Marie Winz

Postdoc positions in Nuclear RNA Biology - Vacancy at Aarhus University Vacancy at Department of Molecular Biology and Genetics - RNA Biology and Innovation, Aarhus University

Postdoc positions available in my lab in Aarhus, Denmark on 'Mammalian Nuclear RNA Production and Turnover Systems'. Please get in touch for further information or simply apply here:
mbg.au.dk/en/news-and-...

Want to map protein-RNA interactions? Check out our new iCLIP3 protocol. Featuring steamlined library prep and visualisation of protein-RNA complexes without radioactivity! Bioinformatics workflow on top :)

With the Müller-McNicoll and Zarnack labs!
@zarnack-group.bsky.social @mixmue.bsky.social

Exciting news:
Our RNA community in @uniregensburg.bsky.social is set to grow!

We are opening a Junior Group Leader position in RNA biochemistry / ribonucleases / RNA stability. A great opportunity to start your own team within our collaborative RNA network.

Details & application 👇

iCLIP3: A streamlined, non-radioactive protocol for mapping protein-RNA interactions in cellular transcripts at single-nucleotide resolution https://www.biorxiv.org/content/10.64898/2026.03.01.708747v1

#PhDPosition #RibosomeBiology #TranslationQC #Biochemistry #Nanopore #YeastGenetics #JGU #Mainz #TRR319 #YouRMaP #ScienceJobs #Germany #BlueskyJobs

🌟 Why us?
→ Cutting-edge tools + collaborative lab
→ Structured PhD training (TRR319 / YouRMaP)
→ Help shape the lab’s future — you’re not just joining, you’re building

📩 Apply now → link above. Questions? DM or email us!

🧑‍🔬 Who Should Apply?
✅ M.Sc. in MolBio/Biochem/related (or soon to graduate)
✅ Lab skills + interest in sequencing/bioinfo
✅ Fluent in English & German (required!)
✅ Will teach a Chem practical (basic Chem knowledge needed)

Are you into:
🔬 ribosome assembly?
🧬 RNA modifications?
🧫 yeast genetics + nanopore sequencing?
🧩 translation quality control & rescue factors?

→ Pick your project:
1️⃣ Ribosome biogenesis & RNA mods
2️⃣ Jlp2 — a new ribosome rescue factor

#PhDPosition open — #RibosomeBiology & #Translation QC
📍 JGU Mainz, Germany
🗓️ Apply by 10 Mar 2026 (or until filled)
🔗 Full details + project options:
👉 ak-winz.pharmazie.uni-mainz.de/jobs/

Thanks Julian! 😁

Thank you, Leo!

5 - also, we are recruiting a PhD student - join us & spread the news! More details at: ak-winz.pharmazie.uni-mainz.de/jobs/

Yeast elongation factor homolog New1 protects a subset of mRNAs from degradation by no-go decay Abstract. New1 is a homologue of the essential yeast translation elongation factor eEF3. Lack of New1 has been shown to induce ribosome queuing upstream of

4 - Still lots to learn about this mysterious factor.
🔗 Read the paper: academic.oup.com/nar/article/...
Funded by @dfg.de via SFB TRR319-RMaP 🙏
#RibosomeBiology #TranslationQC #RNA #Nanopore #Yeast #PhDPosition #DFG #RMaP #New1

3 - Builds on work from @hauryliuk.bsky.social & @wilsonlab.bsky.social.

Big thanks to our collaborators Liz Petfalski, Tamer Butto and Stefan Pastore, and huge kudos to main heroes from Winz lab: Max Müller and Lena Tittel, as well as @kaushikiyer.bsky.social, and Alina-Andrea Kraft!

We used nanopore sequencing to map Cue2 cleavage sites and find >130 targets - many are essential enzymes & translation factors.
Why do cells keep and even enrich these “risky” codons at the end? We think New1 might be a gatekeeper - turning codon choice into a regulatory signal.

🚀 Just published: New1 shields mRNAs from no-go decay — by preventing ribosome crashes at specific codons.
What’s new?
New1 (eEF3 homolog) stops ribosomes from stalling at C-terminal AAA/AGG/CGU codons. No New1 = collisions + Hel2 recruitment + Cue2-mediated no-go decay.

Peptide-RNA photo-crosslinks with tunable RNA chain map protein-RNA interfaces Photo-crosslinking mass spectrometry enables the identification of protein-RNA interactions in living cells, pinpointing interaction interfaces at single-amino acid resolution. However, current isolat...

New preprint: We isolate peptide–RNA photo-crosslinks with tunable RNA chains from living cells for mass spec. This maps over 4,700 crosslinking sites across 744 proteins and offers the first glimpse into the RNA sequences in crosslinks by MS. Read here: doi.org/10.1101/2025...

Thrilled to announce our #preprint on a new factor in the last line of defense in #translation quality control out on #bioRXiv! Spearheaded by fantastic PhD student @kaushikiyer.bsky.social, supported by Chloé Walter, Alina Kraft, Max Müller and Lena Tittel.

Curiously, Jlp2 acts not only on peptidyl-tRNA on large ribosomal subunits, but also on full monosomes. However, we also show that Jlp2 requires ribosome splitting for activity, suggesting that the monosomes represent re-assembled subunits. Read our preprint for full story!

Instead, we find that Jlp2 acts as a release factor enabling peptide release from ribosome-bound peptidyl-tRNA. We show that Jlp2 acts independently of the RQC complex and of other, known or expected release factors. Through peptide release, Jlp2 maintains cellular fitness in translation stress.

We identify yeast Jlp2 as a translation quality control factor that regulates CAT tailing upon RQC dysfunction, counteracting CAT tail-dependent protein aggregation. However, NOT by physically competing with or influencing abundance or function of Rqc2, the factor that catalyzes CAT tailing.

Stalled or collided ribosomes are split during quality control, leaving aberrant nascent peptides conjugated to tRNA bound to large ribosomal subunits. Those peptides are targeted by #RQC, and ubiquitinated and/or CAT tailed to facilitate degradation. If RQC fails, who comes to the rescue?

Thrilled to announce our #preprint on a new factor in the last line of defense in #translation quality control out on #bioRXiv! Spearheaded by fantastic PhD student @kaushikiyer.bsky.social, supported by Chloé Walter, Alina Kraft, Max Müller and Lena Tittel.

Remodeling of RNA-binding proteome and RNA-mediated regulation as a new layer of control of sporulation | mSystems Understanding how bacteria survive extreme conditions is key to tackling challenges in health, food safety, and industry. This study reveals a previously unexplored layer of control in Bacillus subtil...

Thrilled to share my first last-author paper, just out in #mSystems! A work about #RBPs, #RNA and #sporulation in #subtilis.
Special thanks to my brilliant student T. Kaboré who's signing hist first PhD paper and to the whole team @galinier-lab.bsky.social
👉 journals.asm.org/doi/10.1128/...

#proudPI moment yesterday, seeing my PhD student @kaushikiyer.bsky.social ace his talk at #EMBLProtein conference, presenting his work on new translation quality control factor Jlp2. Really did a great job holding up our lab's flag!!! 😄

Postdoc in Structural Biology of RNA processing complexes Postdoctoral positions in structural biology of macromolecular complexes are available in the laboratory of Dr. Eva Kowalinski at the EMBL Grenoble, France. We are looking for highly motivated and amb...

Postdoc positions in structural biology of RNA processing complexes.

An ERC-funded position will dissect pre-mRNA processing pathways in the infective organism Trypanosoma brucei. An ANR-funded position will characterise large complexes in RNA modification.

Details: tinyurl.com/postdoc-RNA-...

Congrats!

Congrats!!!

Remodeling of RNA-Binding Proteome and RNA-mediated regulation as a new layer of control of sporulation Sporulation allows certain bacteria to survive extreme conditions for extended periods posing challenges to public health and food safety. Transcriptional level of regulation relying on σ factors has ...

🚨 New preprint! 🚨
We just dropped our latest work on RNA-binding proteins and sporulation in B. subtilis! Turns out, the RBP landscape gets a major remix during sporulation 👀. Check it out here 👉 www.biorxiv.org/content/10.1...
#RBP #RNA #sporulation #Bacillus #microbiology @lcbofficiel.bsky.social

UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains Ubiquitin chains determine the fates of their modified proteins, including proteasomal degradation. Kiss et al. present UbiREAD, a technology to monitor cellular degradation and deubiquitination at high temporal resolution after intracellular delivery of ubiquitinated proteins. This reveals a degradation code for ubiquitin chains varying by linkage, length, and topology.

Online Now: UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains Online now: