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TitleIn vivo Architecture of the Polar Organizing Protein Z (PopZ) Meshwork in the Alphaproteobacteria Magnetospirillum gryphiswaldense and Caulobacter crescentus.
Journal, issue, pagesJ Mol Biol, Vol. 434, Issue 5, Page 167423, Year 2022
Publish dateMar 15, 2022
AuthorsMauricio Toro-Nahuelpan / Jürgen M Plitzko / Dirk Schüler / Daniel Pfeiffer /
PubMed AbstractThe polar organizing protein Z (PopZ) forms a polar microdomain that is inaccessible to larger macromolecules such as ribosomes, and selectively sequesters proteins crucial for cell cycle control and ...The polar organizing protein Z (PopZ) forms a polar microdomain that is inaccessible to larger macromolecules such as ribosomes, and selectively sequesters proteins crucial for cell cycle control and polar morphogenesis in various Alphaproteobacteria. However, the in vivo architecture of this microdomain has remained elusive. Here, we analyzed the three-dimensional ultrastructural organization of the PopZ network in Magnetospirillum gryphiswaldense and Caulobacter crescentus by Volta phase plate cryo-electron tomography, which provides high spatial resolution and improved image contrast. Our results suggest that PopZ forms a porous network of disordered short, flexible, and branching filaments.
External linksJ Mol Biol / PubMed:34971672
MethodsEM (tomography)
Structure data

EMDB-14021:
Cryo-ET of Magnetospirillum gryphiswaldense delta-popZ overproducing PopZ-Mgr
Method: EM (tomography)

EMDB-14022:
Volta phase plate cryo-ET of Magnetospirillum gryphiswaldense overproducing PopZ-Mgr
Method: EM (tomography)

Source
  • Magnetospirillum gryphiswaldense MSR-1 (magnetotactic)

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