Our first 2021 paper reveals the prevalence and mechanism of a co-translational protein assembly mechanism in human cells: co-co assembly.
Congratulations to the co-co team @KaiFenzl, @matildebertolin and @guenter_kramer!
https://t.co/dTUfKZ06If
@Sciart by @munafomarzia
1/6
What shall Germany deliver next? A good question posed by @faznet, thanks 🙏🏻 Well, the answer is obvious:
Ukraine desperately needs 🇩🇪 fighter jets Tornados & Eurofighters💪
Dear German Government, please do not hesitate
Just do the right thing!
https://t.co/KL7o31erfX
Our team will combine advanced ribosome profiling, cryo-EM and single-molecule experiments, to study how multiple ribosomes, mRNAs, nascent chains, chaperones and other factors form dynamic super-assemblies that act as coordinated protein complex assembly lines.
Great news! Together with @sjtans & @The_Ban_Lab, we are among this year's recipients of a Synergy Grant from @ERC_Research. This marks the beginning of an exciting journey into a mechanistic analysis of the biogenesis of protein complexes 🧬
Hier eine schöne Allegorie wie das von @LabJoazeiro und @PfefferCryoLab beschriebene MutS2 Protein fehlerhafte Proteinbiosynthese anhand kollidierter Ribosome erkennt und verschiedene Qualitätskontrollmechanismen initiiert bevor das fehlerhafte Protein der Zelle schaden kann.
Auffahrunfall auf der „Ribosomen-Autobahn“: Wissenschaftler identifizieren bakterielles Protein, das „stehengebliebene“ Ribosomen erkennt und rettet
@ZmbhH
https://t.co/sEuA2KHraY
How do cells fire up the #RQC engine? Check out our structural and mechanistic blueprint for bacterial #ribosome collision sensing by MutS2, out today in @Nature. MutS2 senses collisions and splits ribosomes to initiate RQC!
https://t.co/SNl3eK2Qkw
B. subtilis MutS2/RqcU deals with stalled ribosomes by binding collided disomes, recruits the RNA degradosome and initiates #RQC by #ribosome splitting. Happy we could contribute to this work led by @LabJoazeiro in collaboration with @PfefferCryoLab https://t.co/US3DJqGyc7
A team of researchers led by ZMBH's PIs C. Joazeiro @LabJoazeiro and S. Pfeffer @PfefferCryoLab discovered how the bacterial MutS2 protein prevents damage by stalled ribosomes! Further details in Nature https://t.co/ZMiSZDxPVb
Comparative SUMO proteome analysis identifies novel SUMO-controlled regulators in EGFR signaling - paper by a team led by @frauke_melchior https://t.co/IOVPBkFakV
@bioSavinov Hi Andrew, that's a good question! Indeed, our method may enrich for more stable interactions which survive the purification procedure. Some additional work in the lab suggests we are not missing many disomes by DiSP, but it is definitely worth further investigation :)
@AChemSynBio Thanks Abhishek, glad you enjoyed our work! That's a good question, some heteromeric subunits are indeed hits of our screening, but they await deeper investigation!!
Our first 2021 paper reveals the prevalence and mechanism of a co-translational protein assembly mechanism in human cells: co-co assembly.
Congratulations to the co-co team @KaiFenzl, @matildebertolin and @guenter_kramer!
https://t.co/dTUfKZ06If
@Sciart by @munafomarzia
1/6
Our data suggest that co-co assembly generally involves neighbouring ribosomes on one mRNA, thereby ensuring specific homomer formation of isoforms and structurally-related proteins which are highly prone to promiscuous interactions inside cells.
5/6
How do you synthesize proteins with only half a ribosome? We are excited to share our work on the structural basis of Alanine tailing in bacterial ribosome-associated quality control (RQC). Great collaboration with @LabJoazeiro@ZmbhH.
https://t.co/LERrasmFtS
PNAS selected our joint work with @BukauLab on the mechanism of fiber disaggregation to be highlighted on their journal club blog! @PNASNews
https://t.co/kK1866YRHg