2OSR

NMR Structure of RRM-2 of Yeast NPL3 Protein

2OSR の概要

• エントリーDOI: 10.2210/pdb2osr/pdb
• 関連するPDBエントリー: 2OSQ
• NMR情報: BMRB: 7382
• 分子名称: Nucleolar protein 3 (1 entity in total)
• 機能のキーワード: npl3, rrm, sr protein, mrna, rna-binding, rna binding protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus, nucleolus: Q01560
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9964.14

構造登録者

Deka, P.,Bucheli, M.,Skrisovska, L.,Allain, F.H.,Moore, C.,Buratowski, S.,Varani, G. (登録日: 2007-02-06, 公開日: 2007-12-18, 最終更新日: 2024-05-22)

主引用文献

Deka, P.,Bucheli, M.E.,Moore, C.,Buratowski, S.,Varani, G.
Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.
J.Mol.Biol., 375:136-150, 2008

PubMed Abstract: Yeast Npl3 is homologous to SR proteins in higher eukaryotes, a family of RNA-binding proteins that have multiple essential roles in RNA metabolism. This protein competes with 3'-end processing factors for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. The NMR structure of its RNA-binding domain shows two unusually compact RNA recognition motifs (RRMs), and identifies the RNA recognition surface in Npl3. Biochemical and NMR studies identify a class of G+U-rich RNA sequences with high specificity for this protein. The protein binds to RNA and forms a single globular structure, but the two RRMs of Npl3 are not equivalent, with the second domain forming much stronger interactions with G+U-rich RNA sequences that occur independently of the interaction of the first RRM. The specific binding to G+U-rich RNAs observed for the two RRMs of Npl3 is masked in the full-length protein by a much stronger but non-sequence-specific RNA-binding activity residing outside of its RRMs. The preference of Npl3 for G+U-rich sequences supports the model for its function in regulating recognition of 3'-end processing sites through competition with the Rna15 (yeast analog of human CstF-64 protein) subunit of the processing complex.

PubMed: 18022637
DOI: 10.1016/j.jmb.2007.09.029

実験手法

SOLUTION NMR