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PfefferCryoLab

@pfeffercryolab.bsky.social

Cryo-electron microscopy, structural biology of molecular machines, ribosome-associated processes, gamma-tubulin complexes

9 Posts126 Follower58 Folgt
PfefferCryoLab@pfeffercryolab.bsky.social · 12mo ago

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...

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...

nature.com

PfefferCryoLab@pfeffercryolab.bsky.social · last yr.

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...

nature.com

Sergey Melnikov@sergeymelnikov.bsky.social · last yr.

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...

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...

nature.com

PfefferCryoLab@pfeffercryolab.bsky.social · last yr.

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...

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 ...

nature.com