Human plasma contains protein-protected mRNA fragments, myriad repeat RNAs, and novel intron RNAs, including a family of structured full-length excised introns, some corresponding to mirtron pre-miRNAs and agotrons.
A structural analysis of the transcription regulator Mot1 in complex with promoter DNA and the proteins TBP and NC2 provides a first structural framework for how a Swi2/Snf2 type remodeler interacts with a histone fold protein:DNA complex.
The crystal structure of human Holliday junction resolvase GEN1 in complex with DNA reveals a conserved chromodomain as an additional DNA-anchoring point that opens new perspectives for enzyme regulation.
X-ray crystallography reveals that the Dna2 nuclease-helicase contains a long tunnel through which single-stranded DNA threads, and an allosteric mechanism for displacing the DNA-binding protein Rpa that restricts cleavage to the proper polarity.
A combination of X-ray crystallography, molecular dynamics and small angle X-ray scattering shows that the transcription antiterminator M2-1 is a structurally dynamic homotetramer that undergoes large concerted conformational changes upon binding its target RNA.
During CRISPR adaptation, Cas4 forms a ternary complex with the Cas1-Cas2 spacer integration complex, an interaction that coordinates substrate hand-off following precise, PAM-dependent prespacer processing prior to integration.
The molecular mechanism behind how emetine inhibits the ribosome of the human malaria parasite, along with structural details of the complex formed, is revealed at high resolution using cryo-electron microscopy.