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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	Asgard archaea shed light on the evolutionary origins of the eukaryotic ubiquitin-ESCRT machinery Tomoyuki Hatano , Saravanan Palani , Dimitra Papatziamou , Ralf Salzer , Diorge P. Souza , Daniel Tamarit , Mehul Makwana , Antonia Potter , Alexandra Haig , Wenjue Xu , David Townsend , David Rochester , Dom Bellini , Hamdi M. A. Hussain , Thijs J. G. Ettema , Jan Lowe , Buzz Baum , Nicholas P. Robinson , Mohan Balasubramanian Nature Communications 13 DOI: 10.1038/s41467-022-30656-2 Diamond Proposal Number(s): [21426] Open Access Show Abstract ▼ Abstract: The ESCRT machinery, comprising of multiple proteins and subcomplexes, is crucial for membrane remodelling in eukaryotic cells, in processes that include ubiquitin-mediated multivesicular body formation, membrane repair, cytokinetic abscission, and virus exit from host cells. This ESCRT system appears to have simpler, ancient origins, since many archaeal species possess homologues of ESCRT-III and Vps4, the components that execute the final membrane scission reaction, where they have been shown to play roles in cytokinesis, extracellular vesicle formation and viral egress. Remarkably, metagenome assemblies of Asgard archaea, the closest known living relatives of eukaryotes, were recently shown to encode homologues of the entire cascade involved in ubiquitin-mediated membrane remodelling, including ubiquitin itself, components of the ESCRT-I and ESCRT-II subcomplexes, and ESCRT-III and Vps4. Here, we explore the phylogeny, structure, and biochemistry of Asgard homologues of the ESCRT machinery and the associated ubiquitylation system. We provide evidence for the ESCRT-I and ESCRT-II subcomplexes being involved in ubiquitin-directed recruitment of ESCRT-III, as it is in eukaryotes. Taken together, our analyses suggest a pre-eukaryotic origin for the ubiquitin-coupled ESCRT system and a likely path of ESCRT evolution via a series of gene duplication and diversification events.	Jun 2022
Krios II-Titan Krios II at Diamond	Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium Alexander Neuhaus , Muniyandi Selvaraj , Ralf Salzer , Julian D. Langer , Kerstin Kruse , Lennart Kirchner , Kelly Sanders , Bertram Daum , Beate Averhoff , Vicki A. M. Gold Nature Communications 11 DOI: 10.1038/s41467-020-15650-w Diamond Proposal Number(s): [18258] Open Access Show Abstract ▼ Abstract: Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus (‘wide’ and ‘narrow’), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.	May 2020

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