Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation

Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation

We report here chemoenzymatic and fully synthetic methodologies to modify aspartate and glutamate side chains with ADP-ribose at specific sites on peptides. Structural analysis of aspartate and glutamate ADP-ribosylated peptides reveals near-quantitative migration of the side chain linkage from the...

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Veröffentlicht in:Journal of the American Chemical Society 2023-06, Vol.145 (25), p.14000-14009
Hauptverfasser: Tashiro, Kyuto, Wijngaarden, Sven, Mohapatra, Jugal, Rack, Johannes G. M., Ahel, Ivan, Filippov, Dmitri V., Liszczak, Glen
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Sprache:eng
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Adenosine Diphosphate Ribose - chemistry
Adenosine Diphosphate Ribose - metabolism
ADP-Ribosylation
Aspartic Acid - metabolism
Glutamic Acid - metabolism
Histones - metabolism
Peptides - chemistry
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container_end_page 14009
container_issue 25
container_start_page 14000
container_title Journal of the American Chemical Society
container_volume 145
creator Tashiro, Kyuto
Wijngaarden, Sven
Mohapatra, Jugal
Rack, Johannes G. M.
Ahel, Ivan
Filippov, Dmitri V.
Liszczak, Glen
description We report here chemoenzymatic and fully synthetic methodologies to modify aspartate and glutamate side chains with ADP-ribose at specific sites on peptides. Structural analysis of aspartate and glutamate ADP-ribosylated peptides reveals near-quantitative migration of the side chain linkage from the anomeric carbon to the 2″- or 3″-ADP-ribose hydroxyl moieties. We find that this linkage migration pattern is unique to aspartate and glutamate ADP-ribosylation and propose that the observed isomer distribution profile is present in biochemical and cellular environments. After defining distinct stability properties of aspartate and glutamate ADP-ribosylation, we devise methods to install homogenous ADP-ribose chains at specific glutamate sites and assemble glutamate-modified peptides into full-length proteins. By implementing these technologies, we show that histone H2B E2 tri-ADP-ribosylation is able to stimulate the chromatin remodeler ALC1 with similar efficiency to histone serine ADP-ribosylation. Our work reveals fundamental principles of aspartate and glutamate ADP-ribosylation and enables new strategies to interrogate the biochemical consequences of this widespread protein modification.
doi_str_mv 10.1021/jacs.3c03771
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subjects Adenosine Diphosphate Ribose - chemistry
Adenosine Diphosphate Ribose - metabolism
ADP-Ribosylation
Aspartic Acid - metabolism
Glutamic Acid - metabolism
Histones - metabolism
Peptides - chemistry
title Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
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