Jakob Farnung

@jakobfarnung.bsky.social

PostDoc Schulman Lab, MPI Biochemistry; formerly Bode Lab, ETH Zürich

Very happy to see the final version of our work on the structure and composition of cytoplasmic lattices in mouse embryos, previously shared on bioRxiv, now published in The EMBO Journal! Many thanks to our editor, Ieva Gailite, and the reviewers for their constructive input.

The EMBO Journal@embojournal.org · 2w ago

What’s the function of embryonic ‘cytoplasmic lattices’? Using cryo-ET, @kashishsingh.bsky.social @carter-lab.bsky.social and coworkers reveal them as megadalton-size hubs of ubiquitination proteins/ubiquitin transfer link.springer.com/article/10.1...

⚡New preprint from the lab⚡: A key early checkpoint in gene expression is promoter proximal pausing of RNA polymerase II. For over 20 years, we as field have not been able to recreate pausing under realistic cellular conditions. @robertovn.bsky.social shows that ELOF1 is the missing piece.

Roberto Vázquez Núñez@robertovn.bsky.social · 3mo ago

🚨 New preprint: GATO-seq did it again! ELOF1 is the missing promoter-proximal factor that confers RNA Pol II resistance to TFIIF. Including ELOF1, DSIF, and NELF in GATO-seq reactions recapitulates promoter-proximal pausing in vitro at physiological conditions for the 1st time. tinyurl.com/ELOF1

Excited that Della Syau's PhD work is now available as a NAR Breakthrough article: academic.oup.com/nar/article/.... Della's work clarifies how IWS1 engages the transcription elongation complex, stimulates transcription, and controls association of other factors such as RECQL5.

Structure and function of IWS1 in transcription elongation

Abstract. Transcription elongation by RNA polymerase II is a tightly regulated process that requires coordinated interactions between transcription elongat

academic.oup.com

Glückwunsch, Bruderherz! Really outstanding work by @bartellab.bsky.social and Schulman Lab. This is how transatlantic research is done 🇺🇸🇩🇪.

Jakob Farnung@jakobfarnung.bsky.social · 5mo ago

The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation (TDMD) is now published! 🎉🍾 We, @bartellab.bsky.social and Schulman lab, describe how 2-RNA factors control protein degradation by recruiting an E3 ligase. @mpibiochem.bsky.social www.nature.com/articles/s41...

Congratulations, @leokiss.bsky.social ! 🎉🎉 looking forward to the exciting research of the Kiss lab. This is a great opportunity for prospective PhD students interested in doing cutting-edge research 🧪 on ubiquitin!

Leo Kiss@leokiss.bsky.social · 6mo ago

I am incredibly excited to share that I will start my independent lab at the @unidue-zmb.bsky.social at the @unidue.bsky.social as Junior Professor of Cellular Biochemistry. Research in my lab has the goal to decipher the ubiquitin code! There are multiple open positions! (1/3)

🧪🧬New preprint We present cryo-EM structures of reconstituted CTCF–nucleosome complexes, showing CTCF dimerization drives nucleosome oligomerization into defined higher-order assemblies. Disrupting CTCF–CTCF interfaces in mESCs reduces looping and impairs differentiation. tinyurl.com/CTCF-nucleos...