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The HP1 protein interactome of mouse embryonic stem cells

ABSTRACT: The family of Heterochromatin Protein 1 (HP1) consists of highly conserved proteins, which have important functions in the nucleus of eukaryotic cells. In mammals there are three HP1 paralogs: HP1(alpha), Hp1(beta), and Hp1(gamma)They are encoded by the Cbx5, Cbx1, and Cbx3 genes, respectively. Hp1 and Hp1 stably interact with Chd4 and Adnp to form the ChAHP complex. In this project, Chd4, Adnp, and the three Cbx genes were endogenously tagged with a FLAG-Avi tag in mouse embryonic stem cells. The tagged proteins were subjected to tandem-affinity purification and analysis by mass spectrometry.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Embryonic Stem Cell

SUBMITTER: Vytautas Iesmantavicius

LAB HEAD: Marc Bühler

PROVIDER: PXD006226 | Pride | 2018-05-22

REPOSITORIES: Pride

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Publications

Activity-dependent neuroprotective protein recruits HP1 and CHD4 to control lineage-specifying genes.

Ostapcuk Veronika V Mohn Fabio F Carl Sarah H SH Basters Anja A Hess Daniel D Iesmantavicius Vytautas V Lampersberger Lisa L Flemr Matyas M Pandey Aparna A Thomä Nicolas H NH Betschinger Joerg J Bühler Marc M

Nature 20180523 7707

De novo mutations in ADNP, which encodes activity-dependent neuroprotective protein (ADNP), have recently been found to underlie Helsmoortel-Van der Aa syndrome, a complex neurological developmental disorder that also affects several other organ functions <sup>1</sup> . ADNP is a putative transcription factor that is essential for embryonic development <sup>2</sup> . However, its precise roles in transcriptional regulation and development are not understood. Here we show that ADNP interacts with ...[more]

PMID: 29795351

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GFI1 tethers the NuRD complex to open and transcriptionally active chromatin in myeloid progenitors

Project description:GFI is a DNA binding transcriptional repressor that regulates myeloid differentiation. Here, we show that GFI1 interacts with the chromodomain helicase CHD4 and other components of the nucleosome remodeling and deacetylase (NuRD) complex. Our data demonstrated that GFI1 and GFI1/CHD4 complexes occupy sites of open chromatin enriched for histone marks associated with active transcription or different sets of genes that are either enriched for IRF1 or SPI-1 consensus binding sites. In addition, our study provided evidence that GFI1 affects the chromatin remodeling activity of the NuRD complex. Overall, our results indicate that GFI1/CHD4 complexes control chromatin openness and histone modifications differentially to regulate target genes, which govern the immune response, nucleosome organization, or metabolic processes.

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Compartmentalization of HP1 proteins in pluripotency acquisition and maintenance

Project description:Embryonic stem cells (ESCs) have a hyperdynamic chromatin structure characterized by fewer discrete foci of heterochromatin protein 1 family of proteins (HP1) compared to somatic cells. During reprogramming of somatic cells, depletion of HP1γ early, reduced, while depletion later, enhanced the generation of induced pluripotent stem cells (iPSCs); concomitant with a change from a centromeric to nucleoplasmic localization. To identify the interactome of HP1γ in different biochemical environment in ESCs, we compared protein complexes of HP1γ at 0.42M salt (Dignam et al, 1983), with micrococcal nuclease (MCN) digestion with 0.3M NaCl, and MCN with 0.5M NaCl. To understand the effectors of the change in localization, we isolated protein complexes containing HP1γ in ESCs and compared the profile to that in partially reprogrammed intermediates called pre-iPSCs. Given the differential distribution of the HP1 family in ESCs, we also compared the protein interactome of HP1γ in ESCs with that of HP1α and HP1β. In addition, we probed histone associations of HP1γ in ESCs further by querying the histone post-translational modifications that were detectable. The HP1 proteins themselves are decorated with multiple PTMs, several of which we have found to be novel. Taken together our results reveal the complex contribution of the HP1 proteins to pluripotency.

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Identification of a novel, tunable interface in the S.pombe HP1 protein, Swi6, that underpins epigenetic inheritance.

Project description:HP1 proteins bind dynamically to H3K9 methylation and are essential for establishing and maintaining transcriptionally silent epigenetic states, known as heterochromatin. HP1 proteins can dimerize, forming a binding interface that interacts with and recruits diverse chromatin-associated factors. HP1 proteins rapidly evolve through sequence changes and gene duplications, but the extent of variation required to achieve functional specialization is unknown. To investigate how changes in amino acid sequence impact epigenetic inheritance, we performed a targeted mutagenesis screen of the dimerization and protein interaction domain of the S.pombe HP1 homolog Swi6. We discovered that substitutions mapping to an auxiliary motif in Swi6 outside the dimerization interface can lead to complete functional divergence. Specifically, we identified point mutations at a single amino acid residue that resulted in either persistent gain or loss of function in epigenetic inheritance without affecting heterochromatin establishment. These substitutions increase Swi6 chromatin occupancy in vivo and alter Swi6-protein interactions that selectively affect H3K9me inheritance. Based on our findings, we propose that relatively minor changes in Swi6 amino acid composition can lead to profound changes in epigenetic inheritance, underscoring the remarkable plasticity associated with HP1 proteins and their ability to evolve new functions.

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CBX3 Regulates Efficient RNA Processing Genome Wide

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Multiple Overlapping Mammalian Chromatin Remodeling Systems Collaborate Genome-wide at Dynamic Chromatin Transitions (ChIP-Seq)

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Defining the interactome of CHD4 in fusion-positive rhabdomyosarcoma

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Proteo-Genomic Characterization and Mapping of Nucleosomes Decoded by Brd and HP1 Proteins

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Mus musculus

Project description:ChAHP (Adnp, Chd4, HP1) mediates sequence-specific recruitment of HP1 independent of H3K9 methylation

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