National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01GM071940
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM007185
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI052348
米国
National Institutes of Health/Office of the Director
S10OD018111
米国
National Institutes of Health/National Center for Research Resources (NIH/NCRR)
S10RR23057
米国
National Science Foundation (NSF, United States)
DMR-1548924
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
U24GM116792
米国
Swiss National Science Foundation
P300PA_174358
スイス
National Science Foundation (NSF, United States)
DBI-1338135
米国
引用
ジャーナル: Elife / 年: 2019 タイトル: Cryo electron tomography with volta phase plate reveals novel structural foundations of the 96-nm axonemal repeat in the pathogen . 著者: Simon Imhof / Jiayan Zhang / Hui Wang / Khanh Huy Bui / Hoangkim Nguyen / Ivo Atanasov / Wong H Hui / Shun Kai Yang / Z Hong Zhou / Kent L Hill / 要旨: The 96-nm axonemal repeat includes dynein motors and accessory structures as the foundation for motility of eukaryotic flagella and cilia. However, high-resolution 3D axoneme structures are ...The 96-nm axonemal repeat includes dynein motors and accessory structures as the foundation for motility of eukaryotic flagella and cilia. However, high-resolution 3D axoneme structures are unavailable for organisms among the Excavates, which include pathogens of medical and economic importance. Here we report cryo electron tomography structures of the 96-nm repeat from , a protozoan parasite in the Excavate lineage that causes African trypanosomiasis. We examined bloodstream and procyclic life cycle stages, and a knockdown lacking DRC11/CMF22 of the nexin dynein regulatory complex (NDRC). Sub-tomogram averaging yields a resolution of 21.8 Å for the 96-nm repeat. We discovered several lineage-specific structures, including novel inter-doublet linkages and microtubule inner proteins (MIPs). We establish that DRC11/CMF22 is required for the NDRC proximal lobe that binds the adjacent doublet microtubule. We propose that lineage-specific elaboration of axoneme structure in reflects adaptations to support unique motility needs in diverse host environments.