with the Volta phase plate, which allowed high fidelity and nanometer precision localization of 26S proteasomes. We undertook a molecular census of single- and double-capped proteasomes and assessed the conformational states of individual complexes. Under the conditions of the experiment—that is, in the absence of proteotoxic stress—only 20% of the 26S proteasomes were engaged in substrate processing. The remainder was in the substrate-accepting ground state. These findings suggest that in the absence of stress, the capacity of the proteasome system is not fully used.
External linksScience / PubMed:25613890
MethodsEM (subtomogram averaging)
Resolution27.0 - 31.0 Å
Structure data

EMDB-2830:
Electron cryotomography, subtomogram averaging and classification of 26S proteasomes in situ in intact hippocampal neurons
Method: EM (subtomogram averaging) / Resolution: 27.0 Å

EMDB-2831:
Electron cryotomography, subtomogram averaging and classification of 26S proteasomes in situ in intact hippocampal neurons
Method: EM (subtomogram averaging) / Resolution: 31.0 Å

Source
  • Rattus norvegicus (Norway rat)

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