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Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, inhibits translation by trapping release factors 1 or 2 associated with ribosomes and arresting termination. Cover art by Erin Dewalt, image from Lorenzo Viola/EyeEm/Getty Images. (p 752)
Group II chaperonins facilitate protein folding by undergoing ATP-driven conformational changes. A recent study reveals a tunable allosteric network in group II chaperonins that includes a residue at the intersubunit interface, which is important for assembly and allosteric coordination. The authors also propose that lower cooperativity allows group II chaperonins to achieve optimal substrate folding over a broad range of ATP concentrations.
The monoallelic expression of many imprinted genes in mammals depends on DNA methylation marks that originate from the germ cells. Recent studies in mice and fruit flies evoke a novel, transient mode of genomic imprinting in which oocyte-acquired histone H3 Lys27 trimethylation (H3K27me3) marks are transmitted to the zygote and modulate the allele specificity and timing of gene expression in the early embryo.
The robustness of the circadian clock deteriorates with aging. Two new studies show that aging reprograms the circadian transcriptome in a cell-type-dependent manner and that such rewiring can be reversed by caloric restriction.
In this Review, Peña, Hurt and Panse discuss our current knowledge on the eukaryotic ribosome assembly, a complex process that takes place across different cellular compartments and involves over 200 assembly factors.
Rps26 promotes translation by recognition of the Kozak sequence in well-translated mRNAs, whereas exposure to cellular stress leads to formation of Rps26-deficient ribosomes, which preferentially translate stress-response mRNAs with Kozak sequence deviations.
The activities of human holophosphatases R15A–PP1 and R15B–PP1 on substrate eIF2α are now reconstituted in vitro, revealing that inhibitors Guanabenz and Sephin1 induce a selective conformational change in R15A and impair the recruitment of eIF2α.
Using a combination of crystallography, SAXS and cryo-EM, the katanin hexamer is observed in spiral or ring arrangements, suggesting a mechanism to generate the power stroke to severe microtubules.
Identification of a tunable network of covarying residues within group II chaperonins suggests how these proteins support robust folding of their clients over a wide range of metabolic conditions.
Functional analysis of TRF2-RuvC chimeras establishes that binding of the TRF2 basic domain to branched-DNA structures of the t-loop is responsible for telomere protection in mouse and human cells.
Structural insight into TIR-domain interactions, which are essential for the recruitment of signaling adapters to Toll-like receptors during innate immune responses, demonstrates a conserved interaction mode involved in both TLR and IL-1R signaling.
Crystal structures of human endothelin ETB receptor bound to bosentan and to ETB-selective derivative provide insight into the basis of antagonism by these drugs.
Computational analyses of the yeast proteome and experimental work show that homorepeats facilitate protein-protein interactions and rapid protein divergence. To balance their propensity to aggregate, homorepeats are preferentially retained in proteins that are stringently regulated.
In echinoderm mitochondria, the codon AAA encodes asparagine instead of lysine. A newly identified nucleoside modification, hydroxy-N6-threonylcarbamoyladenosine (ht6A), is found adjacent to the anticodon in mt-tRNALys and prevents mt-tRNALys from misreading AAA as lysine.
