Formation of HopQ1:14-3-3 complex in the host cytoplasm modulates nuclear import rate of Pseudomonas syringae effector in Nicotiana benthamiana cells.

Autor: Rymaszewski W; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Giska F; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Piechocki MA; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Zembek PB; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland., Krzymowska M; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Jazyk: angličtina
Zdroj: Frontiers in plant science [Front Plant Sci] 2024 Mar 04; Vol. 15, pp. 1335830. Date of Electronic Publication: 2024 Mar 04 (Print Publication: 2024).
DOI: 10.3389/fpls.2024.1335830
Abstrakt: HopQ1, a type three effector from Pseudomonas syringae upon phosphorylation coopts plant 14-3-3 proteins to control its stability and subcellular localization. Mass spectrometry of the cytoplasm-restricted effector revealed that HopQ1 already in this subcellular compartment undergoes phosphorylation at serine 51 within the canonical 14-3-3 binding motif and within the second putative 14-3-3 binding site, 24 RTPSES 29 . Our analyses revealed that the stoichiometry of the HopQ1:14-3-3a complex is 1:2 indicating that both binding sites of HopQ1 are involved in the interaction. Notably, 24 RTPSES 29 comprises a putative nuclear translocation signal (NTS). Although a peptide containing NTS mediates nuclear import of a Cargo protein suggesting its role in the nuclear trafficking of HopQ1, a deletion of 25 TPS 27 does not change HopQ1 distribution. In contrast, elimination of 14-3-3 binding site, accelerates nuclear trafficking the effector. Collectively, we show that formation of the HopQ1:14-3-3 complex occurs in the host cytoplasm and slows down the effector translocation into the nucleus. These results provide a mechanism that maintains the proper nucleocytoplasmic partitioning of HopQ1, and at the same time is responsible for the relocation of 14-3-3s from the nucleus to cytoplasm in the presence of the effector.
Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
(Copyright © 2024 Rymaszewski, Giska, Piechocki, Zembek and Krzymowska.)
Databáze: MEDLINE
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