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In situ cryo-electron tomography reveals the asymmetric architecture of mammalian sperm axonemes.


ABSTRACT: The flagella of mammalian sperm display non-planar, asymmetric beating, in contrast to the planar, symmetric beating of flagella from sea urchin sperm and unicellular organisms. The molecular basis of this difference is unclear. Here, we perform in situ cryo-electron tomography of mouse and human sperm, providing the highest-resolution structural information to date. Our subtomogram averages reveal mammalian sperm-specific protein complexes within the microtubules, the radial spokes and nexin-dynein regulatory complexes. The locations and structures of these complexes suggest potential roles in enhancing the mechanical strength of mammalian sperm axonemes and regulating dynein-based axonemal bending. Intriguingly, we find that each of the nine outer microtubule doublets is decorated with a distinct combination of sperm-specific complexes. We propose that this asymmetric distribution of proteins differentially regulates the sliding of each microtubule doublet and may underlie the asymmetric beating of mammalian sperm.

SUBMITTER: Chen Z 

PROVIDER: S-EPMC10023559 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature

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In situ cryo-electron tomography reveals the asymmetric architecture of mammalian sperm axonemes.

Chen Zhen Z   Greenan Garrett A GA   Shiozaki Momoko M   Liu Yanxin Y   Skinner Will M WM   Zhao Xiaowei X   Zhao Shumei S   Yan Rui R   Yu Zhiheng Z   Lishko Polina V PV   Agard David A DA   Vale Ronald D RD  

Nature structural & molecular biology 20230102 3


The flagella of mammalian sperm display non-planar, asymmetric beating, in contrast to the planar, symmetric beating of flagella from sea urchin sperm and unicellular organisms. The molecular basis of this difference is unclear. Here, we perform in situ cryo-electron tomography of mouse and human sperm, providing the highest-resolution structural information to date. Our subtomogram averages reveal mammalian sperm-specific protein complexes within the microtubules, the radial spokes and nexin-dy  ...[more]

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