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Group leader at Heinrich-Heine University | Exploring different aspects of fungal interactions | Passionate about Structural Biology | altegoerlab.de
Altegoerlab
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As promised: We have an open 2-year postdoc position in my lab at HHU Düsseldorf, starting September 2026. Come join us and help pioneering structural biology of fungal GPCRs! More about the lab: altegoerlab.de Apply here: karriere.hhu.de/index.php?ac... Please share with interested candidates!
1d
karriere.hhu.de
Membrane binding controls the ATPase cycle and localization of MinD in Bacillus subtilis doi.org/10.7554/eLif... - The final version of a long story! Biochemical analysis of MinD in vitro and in vivo (with SMLM). Credit goes to @drhelgon.bsky.social!
Postdoc (m/f/d) structural biology of fungal G-Protein coupled receptors
Altegoerlab
1d
Everything you wanted to know about the protein chemistry behind how amino-acid changes affect the cellular abundance of proteins from @tkschulze.bsky.social Effects of residue substitutions on the cellular abundance of proteins doi.org/10.7554/eLif...
11d
Please RT: Registration is ongoing for our International Symposium "Microbial Networking - from organelles to cross-kingdom communities" organized as highlight of the first funding period of CRC 1535 @mibinet.bsky.social www.sfb1535.hhu.de/internationa... @dfg.de, @hhu.de, @fz-juelich.de
Now out in @pnas.org 🥳 "DNA-intercalating antiphage molecules trigger abortive infection through mutual destruction and synergize with bacterial immunity" --> bad timing can kill you, even as a virus. www.pnas.org/doi/10.1073/... @spp2330.bsky.social, @mibinet.bsky.social, @dfg.de
7d
That celebration has waited for a long time... One year ago we uploaded the preprint and started the endeavor through the peer-reviewing. Lots of emotions on the way 🎭, lots of work, and quite some learning on "friend or foe"... Probably, deserves another post 🤫 But now - the paper is accepted!
6d
We just received funding for a 2yr postdoc position on cryoEM of fungal gpcrs. Official call will open soon. Contact me if you‘re interested!
11d
1mo
Marc Bramkamp
Proceedings of the National Academy of Sciences (PNAS), a peer reviewed journal of the National Academy of Sciences (NAS) - an authoritative source of high-impact, original research that broadly spans...
PNAS
www.pnas.org
Effector recognition by molecular mimicry of its target by an NLR - enabling multiple disease resistance specificities to be generated- first seen on @biorxiv-plants.bsky.social - great work led by @dianagdlc.bsky.social and Matt Moscou www.science.org/doi/10.1126/...
Folddisco is now published @natbiotech.nature.com. It’s a fast motif search for similar 3D DISCOntinuous residues like catalytic sites or zinc fingers across the entire protein universe. 📄 www.nature.com/articles/s41... 💾 folddisco.foldseek.com​​​​​​​​​​​​​​​​ 🌐 https://search.foldseek.com/folddisco
Altegoerlab
‼️Job alert📢🚨 We are recruiting a Junior Group Leader (f) in Protein Science at Martin Luther University Halle-Wittenberg, jointly hosted by the Institute of Biochemistry and Biotechnology and our Collaborative Research Centre CRC 1664 "Plant Proteoform Diversity – SNP2Prot."
Julia Frunzke
Julia Frunzke
Kresten Lindorff-Larsen
5d
Dynamic relocalization of MinD in Bacillus subtilis arises from membrane binding of monomers and dimers with membrane-triggered ATP hydrolysis, suggesting MinE-like activators are unnecessary for Min ...
doi.org
Membrane binding controls the ATPase cycle and localization of MinD in Bacillus subtilis
Kedrov Lab @ HHU
4d
🦠 How did our cells originate? A study by #IRBBarcelona & @bsc-cns.bsky.social by @gabaldonlab.bsky.social, suggests cellular complexity arose through long-term microbial alliances rather than a single evolutionary event. @nature.com ➡️ https://shorturl.at/kCij7 📌 DOI: 10.1038/s41586-026-10639-9
2d
Plants and animals respond to pathogen attack by mounting innate immune responses that require intracellular nucleotide-binding leucine-rich repeat (NLR) proteins. These immune receptors detect pathog...
www.science.org
Molecular mimicry of a pathogen virulence target by a plant immune receptor
3h
Happy to share our recent preprint: "DNA-intercalating antiphage molecules trigger abortive infection through mutual destruction and synergize with bacterial immunity" www.biorxiv.org/content/10.6... @spp2330.bsky.social, @mibinet.bsky.social, @dfg.de @hhu.de @fzj.bsky.social
Folddisco enables protein structural motif search in million scale databases.
www.nature.com
Structural motif search across the protein universe with Folddisco - Nature Biotechnology
Nick Talbot
4mo
Martin Steinegger 🇺🇦
Thorsten Langner
Der Biologe Dr. Florian Altegoer vom Institut für Mikrobiologie der Heinrich-Heine-Universität Düsseldorf (HHU) erhält einen mit 210.000 Euro dotierten „Exploration Grant“ der Boehringer Ingelheim Stiftung (BIS).
IRB Barcelona
Julia Frunzke
Folddisco finds similar (dis)continuous 3D motifs in large protein structure databases. Its efficient index enables fast uncharacterized active site annotation, protein conformational state analysis and PPI interface comparison. 1/9🧶🧬 📄 www.biorxiv.org/content/10.1... 🌐 search.foldseek.com/folddisco
1mo
11mo
Video
Very special feelings to announce this one... A project that started like 10 years ago is reaching the finish line, ready to shine. In a dream-team with @beckmannlab.bsky.social we solved the long-chased structure of the active membrane protein insertase SecYEG-YidC www.biorxiv.org/content/10.1...
Martin Steinegger 🇺🇦
May 27, 2025
Heinrich-Heine-Universität Düsseldorf
Kedrov Lab @ HHU
www.biorxiv.org
The universally conserved Sec translocon and the YidC/Oxa1-type insertases mediate biogenesis of alpha-helical membrane proteins, but the molecular basis of their cooperation has remained disputed over decades. A recent discovery of a multi-subunit insertase in eukaryotes has raised the question about the architecture of the putative bacterial ortholog SecYEG-YidC and its functional mechanism. Here, we combine cryogenic electron microscopy with cell-free protein synthesis in nanodiscs to visualize biogenesis of the polytopic membrane protein NuoK, the subunit K of NADH-quinone oxidoreductase, that requires both SecYEG and YidC for insertion. We demonstrate that YidC is recruited to the back of the translocon at the late stage of the substrate insertion, in resemblance to the eukaryotic system, and in vivo experiments indicate that the complex assembly is vital for the cells. The nascent chain does not utilize the lateral gate of SecYEG, but enters the lipid membrane at the SecYE-YidC interface, with YidC being the primary insertase. SecYEG-YidC complex promotes folding of the nascent helices at the interface prior their insertion, so the examined cellular pathway follows the fundamental thermodynamic principles of membrane protein folding. Our data provide the first detailed insight on the elusive insertase machinery in the physiologically relevant environment, highlight the importance of the nascent chain for its assembly, and prove the evolutionary conservation of the gate-independent insertion route. ### Competing Interest Statement The authors have declared no competing interest. Deutsche Forschungsgemeinschaft, https://ror.org/018mejw64, Ke1879/3, 267205415 (CRC 1208) European Research Council, https://ror.org/0472cxd90, CRYOTRANSLATION
Substrate-induced assembly and functional mechanism of the bacterial membrane protein insertase SecYEG-YidC