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O-GlcNAcylation Prevents Aggregation of the Polycomb Group Repressor Polyhomeotic

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Gambetta,  Maria Cristina
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Müller,  Jürg
Müller, Jürg / Chromatin Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Gambetta, M. C., & Müller, J. (2014). O-GlcNAcylation Prevents Aggregation of the Polycomb Group Repressor Polyhomeotic. DEVELOPMENTAL CELL, 31(5), 629-639. doi:10.1016/j.devcel.2014.10.020.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-9098-1
Abstract
The glycosyltransferase Ogt adds O-linked N-Acetylglucosamine (O-GlcNAc) moieties to nuclear and cytosolic proteins. Drosophila embryos lacking Ogt protein arrest development with a remarkably specific Polycomb phenotype, arising from the failure to repress Polycomb target genes. The Polycomb protein Polyhomeotic (Ph), an Ogt substrate, forms large aggregates in the absence of O-GlcNAcylation both in vivo and in vitro. O-GlcNAcylation of a serine/threonine (SIT) stretch in Ph is critical to prevent nonproductive aggregation of both Drosophila and human Ph via their C-terminal sterile alpha motif (SAM) domains in vitro. Full Ph repressor activity in vivo requires both the SAM domain and O-GlcNAcylation of the SIT stretch. We demonstrate that Ph mutants lacking the SIT stretch reproduce the phenotype of ogt mutants, suggesting that the S/T stretch in Ph is the key Ogt substrate in Drosophila. We propose that O-GlcNAcylation is needed for Ph to form functional, ordered assemblies via its SAM domain.