Year: 2022
Type: article
Abstract: -phosphorylated Rbp1 C-terminal domain in RNA polymerase II. The structure of a Nrd1-Nab3 chimera reveals the basis of heterodimerization, filling a missing gap in knowledge of this system. The free form of the Nrd1 interaction domain of Nab3 (NRID) forms a multi-state three-helix bundle that is clamped in a single conformation upon complex formation with the Nab3 interaction domain of Nrd1 (NAID). The latter domain forms two long helices that wrap around NRID, resulting in an extensive protein-protein interface that would explain the highly favorable free energy of heterodimerization. Mutagenesis of some conserved hydrophobic residues involved in the heterodimerization leads to temperature-sensitive phenotypes, revealing the importance of this interaction in yeast cell fitness. The Nrd1-Nab3 structure resembles the previously reported Rna14/Rna15 heterodimer structure, which is part of the poly(A)-dependent termination pathway, suggesting that both machineries use similar structural solutions despite they share little sequence homology and are potentially evolutionary divergent.
Source: Life Science Alliance
Institutions: Consejo Superior de Investigaciones Científicas, Instituto de Química Física Blas Cabrera, University College London, Helmholtz Munich, Technical University of Munich, Spanish National Cancer Research Centre, Barcelona Institute of Science and Technology, Centre for Genomic Regulation, Centro Nacional de Análisis Genómico, Universidad de Salamanca, Instituto de Biología Funcional y Genómica
Language: English
Topic: RNA Research and Splicing
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,500
Awards: G1175115578, G1520406698, G2262748287, G2551911579, G2972037462, G300979063, G34346518, G3480869486, G410571670, G4246625193, G425668148, G451917667, G488842982, G4889743685, G5080475149, G5455491370, G5903000213, G5967599077, G6080697404, G632910720, G7607029581, G790656459, G855041801, G8656596189, G929308097
OpenAlex ID: W4205964584