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TitleComposition and Biophysical Properties of the Sorting Platform Pods in the Type III Secretion System.
Journal, issue, pagesFront Cell Infect Microbiol, Vol. 11, Page 682635, Year 2021
Publish dateJun 3, 2021
AuthorsShoichi Tachiyama / Ryan Skaar / Yunjie Chang / Brittany L Carroll / Meenakumari Muthuramalingam / Sean K Whittier / Michael L Barta / Wendy L Picking / Jun Liu / William D Picking /
PubMed Abstract, causative agent of bacillary dysentery (shigellosis), uses a type III secretion system (T3SS) as its primary virulence factor. The T3SS injectisome delivers effector proteins into host cells to ..., causative agent of bacillary dysentery (shigellosis), uses a type III secretion system (T3SS) as its primary virulence factor. The T3SS injectisome delivers effector proteins into host cells to promote entry and create an important intracellular niche. The injectisome's cytoplasmic sorting platform (SP) is a critical assembly that contributes to substrate selection and energizing secretion. The SP consists of oligomeric Spa33 "pods" that associate with the basal body MxiK and connect to the Spa47 ATPase MxiN. The pods contain heterotrimers of Spa33 with one full-length copy associated with two copies of a C-terminal domain (Spa33). The structure of Spa33 is known, but the precise makeup and structure of the pods remains elusive. We show here that recombinant wild-type Spa33 can be prepared as a heterotrimer that forms distinct stable complexes with MxiK and MxiN. In two-hybrid analyses, association of the Spa33 complex with these proteins occurs the full-length Spa33 component. Furthermore, these complexes each have distinct biophysical properties. Based on these properties, new high-resolution cryo-electron tomography data and architectural similarities between the Spa33 and flagellar FliM-FliN complexes, we provide a preliminary model of the Spa33 heterotrimers within the SP pods. From these findings and evolving models of SP interfaces and dynamics in the and T3SS, we suggest a model for SP function in which two distinct complexes come together within the context of the SP to contribute to form the complete pod structures during the recruitment of T3SS secretion substrates.
External linksFront Cell Infect Microbiol / PubMed:34150677 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution16.0 Å
Structure data

EMDB-23440:
Shigella Pod
Method: EM (subtomogram averaging) / Resolution: 16.0 Å

Source
  • Shigella flexneri (bacteria)

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