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Analysis of the relationships between transcription, replication, and stability of large genes associated with common fragile sites suggests that high transcription levels alleviate genome instability by altering replication timing and allowing cells to complete replication before mitosis.
Comparative genome-wide analyses reveal that DNA replication origins fire near the initiation site of highly transcribed genes, ensuring co-directional replication and transcription in highly active regions of the human genome.
Cryo-EM structures of rat TRPV2 reveal the architecture of the full-length pore turret and suggest the regulatory role that the turret and lipid binding have in coupling the lower and upper gates of the channel.
The cryo-EM structure of budding yeast supercomplex III2IV2 is now presented, providing molecular details of CIV (also known as cytochrome c oxidase) and revealing notable differences with mammalian systems.
Structures of yeast mitochondrial supercomplexes III2IV and III2IV2 are determined by cryo-EM, revealing the interactions between CIII and CIV and an overall different architecture compared to mammalian assemblies.
The cryo-EM structure of the N-terminal acetyl transferase NatA in complex with the ribosome shows that NatA is dynamically positioned underneath the ribosomal exit tunnel to facilitate modification of the emerging nascent peptide chain.
Rubinstein and colleagues report a structure of the obligate respiratory III2IV2 supercomplex from M. smegmatis, revealing two functionally relevant conformations of the cytochrome cc subunit and a SOD subunit that may detoxify reactive oxygen species.
A combination of proteomics and structural analyses reveals the assembly mechanism of transcription factor TFIID in human cells and identifies the chaperonin CCT as a checkpoint in the process.
Point centromeres of budding yeast direct binding of a CBF3 complex that recruits the centromere-specific Cse4 nucleosome to CEN loci. A cryo-EM structure of CBF3 bound to its cognate CDEIII element and a model of the CBF3–Cse4–CEN complex reveal interactions underlying kinetochore assembly.
This structure of human PTH1R, a key target for the treatment of osteoporosis, reveals the agonist binding mode and molecular details within conserved structural motifs critical for class B GPCR function.
A PxL motif is identified in substrates of yeast phosphatase Cdc14. PxL functions as a docking motif for substrates and contributes to the timing of dephosphorylation during mitotic exit.
SLFN11 sensitizes cancer cells to therapeutic drugs by selectively catalyzing the cleavage of Leu-TAA and Leu-AAG tRNAs in response to camptothecin DDA treatment, thereby inhibiting the translation rate of proteins enriched for these codons.
The lncRNA SAMMSON promotes a balanced increase in rRNA maturation and protein synthesis in the cytosol and mitochondria by modulating the localization of CARF, which affects two rRNA-processing factors.
Baker, Marcos and colleagues analyze β-arches (loops connecting unpaired β-strands) and derive rules used for de novo design of a hyperthermostable jellyroll structure, with eight antiparallel β-strands forming double-stranded β-helices.
A new class of miRNA-recognition elements that function exclusively in protein-coding regions use distinct target-recognition rules and mediate translational repression instead of mRNA destabilization.
A combination of fluorescence approaches that permit conformational changes of SNARE proteins to be visualized in different lipid environments reveals interactions underlying vesicle–membrane fusion.
Crystal structures of the Ku70/80–DNA complex with Ku binding motifs of APLF and XLF reveal distinct interaction sites and an induced conformational change in Ku80 critical for function in NHEJ repair.
Histone variant macroH2A is initially pervasively deposited across the mouse genome and is subsequently selectively evicted from transcriptionally active regions to establish macroH2A chromatin domains.
Crystal structures of human σ1 receptor bound to the antagonists haloperidol and NE-100, and to agonist (+)-pentazocine, alongside MD simulations, reveal a unique binding pose for, and major conformational rearrangements induced by, the agonist.