Beckmann Lab

Beckmann Lab

@beckmannlab.bsky.social

cryoEM, structural biology, ribosomes https://www.genzentrum.uni-muenchen.de/research-groups/beckmann/index.html

444 followers263 following22 posts

Beckmann Lab reposted

OMühlemann lab
@omuhlemann-lab.bsky.social

Today, Wojciech Teodorowicz's PhD work on the role of USP9X in occluded A-site RQC was published. Congrats to Wojciech and Lukas, this was not an easy and definitively not a straightforward project. www.cell.com/cell-reports...

cell.comUSP9X promotes the degradation of trapped translation factors on collided ribosomesTeodorowicz et al. show that USP9X, in conjunction with the E3 ligases RNF14 and RNF25, is required to promote the VCP-dependent proteasomal degradation of eRF1 and eEF1A1 trapped in the ribosomal A-site and identify 4EHP as a mediator of translational shutdown following translation factor clearance.
Beckmann Lab
@beckmannlab.bsky.social

Frank Nijpels from VitriMatics paid us a visit today. Not only did he repair our broken VitroBot Mark IV and returned it in person, he also brought some extremely cool tools ❄️ for reliable cryo-EM grid freezing 🔬. Check out the VitriClip and the SupraBlot at vitrimatics.com. #cryoEM #cryoET

Beckmann Lab reposted

LMU München
@lmu.de

🏅 Olivia Merkel erhält UNIPRENEURS Award 2026! Die LMU-Professorin forscht an neuartigen, nicht-viralen RNA-Transportsystemen im Nanomaßstab. Auf Basis dessen, gründete sie 2023 das Spin-off RNHale mit, welches inhalierbare RNA-Therapeutika zur ursächlichen Behandlung von Asthma & COP entwickelt.

lmu.dePharmazeutin Olivia Merkel mit UNIPRENEURS Award ausgezeichnetHöchste deutsche Auszeichnung für akademisches Unternehmertum geht an die Expertin für RNA-Wirkstofftransport.
Beckmann Lab
@beckmannlab.bsky.social

New preprint! 👀RNAse activity has to be tightly regulated.✂️🧬Here, we present the dynamic architecture of the conserved Rixosome complex – a major player in ribosome maturation and heterochromatin maintenance. Our results give insights into its mode of activation.👇 #cryoEM #Ribosome #RNA

Beckmann Lab reposted

Jonathan Bohlen
@jonathanbohlen.bsky.social

🧬 New preprint: "Selection and surveillance of 5S ribosomal RNA genes in human populations." The 5S rRNA genes sit in a ~80-copy array on chromosome 1, one of the least-explored parts of the genome. We traced its variation from DNA to ribosome. 1/4🧵

Beckmann Lab
@beckmannlab.bsky.social

Preprint alert: a helicase watching the ribosomal A-site 👀🧬 Our cryo-EM structure reveals how yeast Dhx29 senses mRNA hairpins forming in the A-site and positions its helicase at the mRNA entry channel to resolve them during translation elongation: doi.org/10.64898/202... #cryoEM #ribosome #RNA

Beckmann Lab reposted

Gene Center Munich @LMU Munich
@genecenter-lmu.bsky.social

📣Publication alert: Julian Stingele and his team show that the chemotherapeutic drug azacitidine damages RNA and reveal a possible approach to improve therapies🤩👏 www.sciencedirect.com/science/arti... @jstingele.bsky.social @lmu.de @shubozhao.bsky.social

sciencedirect.comRNF25 confers mRNA damage tolerance by curbing activation of the integrated stress responseExcessive RNA damage activates cellular stress responses, triggering cell death. However, pathways that negatively regulate RNA damage responses are l…
Beckmann Lab
@beckmannlab.bsky.social

Proud to share our latest preprint! 🥳 Using a multidisciplinary approach, we uncover a dual function of the snR37 H/ACA snoRNP - combining pseudouridylation with ribosome chaperone activity within a single RNP.🔬🧬 Challenging the traditional view of snoRNP function. 👇 #cryoEM #ribosome #RNA #snoRNA

biorxiv.orgbiorxiv.org
Beckmann Lab
@beckmannlab.bsky.social

How are histones acetylated as they emerge from the ribosome? We show that NAA40 cooperates with the NAC complex to enable co-translational acetylation of H2A/H4, revealing NAC as a coordinator of nascent protein modification. Read more about our collaboration with @kirmizislab.bsky.social #cryoEM

rdcu.beNAA40 and NAC cooperate in co-translational histone acetylation in humansNature Communications - N-terminal histone acetylation by human NAA40 alters epigenetic signaling and affects gene regulation. Here, the authors combine biochemistry and cryo-EM to unravel the...
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Beckmann Lab
@beckmannlab.bsky.social

ZAK is constitutively recruited to ribosomes via its RACK1-interacting helix (RIH), the eS27-pin, and the ES7-contacting patch. Upon stress, ribosome collisions generate a unique interface that enables specific contacts — the ES6-patch and the RIH-peptide. 3/4

Beckmann Lab
@beckmannlab.bsky.social

Only in this collision geometry do the positioning of the two RACK1s allow ZAK’s RACK1-interacting motif (RIM) to engage them and enabling its SAM domains to dimerize — the key step for activation. This activation is further negatively regulated by SERBP1 competing for the RACK1 interface. 4/4

Beckmann Lab
@beckmannlab.bsky.social

Despite being the driving force behind the RSR, the interaction between ZAK and ribosomes has remained elusive for years. Here, we show how ZAK is recruited to ribosomes in native as well as stress-induced conditions, and how collision-specific interactions organized on RACK1 mediate activation. 2/4

Beckmann Lab
@beckmannlab.bsky.social

🎉Thrilled to share that our lab has been awarded an ERC Synergy Grant @erc.europa.eu! Excited for amazing collaborations with the Pertschy (Uni Graz), Henras (CBI Toulouse), and Woodson (Johns Hopkins) labs. #ERCSyG #GeneCenter #LMU #UniGraz #CNRS #JohnsHopkins

Beckmann Lab
@beckmannlab.bsky.social

We are excited to share our collab with @kedrov-lab.bsky.social! Using Cryo-EM❄️ on an amazing sample, we found that YidC is recruited to the back of SecYEG during late-stage substrate insertion —supporting that the "back-of-Sec" route observed in eukaryotes also exists in bacteria 🦠. Check it out👇👇👇

Kedrov Lab @ HHU@kedrov-lab.bsky.social

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...

biorxiv.orgSubstrate-induced assembly and functional mechanism of the bacterial membrane protein insertase SecYEG-YidCThe 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

Beckmann Lab reposted

Kedrov Lab @ HHU
@kedrov-lab.bsky.social

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...

biorxiv.orgSubstrate-induced assembly and functional mechanism of the bacterial membrane protein insertase SecYEG-YidCThe 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

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