Bui Lab @McGill

@builab.bsky.social

Introducing CsMT: A new CryoSPARC workflow for high-resolution microtubule reconstruction based on novel PF-pair classification! You can reconstruct MTs entirely in CryoSPARC—zero custom scripts needed. Inspired & built through a fantastic collaboration with the Cianfrocco lab! tinyurl.com/kdpm86tw

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Our newest paper is now online in Current Biology. In short, we identified 7 proteins in the tip of the cilia and found SPEF1 is a seam-binding protein and important for cilia stability. Great work from my postdoc Thibault Legal and everyone involved! www.sciencedirect.com/science/arti...

Structure of the ciliary tip central pair reveals the unique role of the microtubule-seam binding protein SPEF1

Motile cilia are unique organelles with the ability to move autonomously. The force generated by beating cilia propels cells and moves fluids. The cil…

sciencedirect.com

Excited to share our work on bioRxiv before my thesis defense! Together with my undergraduate mentee Diego, postdocs Wan and Jun, and my advisor Kai, we identified a novel dynein heavy chain subfamily, DNAHX, from sea urchin sperm axoneme. Check out the details here: www.biorxiv.org/content/10.1...

DNAHX: a novel, non-motile dynein heavy chain subfamily, identified by cryo-EM endogenously

Ciliogenesis and cilia motility rely on the coordinated actions of diverse dyneins, yet the complexity of these motor proteins in cilia has posed challenges for understanding their specific roles. Tra...

biorxiv.org

The Bui lab Twitter will stop and we are migrating to Mastodon. Anyway, the last post is to thank the @Beck_Laboratory and @jankosinski @aobarska for the new wall art decoration. NPC rules :

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Taking forever but finally here. We identified close to 40 MIPs in Tetrahymena doublet. Specifically, the MIPs at the outer junction (CFAP77, OJ2 & OJ3). @dynein_awk @TheRealCSBlack @ahmad__khalifa

Presenting the cryo-EM structures of T4SS T-pilus and N-pilus in a fruitful collaboration with @ChristianBaron @NatalieZeytuni @TheRealCSBlack and the twitterless Jaafar Amro. My first ever structures/publication on a bacterial protein biorxiv.org/content/10.110…

Cryo-EM structure of the Agrobacterium tumefaciens T-pilus reveals the importance of positive charges in the lumen

Agrobacterium tumefaciens is a natural genetic engineer that transfers DNA into plants and this is the most frequently applied process for the generation of genetically modified plants. DNA transfer is mediated by a type IV secretion system localized in the cell envelope and extracellular T-pili. We here report the cryo-electron microscopic structures of the T-pilus at 3.2Å resolution and that of the related plasmid pKM101-determined N-pilus at 3Å resolution. Both pili contain a main pilus protein (VirB2 in A. tumefaciens and TraM in pKM101) and phospholipids arranged in a 5-start helical assembly. They contain positively charged amino acids in the pilus lumen and the lipids are positively charged in the T-pilus (phosphatidylcholine) conferring overall positive charge to the lumen. Mutagenesis of the lumen-exposed Arg91 residue in VirB2 resulted in protein destabilization and loss of pilus formation. Our results reveal that different phospholipids can be incorporated into type IV secretion system pili and that the charge of the lumen is of functional importance. ### Competing Interest Statement The authors have declared no competing interest.

biorxiv.org