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ChIP-seq of MOF, MSL and NSL complex members in mouse ES cells and neuronal progenitors

ABSTRACT: We assessed the genome-wide binding of the histone acetylase MOF and members of its two associated complexes, the male-specific lethal and the non-specific lethal complex (MSL, NSL). We generated ChIP-seq profiles for MOF, MSL1, MSL2, KANSL3, and MCRS1 from mouse embryonic stem cells and neuronal progenitor cells. By using two replicates per sample and stringent filtering criteria, we identify five basic groups of genome regions where the proteins show either mutual or exclusive binding. We find that the NSL complex members (KANSL3, MCRS1) target the TSSs of broadly expressed genes with housekeeping functions in both cell types. MOF and particularly the MSL complex target a subset of these NSL-complex-targets, too. In addition, we find several thousand TSS-distal binding sites, particularly in ESCs, where KANSL3, MSL2 and MCRS1 show strong enrichments for annotated ESC enhancers. The vast majority of the binding to these ESC distal regulatory elements is lost in NPCs. Finally, we identify mostly intronic and intergenic regions with predominant MSL2 enrichments without the presence of its known interactors. These binding sites do not overlap with ESC marks of active chromatin (e.g. DNase hypersensitivity sites), but the they increase in number upon differentiation and we detect a strong signature of the (CAGA)n motif. Our study provides the first comprehensive analysis of MOF in the context of its two complexes in the mouse and reveals shared as well as distinct and dynamic functions for gene regulation and pluripotency.

ORGANISM(S): Mus musculus

PROVIDER: GSE51746 | GEO | 2014/06/03

SECONDARY ACCESSION(S): PRJNA224756

REPOSITORIES: GEO

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ChIP-seq of MOF, MSL and NSL complex members in mouse ES cells and neuronal progenitors

Project description:We assessed the genome-wide binding of the histone acetylase MOF and members of its two associated complexes, the male-specific lethal and the non-specific lethal complex (MSL, NSL). We generated ChIP-seq profiles for MOF, MSL1, MSL2, KANSL3, and MCRS1 from mouse embryonic stem cells and neuronal progenitor cells. By using two replicates per sample and stringent filtering criteria, we identify five basic groups of genome regions where the proteins show either mutual or exclusive binding. We find that the NSL complex members (KANSL3, MCRS1) target the TSSs of broadly expressed genes with housekeeping functions in both cell types. MOF and particularly the MSL complex target a subset of these NSL-complex-targets, too. In addition, we find several thousand TSS-distal binding sites, particularly in ESCs, where KANSL3, MSL2 and MCRS1 show strong enrichments for annotated ESC enhancers. The vast majority of the binding to these ESC distal regulatory elements is lost in NPCs. Finally, we identify mostly intronic and intergenic regions with predominant MSL2 enrichments without the presence of its known interactors. These binding sites do not overlap with ESC marks of active chromatin (e.g. DNase hypersensitivity sites), but the they increase in number upon differentiation and we detect a strong signature of the (CAGA)n motif. Our study provides the first comprehensive analysis of MOF in the context of its two complexes in the mouse and reveals shared as well as distinct and dynamic functions for gene regulation and pluripotency. ChIP-seq of MOF and members of its associated complexes (MSL complex: MSL1, MSL2; NSL complex: KANSL3, MCRS1) in male mouse embryonic stem cells and neuronal progenitor cells derived from them.

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MOF-associated complexes have overlapping and unique roles in regulating pluripotency in embryonic stem cells and during differentiation [ChIP-seq]

Project description:The histone acetyltransferase (HAT) Mof is essential for mouse embryonic stem cells (mESC) pluripotency and early development. Mof is the enzymatic subunit of two different HAT complexes, MSL (Male-Specific Lethal) and NSL (Non-specific lethal). The individual contribution of MSL and NSL complexes to transcription regulation in mESCs is not well understood. Our genome-wide analysis of MSL and NSL localization show that i) MSL and NSL bind to specific and common sets of expressed genes, ii) NSL binds at promoters, iii) while MSL binds in gene bodies. Knockdown of Msl1 leads to a global loss of histone H4K16ac indicating that MSL is the main HAT acetylating H4K16 in mESCs. MSL was enriched at many mESC-specific genes, but also at bivalent domains. Thus, NSL and MSL HAT complexes differentially regulate specific sets of expressed genes in mESCs. Furthermore, MSL is essential for the regulation of key mESC-specific and bivalent developmental genes. Genome-wide comparions of Msl1 and Nsl1 binding in mESCs

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MOF-associated complexes have overlapping and unique roles in regulating pluripotency in embryonic stem cells and during differentiation [array]

Project description:The histone acetyltransferase (HAT) Mof is essential for mouse embryonic stem cells (mESC) pluripotency and early development. Mof is the enzymatic subunit of two different HAT complexes, MSL (Male-Specific Lethal) and NSL (Non-specific lethal). The individual contribution of MSL and NSL complexes to transcription regulation in mESCs is not well understood. Our genome-wide analysis of MSL and NSL localization show that i) MSL and NSL bind to specific and common sets of expressed genes, ii) NSL binds at promoters, iii) while MSL binds in gene bodies. Knockdown of Msl1 leads to a global loss of histone H4K16ac indicating that MSL is the main HAT acetylating H4K16 in mESCs. MSL was enriched at many mESC-specific genes, but also at bivalent domains. Thus, NSL and MSL HAT complexes differentially regulate specific sets of expressed genes in mESCs. Furthermore, MSL is essential for the regulation of key mESC-specific and bivalent developmental genes. Gene expression was analysed through microarrays in mESCs infected with shRNA vectors expressing either a non-target control, shRNA against Nsl1 or Msl1 to knockdown Nsl1 or Msl1.

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Kansl2 dependent acetylome study in primary Kansl2 (fl/fl) murine embryonic fibroblasts

Project description:As one of the most important post-translational protein modifications, lysine acetylation is catalyzed by lysine acetyltransferases (KATs), which catalyze the covalent attachment of an acetyl group to the N epsilon–residue of lysine. The histone acetyltransferase MOF, which represents the main histone H4 lysine-16 specific acetyltransferase, is the KAT subunit of two mutually exclusive multiprotein complexes in metazoa, namely the MSL (male-specific lethal) and the NSL (non-specific lethal) complex. Depletion of both, MOF and the NSL complex subunit Kansl2 result in selective changes of the cellular acetylome. As a consequence, modulation of nuclear lamin lysine acetylations correlate with profound changes in nuclear morphology, like micronuclei formation.

2023-01-05 | PXD038521 | Pride

ChIP-Seq of NSL3 and MBD-R2 in Drosophila melanogaster S2 cells to investigate the function of Non-Specific Lethal (NSL) complex

Project description:The major H4K16 acetylase MOF has been found in two complexes, the Male-Specific Lethal (MSL) and the Non-Specific Lethal (NSL) complex. The latter one consists of at least 7 members: NSL1, NSL2, NSL3, MBD-R2, MCRS2, WDS, and MOF. To investigate it's function, we performed genome-wide profiling of NSL3 and MBD-R2 in S2 cells. In addition, we obtained ChIP-Seq profiles for NSL1 and MCRS2 from 3rd instar larvae salivary glands that can be accessed via the accession number E-MTAB-214. This submission is also related to E-MTAB-1084.

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