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TitleThe cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the type III secretion system.
Journal, issue, pagesJ Biol Chem, Vol. 294, Issue 50, Page 19184-19196, Year 2019
Publish dateDec 13, 2019
AuthorsShoichi Tachiyama / Yunjie Chang / Meenakumari Muthuramalingam / Bo Hu / Michael L Barta / Wendy L Picking / Jun Liu / William D Picking /
PubMed AbstractMany Gram-negative bacteria use type III secretion systems (T3SSs) to inject virulence effector proteins into eukaryotic cells. The T3SS apparatus (T3SA) is structurally conserved among diverse ...Many Gram-negative bacteria use type III secretion systems (T3SSs) to inject virulence effector proteins into eukaryotic cells. The T3SS apparatus (T3SA) is structurally conserved among diverse bacterial pathogens and consists of a cytoplasmic sorting platform, an envelope-spanning basal body, and an extracellular needle with tip complex. The sorting platform is essential for effector recognition and powering secretion. Studies using bacterial "minicells" have revealed an unprecedented level of structural detail of the sorting platform; however, many of the structure-function relationships within this complex remain enigmatic. Here, we report on improved cryo-electron tomographic approaches to enhance the resolution of the T3SA sorting platform (at ≤2 nm resolution) done in concert with biochemical and genetic methods to define the sorting platform interactome and interactions with the T3SA inner membrane ring (IR). We observed that the sorting platform consists of "pods" with 6-fold symmetry that interact with the Spa47 ATPase via radial extensions comprising MxiN. Most importantly, MxiK maintained an interaction with the IR via specific interactions with the cytoplasmic domain of the IR protein MxiG (MxiG), which is a noncanonical forkhead-associated domain, and MxiK has an elongated structure that interacts with the IR via MxiG T4 lysozyme-mediated insertional mutagenesis of MxiK revealed its orientation within the sorting platform and enabled disruption of interactions with its binding partners, which abolished sorting platform assembly. Finally, a comparison with the homologous interactions in the T3SS sorting platform revealed clear differences in their IR-sorting platform interfaces that have possible mechanistic implications.
External linksJ Biol Chem / PubMed:31699894 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution18.0 - 27.0 Å
Structure data

EMDB-20561:
Pod structure of Shigella T3SS
Method: EM (subtomogram averaging) / Resolution: 18.0 Å

EMDB-20611:
In situ structure of Shigella flexneri type III secretion system
Method: EM (subtomogram averaging) / Resolution: 27.0 Å

Source
  • Shigella flexneri (bacteria)
  • Shigella flexneri 5a str. M90T (bacteria)

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