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TitleIn situ structural analysis of Golgi intracisternal protein arrays.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 112, Issue 36, Page 11264-11269, Year 2015
Publish dateSep 8, 2015
AuthorsBenjamin D Engel / Miroslava Schaffer / Sahradha Albert / Shoh Asano / Jürgen M Plitzko / Wolfgang Baumeister /
PubMed AbstractWe acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo- ...We acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo-electron tomography. These tomograms revealed structures within the Golgi cisternae that have not been seen before. Narrow trans-Golgi lumina were spanned by asymmetric membrane-associated protein arrays that had ∼6-nm lateral periodicity. Subtomogram averaging showed that the arrays may determine the narrow central spacing of the trans-Golgi cisternae through zipper-like interactions, thereby forcing cargo to the trans-Golgi periphery. Additionally, we observed dense granular aggregates within cisternae and intracisternal filament bundles associated with trans-Golgi buds. These native in situ structures provide new molecular insights into Golgi architecture and function.
External linksProc Natl Acad Sci U S A / PubMed:26311849 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution27.0 Å
Structure data

EMDB-3100:
Cryo-electron tomography of a Golgi intracisternal protein array
Method: EM (subtomogram averaging) / Resolution: 27.0 Å

Source
  • Chlamydomonas reinhardtii (plant)

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