Lotte Søgaard-Andersen
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lottesogaard.bsky.social
Lotte Søgaard-Andersen
@lottesogaard.bsky.social
Ex-director at the Max Planck Institute for Terrestrial Microbiology, Marburg.
6/ Traditionally, the function of proteins depends on their assembly into complexes of well-defined stoichiometry & structure. The PomXYZ architecture illustrates how a co-condensate without a well-defined stoichiometry & structure spatiotemporally regulates cell division with exquisite precision.
January 3, 2025 at 10:32 AM
5/ Because PomY biomolecular condensate formation is templated by & embedded within the PomX meshwork, precisely one PomXYZ co-condensate is formed per cell.
January 3, 2025 at 10:32 AM
4/ PomY associates with the PomX meshwork and undergoes surface-assisted condensation on this meshwork, resulting in the formation of a highly selective PomXY co-condensate that is associated with the nucleoid by PomZ.
January 3, 2025 at 10:32 AM
3/ We show that PomX forms precisely one copy per cell of a highly variable, porous meshwork of randomly intertwined filaments akin to a tumbleweed architecture. The PomX meshwork contains large protein densities & ribosomes and is non-selective.
January 3, 2025 at 10:32 AM
2/ Biomolecular condensates spatially organize cellular reactions in bacteria and eukaryotic cells. PomX, PomY & PomZ form precisely one MDa-sized, nonstoichiometric, nucleoid-associated co-condensate per cell that nucleates FtsZ polymerization to form the cytokinetic FtsZ-ring in Myxococcus.
January 3, 2025 at 10:32 AM
Reposted by Lotte Søgaard-Andersen
Check out this new preprint on bioRxiv about a tyrosine pseudokinase involved in eps synthesis in Myxococcus xanthus by Bloecher et al., @lottesogaard.bsky.social
November 27, 2024 at 5:20 PM