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SUMOylation of the chromodomain factor MRG-1 in C. elegans affects chromatin-regulatory dynamics

Gülkiz Baytek, Alexander Blume, Funda Gerceker Demirel, Selman Bulut, Philipp Mertins, View ORCID ProfileBaris Tursun
doi: https://doi.org/10.1101/2021.02.14.431134
Gülkiz Baytek
1Berlin Institute for Medical Systems Biology, Germany
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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  • For correspondence: Baris.Tursun@mdc-berlin.de Guelkiz.Baytek@mdc-berlin.de
Alexander Blume
1Berlin Institute for Medical Systems Biology, Germany
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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Funda Gerceker Demirel
1Berlin Institute for Medical Systems Biology, Germany
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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Selman Bulut
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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Philipp Mertins
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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Baris Tursun
1Berlin Institute for Medical Systems Biology, Germany
2Max Delbrück Center for Molecular Medicine in the Helmholtz Association, Berlin, Germany
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  • ORCID record for Baris Tursun
  • For correspondence: Baris.Tursun@mdc-berlin.de Guelkiz.Baytek@mdc-berlin.de
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Abstract

Epigenetic mechanisms to control chromatin accessibility and structure is important for gene expression in eukaryotic cells. Chromatin regulation ensures proper development and cell fate specification but is also essential later in life. Modifications of histone proteins as an integral component of chromatin can promote either gene expression or repression, respectively. Proteins containing specific domains such as the chromodomain recognize mono-, di- or tri-methylated lysine residues on histone H3. The chromodomain protein MRG-1 in Caenorhabditis elegans is the ortholog of mammalian MRG15, which belongs to the MORF4 Related Gene (MRG) family in humans. In C. elegans MRG-1 predominantly binds methylated histone H3 lysine residues at position 36 (H3K36me3). MRG-1 is important during germline maturation and for safeguarding the germ cell identity. However, it lacks enzymatic activity and depends on protein-protein interaction to cooperate with other factors to regulate chromatin. To elucidate the variety of MRG-1 interaction partners we performed in-depth protein-protein interaction analysis using immunoprecipitations coupled with mass-spectrometry. Besides previously described and novel interactions with other proteins, we also detected a strong association with the Small Ubiquitin-like Modifier (SUMO). Since SUMO is known to be attached to proteins in order to modulate the target proteins activity we assessed whether MRG-1 is post-translationally modified by SUMOylation. Notably, we provide evidence that MRG-1 is indeed SUMOylated and that this post-translational modification influences the chromatin-binding profile of MRG-1 in the C. elegans genome. Our presented study hints towards an important role of SUMOylation in the context of epigenetic regulation via the chromodomain protein MRG-1, which may be a conserved phenomenon also in mammalian species.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted February 14, 2021.
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SUMOylation of the chromodomain factor MRG-1 in C. elegans affects chromatin-regulatory dynamics
Gülkiz Baytek, Alexander Blume, Funda Gerceker Demirel, Selman Bulut, Philipp Mertins, Baris Tursun
bioRxiv 2021.02.14.431134; doi: https://doi.org/10.1101/2021.02.14.431134
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SUMOylation of the chromodomain factor MRG-1 in C. elegans affects chromatin-regulatory dynamics
Gülkiz Baytek, Alexander Blume, Funda Gerceker Demirel, Selman Bulut, Philipp Mertins, Baris Tursun
bioRxiv 2021.02.14.431134; doi: https://doi.org/10.1101/2021.02.14.431134

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