title: Chemical shift assignments of the first and second RRMs of Nrd1, a fission yeast MAPK-target RNA binding protein.
abstract: Negative regulator differentiation 1 (Nrd1), a fission yeast RNA binding protein, modulates cytokinesis and sexual development and contributes to stress granule formation in response to environmental stresses. Nrd1 comprises four RRM domains and binds and stabilizes Cdc4 mRNA that encodes the myosin II light chain. Nrd1 binds the Cpc2 fission-yeast RACK1 homolog, and the interaction promotes Nrd1 localization to stress granules. Interestingly, Pmk1 mitogen-activated protein kinase phosphorylates Thr40 in the unstructured N-terminal region and Thr126 in the first RRM domain of Nrd1. Phosphorylation significantly reduces RNA-binding activity and likely modulates Nrd1 function. To reveal the relationship between the structure and function of Nrd1 and how phosphorylation affects structure, we used heteronuclear NMR techniques to investigate the three-dimensional structure of Nrd1. Here we report the1H,13C, and15N resonance assignments of RRM1-RRM2 (residues 108-284) comprising the first and second RRMs obtained using heteronuclear NMR techniques. Secondary structures derived from the chemical shifts are reported. These data should contribute to the understanding of the three-dimensional structure of the RRM1-RRM2 region of Nrd1 and the perturbation caused by phosphorylation.
authors.affiliation: Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan.
authors.forename: Ayaho
authors.initials: A
authors.lastname: Kobayashi
authors.affiliation: Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan.|Bruker BioSpin K. K., 3-9, Moriya-cho, Kanagawa, Yokohama, 221-0022, Japan.
authors.forename: Teppei
authors.initials: T
authors.lastname: Kanaba
authors.affiliation: Laboratory of Molecular Pharmacogenomics, Department of Pharmaceutical Sciences, Faculty of Pharmacy, Kindai University, 3-4-1 Kowake, Higashi-Osaka, 577-8502, Japan.
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Satoh
authors.affiliation: Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan.
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Ito
authors.affiliation: Laboratory of Molecular Pharmacogenomics, Department of Pharmaceutical Sciences, Faculty of Pharmacy, Kindai University, 3-4-1 Kowake, Higashi-Osaka, 577-8502, Japan.
authors.forename: Reiko
authors.initials: R
authors.lastname: Sugiura
authors.affiliation: Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, 192-0397, Japan. mishima-masaki@tmu.ac.jp.
authors.forename: Masaki
authors.identifier: http://orcid.org/0000-0001-7626-7287
authors.initials: M
authors.lastname: Mishima
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D012568:Schizosaccharomyces; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D012261:Ribonucleoproteins; D029702:Schizosaccharomyces pombe Proteins; C491210:nrd1 protein, S pombe
keywords: Cpc2; NMR assignments; Nrd1; RACK1; RRM