This entry represents the N-terminal domain of the E3 ubiquitin-protein ligase Msl2. This domain binds Msl1 and exhibits ubiquitin E3 ligase activity towards H2B K34 [].
This entry represents the short coiled dimerisation domain of higher eukaryotic MSL1, part of the MSL or Male-Specific Lethal complex. This complex regulates the dosage compensation of the male X chromosome in Drosophila and other eukaryotes. The structure of the MSL1/MSL2 core shows that two MSL2 subunits bind to a dimer formed by two molecules of MSL1. MSL1 is a substrate for MSL2 E3 ubiquitin ligase activity [].
This domain was first identified in drosophila MSL1 (male-specific lethal 1) []. In drosophila it binds to the histone acetyltransferase males-absent on the first protein (MOF) and to protein male-specific lethal-3 (MSL3) [, ]. This domain can also be found in KAT8 regulatory NSL complex subunit 1 (KANSL1 or NSL1), which is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription [].
Male-specific lethal 3 homolog (MSL3) is a component of the MSL complex []. MSL3 has a chromodomain by which it interacts with DNA [, ]and an MRG domain with which it interacts with MSL1 [].The male-specific lethal (MSL) complex is a histone acetyltransferase with specificity for histone H4 'lysine-16' in chromatin. The complex consists of MOF, MSL1, MSL2, and MSL3 []. The complex was first identified in Drosophila.
