Sonja-Verena Albers

@archaellum.bsky.social

PI at the University of Freiburg, interested in molecular microbiology and all things related to #archaea

The manuscript introducing ArchaeaHQ is still under review😴 As science can't wait... I'm making available a version of the dashboard we use. vee-lab.eu/archaeahq Here the user can have quick access to the information in the database, and select specific genomes of interest. Enjoy 🎉

Pedro Leão@pedroleao.bsky.social · 2mo ago

I'm happy to share the first pre-print of out Lab! 🎉 Introducing ArchaeaHQ www.biorxiv.org/content/10.6... We curated 21,644 genomes across all 4 archaeal kingdoms to bridge the gap in public datasets for computational biology What is inside ArchaeaHQ... (1/2)

(BioRxiv All) Systematic identification of cell division proteins in haloarchaea and the discovery of a membrane anchor for the Z ring: Most archaea rely on the tubulin-like protein FtsZ for division. In the last decade, several novel cell division proteins have been… #BioRxiv #MassSpecRSS

Systematic identification of cell division proteins in haloarchaea and the discovery of a membrane anchor for the Z ring

Most archaea rely on the tubulin-like protein FtsZ for division. In the last decade, several novel cell division proteins have been discovered in the model haloarchaeon Haloferax volcanii which contains two FtsZ proteins, FtsZ1 and FtsZ2. However, the composition of this FtsZ-based archaeal divisome is largely uncharacterized. Here, using in vivo crosslinking coupled with immunoprecipitation and mass spectrometry (CLIP-MS), we identified ten proteins that localize to the division site, including wide-spread proteins predicted to be involved in DNA binding and energy metabolism. Deletion analysis indicate that most of these proteins have a modest or minor impact on cell division, but HVO_0399, renamed as Cell Division Protein C (CdpC), is important for cell division and functions as a membrane anchor for FtsZ1. CdpC consists of three domains, an N-terminal domain (NTD) containing an amphipathic helix critical for membrane binding, a long intrinsically disordered linker, and a C-terminal domain (CTD) that binds FtsZ1 with high affinity and likely promotes its polymerization. Notably, both the NTD and CTD of CdpC harbor a zinc finger that is indispensable for its function. Phylogenetic analysis indicates that CdpC sequences evolved fast across haloarchaea, but exhibited high conservation in domain structure and critical residues found in this study. Overall, our study expands the repertoire of candidate division proteins and establishes CdpC as a membrane anchor for FtsZ1 in haloarchaea. These findings pave the way for in-depth studies of arcaheal cell division and broaden the function of zinc finger proteins in archaea.

dlvr.it

Some bacteria do not live as individuals. They build multicellular filaments and connect neighboring cells through tiny cell-cell junctions. Cyanobacteria are among the most beautiful examples 😍 In our new paper, we reveal first molecuar insights on the cyanobacterial septal junction architecture 🧵

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1/ Happy to share our preprint! The Mtr complex catalyses the second-to-last step of the methanogenesis and is an essential bioenergetic machine in most methanogenic archaea. Anaerobic cryo-EM of Mtr reveals a nitrogenase-like metallocluster bound at its active site! www.biorxiv.org/content/10.6...

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Meet AbpX, a biomatrix protein from the hyperthermophile Pyrodictium abyssi. It forms Ca²⁺-triggered fibrils via donor strand complementation. Using cryo-EM + X-ray, we built a full lattice model and place AbpX in a new TasA superfamily clade. A very nice collaborative project! tinyurl.com/mryzcz4n

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