Authors
Jui-Yun Rei Liao, Giulia Friso, Evan S Forsythe, Elena JS Michel, Alissa M Williams, Sasha S Boguraev, Lalit Ponnala, Daniel B Sloan, Klaas J van Wijk
Publication date
2022/3/1
Journal
Journal of Biological Chemistry
Volume
298
Issue
3
Publisher
Elsevier
Description
The chloroplast chaperone CLPC1 unfolds and delivers substrates to the stromal CLPPRT protease complex for degradation. We previously used an in vivo trapping approach to identify interactors with CLPC1 in Arabidopsis thaliana by expressing a STREPII-tagged copy of CLPC1 mutated in its Walker B domains (CLPC1-TRAP) followed by affinity purification and mass spectrometry. To create a larger pool of candidate substrates, adaptors, or regulators, we carried out a far more sensitive and comprehensive in vivo protein trapping analysis. We identified 59 highly enriched CLPC1 protein interactors, in particular proteins belonging to families of unknown functions (DUF760, DUF179, DUF3143, UVR-DUF151, HugZ/DUF2470), as well as the UVR domain proteins EXE1 and EXE2 implicated in singlet oxygen damage and signaling. Phylogenetic and functional domain analyses identified other members of these …
Total citations
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