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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.
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 analysis of the human CST–Polα/primase complex reveals a metazoan-specific mode of interaction between CST and DNA polymerase α that is proposed to function in telomeric recruitment of Polα/primase for C-strand maintenance.
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.
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.
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.
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.
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.
The CRISPR–Cas enzyme Cas9 faces the challenge of identifying a specific nucleotide sequence within double-stranded DNA. New cryo-EM and biochemical studies show that in the earliest steps of binding, Cas9 bends the DNA and promotes unwinding of two base pairs, enabling it to efficiently scan the sequence of this critical region.
Cryo-EM analysis reveals the mechanism by which chromatin is compacted at the centromere by the H3 histone variant CENP-N. Intriguingly, despite the structural differences between CENP-N and linker H1 histones, both appear to similarly compact higher-order nucleosome structures.
Cryo-EM and biochemical analyses reveal that centromere-associated protein CENP-N promotes centromere-specific nucleosome stacking and higher order structures in vitro and in the cell.
Here, the authors use cryo-EM and biochemical analysis to investigate how the CRISPR-associated protein Cas9 interrogates DNA to locate its RNA-matching target sequence.
Eukaryotes possess several clamp loaders comprising four common subunits and a fifth subunit unique to each complex. The RFC-A–E clamp loader loads the PCNA clamp at 3′-recessed structures for DNA replication. However, swapping a single subunit, Rad24, for RFC-A yields a clamp loader that prefers the 911 clamp and 5′-recessed DNA. Three new studies reveal detailed views of the clamp loading reaction and provide insights into substrate preferences of each loader.
Through structural and functional analyses, this work defines the molecular mechanisms underlying the activation of the insulin receptor (IR) involving multisite insulin binding, paving the way for the eventual therapeutic intervention for diseases caused by aberrant activation of IR.
Comprehensive functional and structural probing of the HIV-1 5′ untranslated region reveals novel interactions that regulate RNA dimerization, Pr55Gag binding and genome packaging into virions.
Cryo-EM structures of the AP2 clathrin adaptor complex describe a new checkpoint in the formation of clathrin vesicles and reveal how a conserved family of regulators called muniscins couple the initial recruitment of AP2 with downstream cargo engagement
