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M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity.

ABSTRACT: Genome organization is driven by forces affecting transcriptional state, but the relationship between transcription and genome architecture remains unclear. Here, we identified the Drosophila transcription factor Motif 1 Binding Protein (M1BP) in physical association with the gypsy chromatin insulator core complex, including the universal insulator protein CP190. M1BP is required for enhancer-blocking and barrier activities of the gypsy insulator as well as its proper nuclear localization. Genome-wide, M1BP specifically colocalizes with CP190 at Motif 1-containing promoters, which are enriched at topologically associating domain (TAD) borders. M1BP facilitates CP190 chromatin binding at many shared sites and vice versa. Both factors promote Motif 1-dependent gene expression and transcription near TAD borders genome-wide. Finally, loss of M1BP reduces chromatin accessibility and increases both inter- and intra-TAD local genome compaction. Our results reveal physical and functional interaction between CP190 and M1BP to activate transcription at TAD borders and mediate chromatin insulator-dependent genome organization.

SUBMITTER: Bag I

PROVIDER: S-EPMC8263732 | biostudies-literature |

REPOSITORIES: biostudies-literature

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M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity

Project description:Genome organization is driven by forces affecting transcriptional state, but the relationship between transcription and genome architecture remains unclear. Here, we identified the Drosophila transcription factor Motif 1 Binding Protein (M1BP) in physical association with the gypsy chromatin insulator core complex, including the universal insulator protein CP190. M1BP is required for enhancer-blocking and barrier activities of the gypsy insulator as well as its proper nuclear localization. Genome-wide, M1BP specifically colocalizes with CP190 at Motif 1-containing promoters, which are enriched at topologically associating domain (TAD) borders. M1BP facilitates CP190 chromatin binding at many shared sites and vice versa. Both factors promote Motif 1-dependent gene expression and transcription near TAD borders genome-wide. Finally, loss of M1BP reduces chromatin accessibility and increases both inter- and intra-TAD local genome compaction. Our results reveal physical and functional interaction between CP190 and M1BP to activate transcription at TAD borders and mediate chromatin insulator-dependent genome organization.

2021-06-07 | PXD026497 | Pride

M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity

Project description:In order to identify more gypsy insulator interactors, we performed immunoaffinity purification of Drosophila embryonic nuclear extracts using antibodies specific for CP190 and analyzed the eluates using quantitative mass spectrometry.

2021-06-07 | PXD026493 | Pride

M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity (ATAC-seq)

Project description:Genome organization is driven by forces affecting transcriptional state, but the relationship between transcription and genome architecture remains unclear. Here, we identified the Drosophila transcription factor Motif 1 Binding Protein (M1BP) in physical association with the gypsy chromatin insulator core complex, including the universal insulator protein CP190. M1BP is required for enhancer-blocking and barrier activities of the gypsy insulator as well as its proper nuclear localization. Genome-wide, M1BP specifically colocalizes with CP190 at Motif 1-containing promoters, which are enriched at topologically associating domain (TAD) borders. M1BP is required for CP190 chromatin binding at many shared sites, and CP190 also affects M1BP chromatin association. Both factors are required for Motif 1-dependent gene expression and transcription near TAD borders genome-wide. Finally, loss of M1BP alters local genome compaction. Our results reveal physical and functional interaction between CP190 and M1BP to activate transcription at TAD borders and mediate chromatin insulator-dependent genome organization.

2021-04-14 | GSE169105 | GEO

M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity (ATAC-seq)

Project description:M1BP cooperates with CP190 to activate transcription at TAD borders and promote chromatin insulator activity (ATAC-seq)

| PRJNA715215 | ENA

RNAi-independent role for Argonaute2 in CTCF/CP190 chromatin insulator function.

Project description:A major role of the RNAi pathway in Schizosaccharomyces pombe is to nucleate heterochromatin, but it remains unclear whether this mechanism is conserved. To address this question in Drosophila, we performed genome-wide localization of Argonaute2 (AGO2) by chromatin immunoprecipitation (ChIP)-seq in two different embryonic cell lines and found that AGO2 localizes to euchromatin but not heterochromatin. This localization pattern is further supported by immunofluorescence staining of polytene chromosomes and cell lines, and these studies also indicate that a substantial fraction of AGO2 resides in the nucleus. Intriguingly, AGO2 colocalizes extensively with CTCF/CP190 chromatin insulators but not with genomic regions corresponding to endogenous siRNA production. Moreover, AGO2, but not its catalytic activity or Dicer-2, is required for CTCF/CP190-dependent Fab-8 insulator function. AGO2 interacts physically with CTCF and CP190, and depletion of either CTCF or CP190 results in genome-wide loss of AGO2 chromatin association. Finally, mutation of CTCF, CP190, or AGO2 leads to reduction of chromosomal looping interactions, thereby altering gene expression. We propose that RNAi-independent recruitment of AGO2 to chromatin by insulator proteins promotes the definition of transcriptional domains throughout the genome.

| S-EPMC3165934 | biostudies-literature

Two new insulator proteins, Pita and ZIPIC, target CP190 to chromatin.

Project description:Insulators are multiprotein-DNA complexes that regulate the nuclear architecture. The Drosophila CP190 protein is a cofactor for the DNA-binding insulator proteins Su(Hw), CTCF, and BEAF-32. The fact that CP190 has been found at genomic sites devoid of either of the known insulator factors has until now been unexplained. We have identified two DNA-binding zinc-finger proteins, Pita, and a new factor named ZIPIC, that interact with CP190 in vivo and in vitro at specific interaction domains. Genomic binding sites for these proteins are clustered with CP190 as well as with CTCF and BEAF-32. Model binding sites for Pita or ZIPIC demonstrate a partial enhancer-blocking activity and protect gene expression from PRE-mediated silencing. The function of the CTCF-bound MCP insulator sequence requires binding of Pita. These results identify two new insulator proteins and emphasize the unifying function of CP190, which can be recruited by many DNA-binding insulator proteins.

| S-EPMC4317163 | biostudies-literature

The transcription factor M1BP targets CP190 to chromatin to regulate transcription and chromatin insulator activity

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-10-27 | GSE142533 | GEO

The transcription factor M1BP targets CP190 to chromatin to regulate transcription and chromatin insulator activity (RNA-Seq)

Project description:Chromatin insulators are DNA-protein complexes that establish distinct higher order transcriptional domains. In Drosophila, CP190 is the only common factor for all the DNA-binding insulator protein complex. Insulators harbour two properties: they can block communication between an enhancer and a promoter, and also act as a barrier between heterochromatin and euchromatin. In Drosophila, the gypsy insulator complex contains three core components; Su(Hw), CP190 and Mod(mdg4)67.2. In our studies, using mass-spec analysis and of immunopurified complexes from Drosophila embryonic nuclear extracts, we identified the transcription factor Motif 1 Binding Protein (M1BP) associated with CP190 and verified this interaction by coimmunoprecipitation. Furthermore, depletion of M1BP results in loss of both enhancer-blocking and barrier activities, also disrupts the nuclear localization of CP190-marked insulator bodies within the developing fly. ChIP-seq analysis of both factors in Kc167 cultured hemocytes revealed extensive overlap of the two factors, particularly at Motif 1 containing promoters. Depletion of M1BP results in extensive loss of CP190 chromatin association, and depletion of CP190 also greatly affects M1BP chromatin association. Moreover, EU-seq analysis after depletion of either CP190 or M1BP suggests they regulate gene expression in similar fashion. Further analysis using reporter assays verifies that CP190-dependent gene expression changes are dependent on the presence of Motif 1. Our results suggest a novel mechanistic relationship between CP190 and M1BP function with respect to transcriptional regulation and higher order chromatin organization.

2020-10-27 | GSE142532 | GEO

The transcription factor M1BP targets CP190 to chromatin to regulate transcription and chromatin insulator activity (ChIP-Seq)

2020-10-27 | GSE142531 | GEO

EAST Organizes Drosophila Insulator Proteins in the Interchromosomal Nuclear Compartment and Modulates CP190 Binding to Chromatin.

Project description:Recent data suggest that insulators organize chromatin architecture in the nucleus. The best studied Drosophila insulator proteins, dCTCF (a homolog of the vertebrate insulator protein CTCF) and Su(Hw), are DNA-binding zinc finger proteins. Different isoforms of the BTB-containing protein Mod(mdg4) interact with Su(Hw) and dCTCF. The CP190 protein is a cofactor for the dCTCF and Su(Hw) insulators. CP190 is required for the functional activity of insulator proteins and is involved in the aggregation of the insulator proteins into specific structures named nuclear speckles. Here, we have shown that the nuclear distribution of CP190 is dependent on the level of EAST protein, an essential component of the interchromatin compartment. EAST interacts with CP190 and Mod(mdg4)-67.2 proteins in vitro and in vivo. Over-expression of EAST in S2 cells leads to an extrusion of the CP190 from the insulator bodies containing Su(Hw), Mod(mdg4)-67.2, and dCTCF. In consistent with the role of the insulator bodies in assembly of protein complexes, EAST over-expression led to a striking decrease of the CP190 binding with the dCTCF and Su(Hw) dependent insulators and promoters. These results suggest that EAST is involved in the regulation of CP190 nuclear localization.

| S-EPMC4638101 | biostudies-literature

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