The Munich-Würzburg Cluster of Excellence NUCLEATE on Nucleic Acid Sciences and Technologies is recruiting independent group leaders, PhDs and PostDocs 🧬. Learn more here and apply to join: www.nature.com/naturecareers/job/12861192/independent-group-leader-at-nucleate-excellence-cluster/

Independent Group Leader at NUCLEATE Excellence Cluster - Munich or Würzburg job with NUCLEATE Cluster | 12861192

Independent Group Leader in Nucleic Acid Sciences and Technologies within the NUCLEATE Cluster at LMU Munich, TU Munich or JMU Würzburg.

nature.com

NUCLEATE Cluster@nucleate-cluster.bsky.social · 4w ago

The NUCLEATE Cluster of Excellence is hiring! Shape the future of nucleic acid sciences 🧬 🚀 Group Leaders: All 3 locations (LMU, TUM, JMU Würzburg) 🔬 PhDs & Postdocs: Open call in Würzburg and speculative applications welcome! Deadline: Aug 16, 2026 👉 More info: nucleate-cluster.de/careers/

📣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

RNF25 confers mRNA damage tolerance by curbing activation of the integrated stress response

Excessive RNA damage activates cellular stress responses, triggering cell death. However, pathways that negatively regulate RNA damage responses are l…

sciencedirect.com

🎉 Congratulations to the first authors, Priyanka Aggarwal and Manmohan Sharma! Their study in the laboratory of Prof. Karl-Peter Hopfner provides important #mechanistic insight into #chromatin #remodeling across diverse #nucleosomalstates. 🧬🔬 #NARbreakthrough #Chromatin #Epigenetics #INO80

We are excited to share our latest cryo-EM study of the human INO80 remodeler, now featured as a Breakthrough article in NAR @narjournal.bsky.social Check it out here and a big shoutout to @priyanka-pdm.bsky.social and Manmohan et al. for their contributions! 🧬

Nucleic Acids Research@narjournal.bsky.social · 5mo ago

⭐NAR Breakthrough! ⭐ 🧬 New #cryo-EM work shows the #humanINO80 motor adapts to DNA unwrapping and can remodel altered particles like #hexasomes - highlighting its versatility across #nucleosome states. 🔬✨ @lmu.de @genecenter-lmu.bsky.social Read the full article here: doi.org/10.1093/nar/...

When art meets science! 🤩 Check out Drew's stunning animation of the cellular machinery behind homologous recombination — featuring our favorite DNA repair complex MRN, and other DNA repair heroes! 🧬🔧 @drewberry.bsky.social

SFB1361@sfb1361.bsky.social · 8mo ago

Loving @drewberry.bsky.social's beautiful animation of DNA break repair by HR - featuring the MRN complex architecture and function inspired by the research from @hopfnerlab.bsky.social! Dive into the science behind it🧬 www.sciencedirect.com/science/arti... www.nature.com/articles/s41...

🧐Curious about what has happened at the Gene Center over the past 5 years? Take a look at our hot-off-the-press report.🤩 www.genzentrum.uni-muenchen.de/institute/ab...

📣Publication alert! A team led by Roland Beckmann shows: Ribosome collisions activate the kinase ZAK and thus trigger the ribotoxic stress response — a key mechanism of the cellular stress defense. More about it here👇 www.lmu.de/en/newsroom/...

Colliding ribosomes signal cellular stress

LMU researchers uncover the mechanism by which ribosomes raise alarms in the cell.

lmu.de

Check out our paper on nucleosome positioning by our favorite remodeler INO80 in a collaboration with the Bartholomew Lab, finally out in MolCell 🧬 kwnsfk27.r.eu-west-1.awstrack.me/L0/https:%2F...

Gene Center Munich @LMU Munich@genecenter-lmu.bsky.social · 8mo ago

📣Publication alert! Collaboration between Bartholomew lab and @hopfnerlab.bsky.social shows that INO80 positions nucleosomes at specific genomic sites by sensing intranucleosomal DNA shape and stalling at rigid DNA via its Arp5 subunit. authors.elsevier.com/c/1m9kd3vVUP... @mdanderson.bsky.social

Excited to share our latest contribution in a collab with Helle Ulrich's Lab. Great work by Ronald and Mariia! Thanks to @sfb1361.bsky.social and @imbmainz.bsky.social 🧬🔨

SFB1361@sfb1361.bsky.social · 10mo ago

New publication!! 📑 Congrats to the Ulrich and @hopfnerlab.bsky.social labs on their latest work exploring how the INO80 chromatin remodeller facilitates DNA damage bypass via postreplicative gap repair. 🔎Read the paper here: www.embopress.org/doi/full/10.1038/s44318-025-00580-4

Thrilled that our work is now finally out in Nature Comms! rdcu.be/eG3vP We reveal cryo-EM structures of the MRN complex bound to DNA & TRF2 - showing how DNA breaks are sensed and regulated at telomeres. Fantastic work by first authors @yilanfan.bsky.social @filizkuybu.bsky.social & Hengjun!

Feeling recharged after our lab retreat in Obergurgl 🌞⛰️ Great hikes, perfect weather, motivating talks from @oliveiramann.bsky.social, Liudmila Andreeva and lots of inspiring discussions. Big thanks for the warm hospitality!

We‘re proud to share that our #SFB1361 PhD student, Yilan Fan from the @hopfnerlab.bsky.social, has been awarded a poster prize at the CNIO-CaixaResearch Frontiers Meeting “Machines on DNA and RNA: A Molecular Mechanistic Perspective“ held on 28-30 May 2025 in Madrid, Spain. Congrats! 🎉

Check out our pre-print on how the human INO80 complex acts on nucleosomes and hexasomes: PostDocs Priyanka & Manmohan et al. solved structures of INO80 bound to several substrates and completed missing questions about similarities of modes of actions across species🧬 www.biorxiv.org/content/10.1...

Recognition and remodelling of nucleosomes and hexasomes by the human INO80 complex

The ATP-dependent INO80 chromatin remodeller slides and repositions nucleosomes to shape and maintain chromatin around gene regulatory elements and replication origins. Recent work uncovered capabilit...

biorxiv.org

Now peer reviewed and in its final form @natcomms.nature.com www.nature.com/articles/s41...

Allosteric activation of the SPRTN protease by ubiquitin maintains genome stability - Nature Communications

The DNA-dependent protease SPRTN cleaves toxic DNA-protein crosslinks (DPCs). Here, the authors show that SPRTN is activated by DPC-ubiquitylation through an allosteric ubiquitin binding interface. Th...

nature.com

Julian Stingele@jstingele.bsky.social · 2y ago

Happy to share our latest work🍾 🥳 PhD student Sophie Dürauer discovered together with many wonderful collaborators that the ubiquitylation of DNA-protein crosslinks promotes their cleavage by SPRTN more than 100-fold 🧬🔧

Happy to share our latest pre-print! We solved the cryoEM structures of human DNA repair factor MRN bound to DNA and to TRF2. Main work of Yilan, Filiz @filizkuybu.bsky.social and Hengjun. Great collab within the @sfb1361.bsky.social and @genecenter-lmu.bsky.social 🧬🔨 www.biorxiv.org/content/10.1...

Structural basis for DNA double-strand break sensing by human MRE11-RAD50-NBS1 and its TRF2 complex

The MRE11-RAD50-NBS1 (MRN) complex is a central, multifunctional factor in the detection, signaling and nucleolytic processing of DNA double-strand breaks (DSBs). To clarify how human MRN binds generi...

biorxiv.org

Hello, Bluesky! To kick things off here, we’re excited to share: The SLFN11 story continues! We combined cryo-EM and biochemical assays to explain how phosphorylation regulates SLFN11´s tRNA cleavage and ssDNA binding activities. Check out our new paper here www.nature.com/articles/s41... + movie