Fruzsina Hobor

TL;DR: Biochemical and structural data revealed that affinity and specificity of RNA recognition by Nab3p relies on induced fit recognition implicating an α‐helical extension of the RNA recognition motif, suggesting that they function as general transcriptional insulators to prevent interference between the non‐coding and the coding yeast transcriptomes.

TL;DR: It is reported that Syncrip’s amino-terminal domain, which was previously thought to mediate protein–protein interactions, is a cryptic, conserved and sequence-specific RNA-binding domain, designated NURR (N- terminal unit for RNA recognition).

TL;DR: A comparative analysis of multiple CAS methods is described, which highlights effective approaches to improve the accuracy of predicting hot-spot residues and introduces a new method, BUDE Alanine Scanning, which can be applied to single structures from crystallography and to structural ensembles from NMR or molecular dynamics data.

TL;DR: It is shown that Air2p is an RNA-binding subunit of TRAMP, and the RNA binding part of the Mtr4p arch, the KOW domain, is uncovered as the essential component for TRAMP-mediated exosome activation.

TL;DR: The solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element is reported, showing that the first three nucleotides of UCUU are accommodated on the β-sheet surface of Nab 3 RRM, but reveals a sequence-specific recognition only for the central cytidine and uridine.