7PRD

Solution structure of the chimeric Nrd1-Nab3 heterodimerization domains

7PRD の概要

• エントリーDOI: 10.2210/pdb7prd/pdb
• NMR情報: BMRB: 34668
• 分子名称: Protein NRD1,HLJ1_G0022400.mRNA.1.CDS.1 (1 entity in total)
• 機能のキーワード: transcription termination, nns pathway, nab3, nrd1, heterodimerization, chimera, yeast, transcription
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13943.86

構造登録者

Chaves-Arquero, B.,Martinez-Lumbreras, S.,Perez-Canadillas, J.M. (登録日: 2021-09-21, 公開日: 2022-01-12, 最終更新日: 2024-06-19)

主引用文献

Chaves-Arquero, B.,Martinez-Lumbreras, S.,Camero, S.,Santiveri, C.M.,Mirassou, Y.,Campos-Olivas, R.,Jimenez, M.A.,Calvo, O.,Perez-Canadillas, J.M.
Structural basis of Nrd1-Nab3 heterodimerization.
Life Sci Alliance, 5:-, 2022

PubMed Abstract: Heterodimerization of RNA binding proteins Nrd1 and Nab3 is essential to communicate the RNA recognition in the nascent transcript with the Nrd1 recognition of the Ser-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.

PubMed: 35022249
DOI: 10.26508/lsa.202101252

実験手法

SOLUTION NMR