Proteomics

Dataset Information

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PARylation of UBC13 and PDI proteins


ABSTRACT: NH2OH was used to remove PAR from the PARylated proteins. This treatment left on the PARylated residues a hydroxamic acid derivative, which has a signature mass increase of +15.0109 Da and could be distinguished by mass spectrometry.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702)

SUBMITTER: Junqi Song  

PROVIDER: MSV000087876 | MassIVE | Fri Jul 23 13:37:00 BST 2021

REPOSITORIES: MassIVE

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Publications

Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.

Yao Dongsheng D   Arguez Marcus A MA   He Ping P   Bent Andrew F AF   Song Junqi J  

Molecular plant 20210818 12


Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification reversibly catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs) and plays a key role in multiple cellular processes. The molecular mechanisms by which PARylation regulates innate immunity remain largely unknown in eukaryotes. Here we show that Arabidopsis UBC13A and UBC13B, the major drivers of lysine 63 (K63)-linked polyubiquitination, directly interact with PARPs/PARGs. Activation  ...[more]

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