PfefferCryoLab

Congratulations to the shared first authors @wuertzmartin.bsky.social and Giulia Tonon. Fantastic collaboration with the Schiebel Lab @zmbh.uni-heidelberg.de‬, @fabiololicato.com @bzh-hd.bsky.social, the Eustermann Lab @embl.org, and @erhardtlab.bsky.social @kit.edu. Thanks to all who contributed!

Nearly two decades after augmin's discovery in Drosophila, we have reconstituted the microtubule-binding region of the Drosophila augmin complex on microtubules and demonstrate the conserved mechanism by which augmin subunit HAUS6 orients augmin for microtubule branching.

Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching - Nature Communications Augmin is essential for microtubule nucleation during cell division. This study reveals how the conserved calponin homology domain of the augmin subunit HAUS6 binds to microtubules to orient augmin fo...

We are excited to share our latest work elucidating the structural basis for how augmin binds to microtubules. Out just now @natcomms.nature.com :

www.nature.com/articles/s41...

Great collaboration with the Melnikov Lab @sergeymelnikov.bsky.social and the Hill Lab @chillzaa.bsky.social. Congratulations to all authors, in particular the shared first authors Karla Helena Bueno and Sophie Kopetschke sophiekopetschke.bsky.social.

Structurally heterogeneous ribosomes cooperate in protein synthesis in bacterial cells - Nature Communications Cells can simultaneously produce structurally dissimilar ribosomes, suggesting functional specialization of distinct ribosome populations. Here, the authors show that distinct ribosomes cooperate rath...

Out just now @naturecomms.bsky.social: using cryo-EM and cryo-electron tomography, we provide evidence that structurally heterogeneous ribosomes can cooperate in protein synthesis in bacterial cells:

www.nature.com/articles/s41...

Structurally heterogeneous ribosomes cooperate in protein synthesis in bacterial cells - Nature Communications Cells can simultaneously produce structurally dissimilar ribosomes, suggesting functional specialization of distinct ribosome populations. Here, the authors show that distinct ribosomes cooperate rath...

Here we unexpectedly find that the ribosomal protein S20/L26—identified at the dawn of ribosome research but later deemed a biochemical artifact—is indeed a genuine component of the large ribosomal subunit. More on this ribosome content variation is here: www.nature.com/articles/s41...

Thanks, Friedrich!

Thanks a lot, Marius!

A great collaboration with the Schiebel Lab @zmbh.uni-heidelberg.de and the Gruss Lab @unibonn.bsky.social. Congratulations to all authors, in particular the shared first authors Qi Gao, Florian Hofer @florianwhofer.bsky.social, Bram Vermeulen @bram-vermeulen.bsky.social and Sebastian Filbeck!

Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC - Nature Communications The γ-TuRC plays a central role for nucleation of microtubules at the centrosome. Here, the authors dissect structural mechanisms for centrosomal recruitment and regulation of the γ-TuRC and identify ...

Online today at @naturecomms.bsky.social and a great opportunity for our first post @bsky.app: in a major team effort, we reveal the structural mechanisms for centrosomal recruitment and organization of the human microtubule nucleator γ-TuRC: www.nature.com/articles/s41...