In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.
In the cytosol, the proteins constituting cell-matrix adhesion sites form multi-protein building blocks which enter and leave these sites unaltered, thereby contributing to their rapid and correct self-assembly.
Transcriptome and eCLIP analyses in mouse and human reveal splicing factor proline/glutamine rich (SFPQ) as a conserved and critical guardian of long-intron integrity, splicing, and circular RNA (circRNA) production.
The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.
Single-cell splicing of a conserved neuronal kinase is established by a combinatorial code of fate-determining transcription factors and neuronal RNA binding proteins, with different combinations in different neuron types.
Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.