Date: 22 October 2026 (Thursday)
Time: 10:00 am – 11:00 am
Venue: Mrs Chen Yang Foo Oi Telemedicine Centre, 2/F, William M.W. Mong Block, 21 Sassoon Road 
Host: Professor Tao Ni

Jiangfeng Zhao is a structural biologist specializing in RNA biology and cryo-electron microscopy. He completed his doctoral research at the Max Planck Institute of Biophysics in Frankfurt, Germany, under the supervision of Prof. Hartmut Michel, where he studied membrane proteins using structural and biophysical approaches. 

He subsequently joined the European Molecular Biology Laboratory (EMBL) in Grenoble, France, as a postdoctoral researcher in Dr. Wojciech Galej's group, supported by a Marie Skłodowska-Curie Postdoctoral Fellowship. His research focuses on understanding the molecular mechanisms of human minor spliceosome assembly through an integrated approach combining cryo-EM, RNA biochemistry, and quantitative proteomics.

His broader research interests include RNA processing, the structural basis of gene regulation, and the molecular mechanisms underlying human disease.

The minor spliceosome removes a rare but functionally important class of introns (U12-type introns), yet the molecular mechanisms governing their initial recognition and prespliceosome assembly remain poorly understood. Here, we combine cryo-electron microscopy with single-molecule, biochemical and proteomic analyses to define five structural states spanning the early stages of human minor spliceosome assembly. These structures reveal a stepwise assembly pathway in which the U11/U12 di-snRNP first recognizes the 5’ splice site in an ATP-independent manner, followed by branch-site recognition and subsequent docking of the branch helix onto SF3B1. These transitions are coordinated by the minor spliceosome-specific factors ZCRB1 and RNPC3, which act as sequential assembly checkpoints, coupling branch-site recognition and prespliceosome maturation. Successful branch-helix docking initiates remodelling of the U11/U12 interface and facilitates the recruitment of the minor tri-snRNP. Together, our findings provide a mechanistic framework for early U12-type intron recognition and reveal how sequential conformational checkpoints ensure the fidelity of the minor spliceosome assembly.

All are welcome.