Topic: In Situ CryoET Study of Bacterial Dividing PomXZY Co-condensate
Speaker: Dr. Peng Xu, Max-Planck Institute of Biochemistry (MPIB)
Date and time: August 15, 15:00
Venue: Auditorium, Y Building
Host: Wolfgang Baumeister
Abstract:
Cryo-ET is a cutting-edge technique that enables the study of protein function within their physiological cellular context. This technique allows researchers to visualize proteins at molecular resolution through subtomogram averaging, making it an invaluable tool for structural biology. In most bacteria, cell division relies on the tubulin-homolog FtsZ, which polymerizes to form the cytokinetic Z-ring. The mechanisms that position the Z-ring and modulate FtsZ polymerization are not fully understood. In Myxococcus, the proteins PomX, PomY, and PomZ form a single megadalton-sized (MDa), non-stoichiometric, nucleoid-associated assembly that guides Z-ring formation. Using cryo-correlative light and electron microscopy combined with in situ cryo-electron tomography, we determine the architecture of the PomXYZ assembly under near-native conditions. This approach provides detailed insights into how the PomXYZ complex orchestrates Z-ring formation, enhancing our understanding of bacterial cell division.
Biography:
2017–present Postdoc
Molecular Structural Biology Department, Max-Planck Institute of Biochemistry
2012–2017 PhD
Center for Structural Biology, School of Life Science, Tsinghua University
2008–2012 BS
National Key Course of Biotechnology, School of Life Science, Sichuan University