Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses
Agrofoglio YC, Iglesias MJ, Perez-Santángelo S, José de Leone M, Köster T, Catalá R, Salinas J, Yanovsky MJ, Staiger D, Mateos JL (2023)
bioRxiv.
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Autor*in
Agrofoglio, Yamila Carla;
Iglesias, María José;
Perez-Santángelo, Soledad;
José de Leone, María;
Köster, TinoUniBi ;
Catalá, Rafael;
Salinas, Julio;
Yanovsky, Marcelo J.;
Staiger, DorotheeUniBi;
Mateos, Julieta L.
Abstract / Bemerkung
**Abstract**
Arabidopsis PROTEIN ARGININE METHYLTRANSFERASE 5 (PRMT5) post-translationally modifies RNA-binding proteins by arginine (R) methylation. The impact of this modification on the regulation of RNA processing is largely unknown. Here we use LSM4, a component of the spliceosome, as a paradigm to study the impact of R-methylation on its function in RNA processing. We identify in vivo targets of LSM4 and show that LSM4 regulates alternative splicing of a suite of them. Furthermore, LSM4 affects mRNA levels of some of the targets, showing for the first time its role in both AS and steady-state abundance. Thelsm4andprmt5mutants show a considerable overlap of genes with altered splicing patterns, suggesting that these might be regulated by PRMT5-dependent LSM4 methylation. Wild-type LSM4 and an unmethylable version complement thelsm4-1growth and circadian rhythms defects, suggesting that methylation is not critical for growth in normal environments. However, LSM4 methylation increases with ABA and is necessary for plants to respond properly to salt stress. In contrast, LSM4 methylation is reduced by bacterial infection, and plants expressing unmethylable LSM4 are more resistant than plants expressing wild-type LSM4. This tolerance correlates with decreased intron retention of immune-response genes upon infection, augmenting the functional isoform. Taken together, this provides the first direct evidence that R methylation adjusts LSM4 function on pre-mRNA splicing in an antagonistic manner in response to biotic and abiotic stress.
Arabidopsis PROTEIN ARGININE METHYLTRANSFERASE 5 (PRMT5) post-translationally modifies RNA-binding proteins by arginine (R) methylation. The impact of this modification on the regulation of RNA processing is largely unknown. Here we use LSM4, a component of the spliceosome, as a paradigm to study the impact of R-methylation on its function in RNA processing. We identify in vivo targets of LSM4 and show that LSM4 regulates alternative splicing of a suite of them. Furthermore, LSM4 affects mRNA levels of some of the targets, showing for the first time its role in both AS and steady-state abundance. Thelsm4andprmt5mutants show a considerable overlap of genes with altered splicing patterns, suggesting that these might be regulated by PRMT5-dependent LSM4 methylation. Wild-type LSM4 and an unmethylable version complement thelsm4-1growth and circadian rhythms defects, suggesting that methylation is not critical for growth in normal environments. However, LSM4 methylation increases with ABA and is necessary for plants to respond properly to salt stress. In contrast, LSM4 methylation is reduced by bacterial infection, and plants expressing unmethylable LSM4 are more resistant than plants expressing wild-type LSM4. This tolerance correlates with decreased intron retention of immune-response genes upon infection, augmenting the functional isoform. Taken together, this provides the first direct evidence that R methylation adjusts LSM4 function on pre-mRNA splicing in an antagonistic manner in response to biotic and abiotic stress.
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Arginine methylation of the LSM4 spliceosome component by PROTEIN ARGININE METHYLTRANSFERASE 5 fine-tunes alternative splicing of a set of stress-related genes to antagonistically control biotic and abiotic responses in Arabidopsis.
Erscheinungsjahr
2023
Zeitschriftentitel
bioRxiv
Page URI
https://pub.uni-bielefeld.de/record/2987856
Zitieren
Agrofoglio YC, Iglesias MJ, Perez-Santángelo S, et al. Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses. bioRxiv. 2023.
Agrofoglio, Y. C., Iglesias, M. J., Perez-Santángelo, S., José de Leone, M., Köster, T., Catalá, R., Salinas, J., et al. (2023). Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses. bioRxiv. https://doi.org/10.1101/2023.12.08.570794
Agrofoglio, Yamila Carla, Iglesias, María José, Perez-Santángelo, Soledad, José de Leone, María, Köster, Tino, Catalá, Rafael, Salinas, Julio, Yanovsky, Marcelo J., Staiger, Dorothee, and Mateos, Julieta L. 2023. “Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses”. bioRxiv.
Agrofoglio, Y. C., Iglesias, M. J., Perez-Santángelo, S., José de Leone, M., Köster, T., Catalá, R., Salinas, J., Yanovsky, M. J., Staiger, D., and Mateos, J. L. (2023). Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses. bioRxiv.
Agrofoglio, Y.C., et al., 2023. Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses. bioRxiv.
Y.C. Agrofoglio, et al., “Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses”, bioRxiv, 2023.
Agrofoglio, Y.C., Iglesias, M.J., Perez-Santángelo, S., José de Leone, M., Köster, T., Catalá, R., Salinas, J., Yanovsky, M.J., Staiger, D., Mateos, J.L.: Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses. bioRxiv. (2023).
Agrofoglio, Yamila Carla, Iglesias, María José, Perez-Santángelo, Soledad, José de Leone, María, Köster, Tino, Catalá, Rafael, Salinas, Julio, Yanovsky, Marcelo J., Staiger, Dorothee, and Mateos, Julieta L. “Antagonistic effects of arginine methylation of LSM4 on alternative splicing during plant stress responses”. bioRxiv (2023).
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Preprint: 10.1101/2023.12.08.570794
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