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p53 oscillations in response to DNA damage lead to oscillatory p53 DNA-binding dynamics, whereas post-transcriptional mechanisms are responsible for the differences in gene expression dynamics.
PCSK9 binds to and promotes degradation of LDLR, thus regulating serum levels of LDL. An accessible groove in PCSK9, adjacent to the LDLR-binding site, can be targeted by peptides that disrupt the LDLR interaction.
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.
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.
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.
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.
Meiotic progression is controlled by cytoplasmic polyadenylation and translational activation of masked, maternal mRNAs. RNA-binding-protein interactions with adjacent cis elements cause local conformational changes to the mRNAs that determine the extent and timing of their activation.
An unusual pairing of homologous X chromosomes occurs during X inactivation. A new study in mouse embryonic stem cells shows that telomeres and the telomeric RNA PAR-TERRA are responsible for additional pairwise interactions that guide Xic–Xic pairing.
The ribosome-associated complex (RAC) is formed by the JD protein Zuo1 and the unconventional Hsp70 Ssz1. This Review presents recent developments that have increased our understanding of RAC's mechanisms and cellular functions.
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.
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.
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.
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.
New data reveal how Musashi binding to Xenopus oocyte mRNAs promotes changes in RNA secondary structure that modulate CPEB1 binding and influence polyadenylation and translational efficiency.
The crystal structure of Thermotoga maritima lysophosphatidic acid acyltransferase reveals a two-helix motif that positions the active site for catalysis within the membrane bilayer.
New analyses reveal that TERRA transcripts arising from the subtelomeric pseudoautosomal (PAR) region of sex chromosomes nucleate pairing of X alleles in mouse ES cells.
Single-molecule spectroscopy analyses of titin fragments from modern animals and reconstructed from the last common ancestors to mammals, sauropsids and tetrapods shed light on the evolution of the mechanical properties of muscle titin from the Paleozoic to our days.
Structural analysis of the uridyl transferases TUT4 and TUT7 reveals the use of two functional modules in the switch from monouridylation of pre-let-7, which promotes let-7 expression, to oligouridylation of pre-let-7, which marks it for degradation.