Year: 2023
Type: article
Abstract: Sulfation widely exists in the eukaryotic proteome. However, understanding the biological functions of sulfation in peptides and proteins has been hampered by the lack of methods to control its spatial or temporal distribution in the proteome. Herein, we report that fluorosulfate can serve as a latent precursor of sulfate in peptides and proteins, which can be efficiently converted to sulfate by hydroxamic acid reagents under physiologically relevant conditions. Photocaging the hydroxamic acid reagents further allowed for the light-controlled activation of functional sulfopeptides. This work provides a valuable tool for probing the functional roles of sulfation in peptides and proteins.
DOI: 10.1021/jacs.3c07937
Institutions: Boston College, Boston University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: CryoProbe-enabled Bruker AVANCE NEO 500 MHz NMR Spectrometer, G1726345278, G282645812, G5217627585, Development of Compact CRISPR Editors for Multiplexed Editing of Complex Gene Networks, G6884064952, MRI: Acquisition of a CryoProbe-Enabled NMR Spectrometer for Enhanced Efficiency and Sensitivity in Chemical and Biological Research, G8869753781, A genetically encoded toolset to decipher the biology of post-translational modifications in the mammalian proteome
OpenAlex ID: W4386272374
