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MSL3 encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. De plus, nous expédions MSL3 Anticorps (40) et beaucoup plus de produits pour cette protéine.
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MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me(1).
A multisubunit human histone acetylase complex that contains homologs of the Drosophila MSL proteins MOF, MSL1 (hampin A), MSL2, and MSL3 was described. This complex is responsible for histone H4 lysine-16 acetylation of all cellular chromosomes.
Data show that complete removal of paternally expressed gene 3 (PEG3) resulted in up-regulation of male-specific lethal 1 (Msl1) and male-specific lethal 3 (Msl3).
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.
Analysis of Mid1, Hccs, Arhgap6, and Msl3l1 in X-linked polydactyly (Xpl) and Patchy-fur (Paf) mutant mice
This gene encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. The Drosophila protein plays a critical role in a dosage-compensation pathway, which equalizes X-linked gene expression in males and females. Thus, the human protein is thought to play a similar function in chromatin remodeling and transcriptional regulation, and it has been found as part of a complex that is responsible for histone H4 lysine-16 acetylation. This gene can undergo X inactivation. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 2, 7 and 8.
male-specific lethal 3 homolog (Drosophila)
, male-specific lethal 3-like 1
, Male-specific lethal 3-like 1
, MSL3-like 1
, male-specific lethal 3 homolog
, male-specific lethal-3 protein-like 1
, male-specific lethal-3 homolog 1