2Y0N

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN DOSAGE COMPENSATION FACTORS MSL1 AND MSL3

Summary for 2Y0N

• Entry DOI: 10.2210/pdb2y0n/pdb
• Descriptor: MALE-SPECIFIC LETHAL 3 HOMOLOG, MALE-SPECIFIC LETHAL 1 HOMOLOG (2 entities in total)
• Functional Keywords: transcription, chromatin, x chromosome, msl complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus (Probable): Q8N5Y2; Nucleus: Q6PDM1
• Total number of polymer chains: 8
• Total formula weight: 124190.98

Authors

Kadlec, J.,Hallacli, E.,Lipp, M.,Holz, H.,Sanchez Weatherby, J.,Cusack, S.,Akhtar, A. (deposition date: 2010-12-04, release date: 2011-01-12, Last modification date: 2023-12-20)

Primary citation

Kadlec, J.,Hallacli, E.,Lipp, M.,Holz, H.,Sanchez-Weatherby, J.,Cusack, S.,Akhtar, A.
Structural Basis for Mof and Msl3 Recruitment Into the Dosage Compensation Complex by Msl1.
Nat.Struct.Mol.Biol., 18:142-, 2011

PubMed Abstract: The male-specific lethal (MSL) complex is required for dosage compensation in Drosophila melanogaster, and analogous complexes exist in mammals. We report structures of binary complexes of mammalian MSL3 and the histone acetyltransferase (HAT) MOF with consecutive segments of MSL1. MSL1 interacts with MSL3 as an extended chain forming an extensive hydrophobic interface, whereas the MSL1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of MSL1. This structure provides insights into the catalytic mechanism of MOF and enables us to show analogous interactions of MOF with NSL1. In Drosophila, selective disruption of Msl1 interactions with Msl3 or Mof severely affects Msl1 targeting to the body of dosage-compensated genes and several high-affinity sites, without affecting promoter binding. We propose that Msl1 acts as a scaffold for MSL complex assembly to achieve specific targeting to the X chromosome.

PubMed: 21217699
DOI: 10.1038/NSMB.1960

Experimental method

X-RAY DIFFRACTION (3 Å)