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UnknownPseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7.
Not available
S-EPMC3590987 | biostudies-literature
ProteomicsSupplementary Dataset S7. ADP-ribosylated peptides identified in two Af1521 Macro pulldown experiments from HopU1-Flag vs. Col-0 samples by the ‘triggering’ method.
During infection, the plant pathogenic bacterium Pseudomonas syringae translocates type 3 effector proteins into the host cell. The effector protein HopU1 is an ADP-ribosyltransferases that ADP-ribosylates host proteins to subvert plant innate immunity. The aim of this experiment was to compare affi...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-11-17 | PXD068739 | Pride
Hopu1 Lc-msms Arabidopsis thaliana Affinity purification Plant Pseudomonas syringae Adp-ribosylation Plant pathogen Type 3 effector 
ProteomicsAffinity purification of ADP-ribosylated proteins from A. thaliana plants expressing the Pseudomonas syringae type III effector HopU1
ADP-ribosylated proteins were enriched using the engineered Af1521 Macro domain (Nowak et al., https://doi.org/10.1038/s41467-020-18981-w) from transgenic A. thaliana lines expressing the Pseudomonas syringae type III effector HopU1. A non-functional Af1521 G42E mutant of the engineered Macro domain...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-10-22 | PXD056608 | Pride
Arabidopsis thaliana Type iii effector Pseudomonas syringae Plant pathogen Adp-ribosylation 
UnknownStructure function analysis of an ADP-ribosyltransferase type III effector and its RNA-binding target in plant immunity.
Not available
S-EPMC3234823 | biostudies-literature
UnknownNovel bacterial ADP-ribosylating toxins: structure and function.
Not available
S-EPMC5846498 | biostudies-literature
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