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Proc Natl Acad Sci U S A. 2015 Sep 8;112(36):11264-9. doi: 10.1073/pnas.1515337112. Epub 2015 Aug 26.

In situ structural analysis of Golgi intracisternal protein arrays.

Author information

1
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany baumeist@biochem.mpg.de engelben@biochem.mpg.de.
2
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.

Abstract

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.

KEYWORDS:

Chlamydomonas; Golgi; cryo-electron tomography; focused ion beam; glycosyltransferase

PMID:
26311849
PMCID:
PMC4568700
DOI:
10.1073/pnas.1515337112
[Indexed for MEDLINE]
Free PMC Article

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