Nicolae Solcan

TL;DR: The RNA-binding protein hnRNPK is identified as the principal XR-PID binding factor required to recruit PCGF3/5-PRC1, providing important insights into mechanisms of chromatin modification by non-coding RNA.

TL;DR: Crystallized in an inward open conformation the structure identifies a hinge‐like movement within the C‐terminal half of the transporter that facilitates opening of an intracellular gate controlling access to a central peptide‐binding site, which supports a model for peptide transport that highlights the importance of salt bridge interactions in orchestrating alternating access within the POT family.

TL;DR: High-resolution crystal structures of a bacterial POT family transporter, including its complex with a dipeptide analog, alafosfalin, revealed the key mechanistic and functional roles for a conserved glutamate residue (Glu310) in the peptide binding site.

TL;DR: It is shown that, for all the current structures of MFS transporters, the first two helices of each of the four inverted-topology repeat units form half of either the periplasmic or cytoplasmic gate and that these function cooperatively in a scissor-like motion to control access to the peptide binding site during transport.

TL;DR: Crystal structures of di‐ and tripeptide‐bound complexes of a bacterial homologue of PepT1 reveal at least two mechanisms for peptide recognition that operate within a single, centrally located binding site, and suggest that transport promiscuity has arisen in part through the ability of the binding site to accommodate peptides in multiple orientations for transport.