Proteomics

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Quantitative O-GlcNAc analysis between wild type and sec-5 using SILIA (F1 on QE-HF) and Eclipse (HCD)

ABSTRACT: O-GlcNAcylation is a crucial post-translational modification of proteins observed in both plants and animals and plays a key role in growth and development. Plants have close OGT homologs, SECRET AGENT (SEC) and SPINDLY (SPY). In vitro, SEC has shown O-GlcNAc activity. Recently, a surprising discovery in wheat revealed an atypical TaOGT(TaOGT1) with no structural similarity to SEC and SPY enzyme (Fan et al. 2021). TaOGT1 was found to O-GlcNAcylate TaGRP2. In Arabidopsis, approximately 34 unannotated or uncharacterized proteins share similarity with TaOGT1, leading to questions about whether SEC is the primary contributor to O-GlcNAcylation in plants. Here we use LWAC enrichment and SILIA labeling, quantifying at both MS1. Our findings reveal a significant reduction in O-GlcNAc levels in the sec mutant, indicating SEC’s critical role in mediating O-GlcNAcylation.

INSTRUMENT(S): Orbitrap Eclipse, Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Shoot

SUBMITTER: Shouling Xu  

LAB HEAD: shouling xu

PROVIDER: PXD044668 | Pride | 2024-05-21

REPOSITORIES: Pride

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Dataset's files

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Action DRS
E20210820_01.raw Raw
E20210820_01f.pep.xml Pepxml
E20210820_02.raw Raw
E20210820_02f.pep.xml Pepxml
E20210820_03.raw Raw
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Publications

SECRET AGENT O-GlcNAcylates Hundreds of Proteins Involved in Diverse Cellular Processes in Arabidopsis.

Shrestha Ruben R   Karunadasa Sumudu S   Grismer TaraBryn S TS   Reyes Andres V AV   Xu Shou-Ling SL  

Molecular & cellular proteomics : MCP 20240208 4

O-GlcNAcylation is a critical post-translational modification of proteins observed in both plants and animals and plays a key role in growth and development. While considerable knowledge exists about over 3000 substrates in animals, our understanding of this modification in plants remains limited. Unlike animals, plants possess two putative homologs: SECRET AGENT (SEC) and SPINDLY, with SPINDLY also exhibiting O-fucosylation activity. To investigate the role of SEC as a major O-GlcNAc transferas  ...[more]

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