4B86

Crystal structure of the MSL1-MSL2 complex (3.5A)

4B86 の概要

• エントリーDOI: 10.2210/pdb4b86/pdb
• 関連するPDBエントリー: 4B7Y
• 分子名称: MALE-SPECIFIC LETHAL 1 HOMOLOG, MALE-SPECIFIC LETHAL 2 HOMOLOG, ZINC ION (3 entities in total)
• 機能のキーワード: gene regulation, dosage compensation, chromatin
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: Q68DK7
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 120744.14

構造登録者

Hallacli, E.,Lipp, M.,Georgiev, P.,Spielman, C.,Cusack, S.,Akhtar, A.,Kadlec, J. (登録日: 2012-08-24, 公開日: 2013-02-06, 最終更新日: 2024-05-08)

主引用文献

Hallacli, E.,Lipp, M.,Georgiev, P.,Spielman, C.,Cusack, S.,Akhtar, A.,Kadlec, J.
Msl1-Mediated Dimerization of the Dosage Compensation Complex is Essential for Male X-Chromosome Regulation in Drosophila.
Mol.Cell, 48:587-, 2012

PubMed Abstract: The Male-Specific Lethal (MSL) complex regulates dosage compensation of the male X chromosome in Drosophila. Here, we report the crystal structure of its MSL1/MSL2 core, where two MSL2 subunits bind to a dimer formed by two molecules of MSL1. Analysis of structure-based mutants revealed that MSL2 can only interact with the MSL1 dimer, but MSL1 dimerization is MSL2 independent. We show that Msl1 is a substrate for Msl2 E3 ubiquitin ligase activity. ChIP experiments revealed that Msl1 dimerization is essential for targeting and spreading of the MSL complex on X-linked genes; however, Msl1 binding to promoters of male and female cells is independent of the dimer status and other MSL proteins. Finally, we show that loss of Msl1 dimerization leads to male-specific lethality. We propose that Msl1-mediated dimerization of the entire MSL complex is required for Msl2 binding, X chromosome recognition, and spreading along the X chromosome.

PubMed: 23084835
DOI: 10.1016/J.MOLCEL.2012.09.014

実験手法

X-RAY DIFFRACTION (3.5 Å)