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La-related protein 1 specifically and directly binds the 5' cap and first nucleotide of mRNAs encoding ribosomal proteins and translation factors, inhibiting the assembly of translation initiation factors on these messages and therefore their translation.

Aberrant neddylation of non-cullin substrates disrupts normal cell cycle progression.

A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.

Fam20A, a pseudokinase involved in the formation of tooth enamel, binds ATP in an unexpected orientation.

The CDC25 family protein phosphatase Mih1 promotes downregulation of cell surface proteins in budding yeast by dephosphorylating a subunit of the retromer complex, which mediates plasma membrane recycling.

Along with preventing D-amino acids from being incorporated into proteins, D-aminoacyl-tRNA deacylase clears achiral glycine that is incorrectly attached to tRNA^Ala.

After DNA replication, nucleosomes are assembled by two histone chaperone complexes each bound to an H3-H4 histone dimer, suggesting the feasibility for a semi-conservative mode of epigenome inheritance.

The CAF1 complex binds single histone H3-H4 dimers, and two such complexes associate with extended DNA elements to ensure the deposition of H3-H4 tetramers, the first step in the assembly of nucleosomes.

Phosphorylated translation initiation factor eIF2, a potent inhibitor of protein synthesis in eukaryotic cells, is also inhibitory to protein synthesis when bound to GTP and initiator tRNA broadening the reach and immediacy of eIF2-mediated control.

An integrated biochemical and evolutionary analysis shows how enzyme specificity evolves after gene loss during genome decay, implicating relaxation of purifying selection as a driving force for functional divergence.