5AGQ

Solution structure of the TAM domain of human TIP5 BAZ2A involved in epigenetic regulation of rRNA genes

5AGQ の概要

• エントリーDOI: 10.2210/pdb5agq/pdb
• NMR情報: BMRB: 26517
• 分子名称: BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A (1 entity in total)
• 機能のキーワード: transcription, tam domain, tip5/baz2a, protein rna interaction, epigenetics, rrna gene silencing
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13417.30

構造登録者

Anosova, I.,Melnik, S.,Tripsianes, K.,Kateb, F.,Grummt, I.,Sattler, M. (登録日: 2015-02-03, 公開日: 2015-05-06, 最終更新日: 2024-06-19)

主引用文献

Anosova, I.,Melnik, S.,Tripsianes, K.,Kateb, F.,Grummt, I.,Sattler, M.
A Novel RNA Binding Surface of the Tam Domain of Tip5/Baz2A Mediates Epigenetic Regulation of Rrna Genes.
Nucleic Acids Res., 43:5208-, 2015

PubMed Abstract: The chromatin remodeling complex NoRC, comprising the subunits SNF2h and TIP5/BAZ2A, mediates heterochromatin formation at major clusters of repetitive elements, including rRNA genes, centromeres and telomeres. Association with chromatin requires the interaction of the TAM (TIP5/ARBP/MBD) domain of TIP5 with noncoding RNA, which targets NoRC to specific genomic loci. Here, we show that the NMR structure of the TAM domain of TIP5 resembles the fold of the MBD domain, found in methyl-CpG binding proteins. However, the TAM domain exhibits an extended MBD fold with unique C-terminal extensions that constitute a novel surface for RNA binding. Mutation of critical amino acids within this surface abolishes RNA binding in vitro and in vivo. Our results explain the distinct binding specificities of TAM and MBD domains to RNA and methylated DNA, respectively, and reveal structural features for the interaction of NoRC with non-coding RNA.

PubMed: 25916849
DOI: 10.1093/NAR/GKV365

実験手法

SOLUTION NMR