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Truncation of the TPR domain of OGT alters substrate and glycosite selection

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Abstract

O-GlcNAc transferase (OGT) is an essential enzyme that installs O-linked N-acetylglucosamine (O-GlcNAc) to thousands of protein substrates. OGT and its isoforms select from these substrates through the tetratricopeptide repeat (TPR) domain, yet the impact of truncations to the TPR domain on substrate and glycosite selection is unresolved. Here, we report the effects of iterative truncations to the TPR domain of OGT on substrate and glycosite selection with the model protein GFP-JunB and the surrounding O-GlcNAc proteome in U2OS cells. Iterative truncation of the TPR domain of OGT maintains glycosyltransferase activity but alters subcellular localization of OGT in cells. The glycoproteome and glycosites modified by four OGT TPR isoforms were examined on the whole proteome and a single target protein, GFP-JunB. We found the greatest changes in O-GlcNAc on proteins associated with mRNA splicing processes and that the first four TPRs of the canonical nucleocytoplasmic OGT had the broadest substrate scope. Subsequent glycosite analysis revealed that alteration to the last four TPRs corresponded to the greatest shift in the resulting O-GlcNAc consensus sequence. This dataset provides a foundation to analyze how perturbations to the TPR domain and expression of OGT isoforms affect the glycosylation of substrates, which will be critical for future efforts in protein engineering of OGT, the biology of OGT isoforms, and diseases associated with the TPR domain of OGT.

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Data availability

The MS data were deposited at the ProteomeXchange Consortium [57] via the PRIDE partner repository, and are available with the identifier PXD028141.

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Funding

Support from the National Institutes of Health (U01CA242098-01, C.M. Woo), the Sloan Foundation (C.M. Woo), the Camille and Henry Dreyfus Foundation (C.M. Woo), and Harvard University is gratefully acknowledged.

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  1. Daniel H. Ramirez

    Present address: Department of Plant Biology, Carnegie Institution for Science, Stanford, CA, USA

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  1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, USA

    Daniel H. Ramirez, Bo Yang, Alexandria K. D’Souza, Dacheng Shen & Christina M. Woo

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Contributions

D.H. Ramirez and C.M. Woo conceived the project and designed the experiments. D.H. Ramirez performed the experiments. B. Yang and A.K. D’Souza helped with quantitative MS analyses. D. Shen contributed IsoTag reagents. D.H. Ramirez and C.M. Woo analyzed the data and wrote the paper with input from all authors.

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Correspondence to Christina M. Woo.

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Ramirez, D.H., Yang, B., D’Souza, A.K. et al. Truncation of the TPR domain of OGT alters substrate and glycosite selection. Anal Bioanal Chem 413, 7385–7399 (2021). https://doi.org/10.1007/s00216-021-03731-8

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