7SXI

Solution Structure of Sds3 Capped Tudor Domain

7SXI の概要

• エントリーDOI: 10.2210/pdb7sxi/pdb
• NMR情報: BMRB: 30969
• 分子名称: Sin3 histone deacetylase corepressor complex component SDS3 (1 entity in total)
• 機能のキーワード: transcriptional corepressor, tudor domain, nucleic acid binding, g-quadruplex binding, gene regulation
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9390.71

構造登録者

Marcum, R.D.,Radhakrishnan, I. (登録日: 2021-11-23, 公開日: 2022-01-19, 最終更新日: 2024-05-15)

主引用文献

Marcum, R.D.,Hsieh, J.,Giljen, M.,Justice, E.,Daffern, N.,Zhang, Y.,Radhakrishnan, I.
A capped Tudor domain within a core subunit of the Sin3L/Rpd3L histone deacetylase complex binds to nucleic acid G-quadruplexes.
J.Biol.Chem., 298:101558-101558, 2022

PubMed Abstract: Chromatin-modifying complexes containing histone deacetylase (HDAC) activities play critical roles in the regulation of gene transcription in eukaryotes. These complexes are thought to lack intrinsic DNA-binding activity, but according to a well-established paradigm, they are recruited via protein-protein interactions by gene-specific transcription factors and posttranslational histone modifications to their sites of action on the genome. The mammalian Sin3L/Rpd3L complex, comprising more than a dozen different polypeptides, is an ancient HDAC complex found in diverse eukaryotes. The subunits of this complex harbor conserved domains and motifs of unknown structure and function. Here, we show that Sds3, a constitutively-associated subunit critical for the proper functioning of the Sin3L/Rpd3L complex, harbors a type of Tudor domain that we designate the capped Tudor domain. Unlike canonical Tudor domains that bind modified histones, the Sds3 capped Tudor domain binds to nucleic acids that can form higher-order structures such as G-quadruplexes and shares similarities with the knotted Tudor domain of the Esa1 histone acetyltransferase that was previously shown to bind single-stranded RNA. Our findings expand the range of macromolecules capable of recruiting the Sin3L/Rpd3L complex and draw attention to potentially new biological roles for this HDAC complex.

PubMed: 34979096
DOI: 10.1016/j.jbc.2021.101558

実験手法

SOLUTION NMR