Volume 29 Issue 5, May 2022

The central apparatus regulates the beating of motile cilia. High-resolution structures of the almost complete central apparatus are now reported in two separate studies, shedding light on the mechanism of ciliary beating and marking a new era in our molecular understanding of cilia architecture and function.

Tagging of the endogenous type II chaperonin TRiC complex using CRISPR knock-in enables its purification for cryo-EM. A series of structures reveal the fate of substrates and co-chaperones inside the TRiC chamber to uncover its inner workings.

V-ATPases acidify the intracellular compartments of eukaryotic cells and their activity is regulated by reversible dissociation of the complex. Cryo-EM structures show the conformational changes associated with assembly and autoinhibition of V-ATPase.

High-resolution (≤1.2 Å) structures of functional states of bacteriorhodopsin reveal the molecular mechanism for generating a membrane proton electrochemical gradient, a key event of cell bioenergetics driving ATP synthesis.

New data show that the HMCES protein suppresses DNA double-strand break formation by cross-linking to and thereby stabilizing an abasic site generated during replication-coupled repair of a DNA interstrand cross-link, thus demonstrating a physiological role of HMCES in DNA repair.

Using single-molecule imaging and manipulation, the authors show linker histone H1 preferentially forms phase-separated droplets with single-stranded nucleic acids over double-stranded DNA and nucleosomes, suggesting a noncanonical nuclear function.

Here, authors solve cryo-EM structures of the central apparatus of motile cilia and analyze its dynamic conformations to elucidate the mechanism of ciliary beating.

Here, the authors use cryo-EM to build atomic models of the central apparatus of motile cilia from Chlamydomonas reinhardtii to shed light on the mechanism of ciliary motility and corresponding disease mutations in human.

Cryo-EM structures of human H1-containing tetranucleosome arrays with distinct, physiological nucleosome repeat lengths reveal that nucleosomes assume a zig-zag arrangement and H1 binds to stacked nucleosomes with longer linker DNA.