Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 26, Issue 11, Pages 1071-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41594-019-0325-8
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Funding
- Wellcome Trust Investigator Award [110061]
- Wellcome Trust 4-year PhD studentship [105310/Z/14/Z]
- Wellcome Trust [105310/Z/14/Z] Funding Source: Wellcome Trust
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Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GIcNAc, catalyzed by O-GIcNAc transferase (OGT), is an abundant posttranslational event essential for proper animal development and is dysregulated in various diseases. Due to the rapid concurrent removal by the single O-GIcNAcase (OGA), precise functional dissection of site-specific O-GIcNAc modification in vivo is currently not possible without affecting the entire O-GIcNAc proteome. Exploiting the fortuitous promiscuity of OGT, we show that S-GIcNAc is a hydrolytically stable and accurate structural mimic of O-GIcNAc that can be encoded in mammalian systems with CRISPR-Cas9 in an otherwise unperturbed O-GIcNAcome. Using this approach, we target an elusive Ser 405 O-GIcNAc site on OGA, showing that this site-specific modification affects OGA stability.
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