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PICLN modulates alternative splicing and light/temperature responses in plants
Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina; Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE-UBA-CONICET), Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, Argentina; RNA Biology and Molecular Physiology, Faculty of Biology, Bielefeld University, Bielefeld, Germany.
Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina.
Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Buenos Aires, Argentina; Department of Molecular Biology, Max Planck Institute for Biology Tübingen, Tübingen, Germany.
Instituto de Biología Molecular y Celular de Plantas, CSIC-Universidad Politecnica de Valencia, Valencia, Spain.
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2023 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 191, no 2, p. 1036-1051Article in journal (Refereed) Published
Abstract [en]

Plants undergo transcriptome reprograming to adapt to daily and seasonal fluctuations in light and temperature conditions. While most efforts have focused on the role of master transcription factors, the importance of splicing factors modulating these processes is now emerging. Efficient pre-mRNA splicing depends on proper spliceosome assembly, which in plants and animals requires the methylosome complex. Ion Chloride nucleotide-sensitive protein (PICLN) is part of the methylosome complex in both humans and Arabidopsis (Arabidopsis thaliana), and we show here that the human PICLN ortholog rescues phenotypes of Arabidopsis picln mutants. Altered photomorphogenic and photoperiodic responses in Arabidopsis picln mutants are associated with changes in pre-mRNA splicing that partially overlap with those in PROTEIN ARGININE METHYL TRANSFERASE5 (prmt5) mutants. Mammalian PICLN also acts in concert with the Survival Motor Neuron (SMN) complex component GEMIN2 to modulate the late steps of UsnRNP assembly, and many alternative splicing events regulated by PICLN but not PRMT5, the main protein of the methylosome, are controlled by Arabidopsis GEMIN2. As with GEMIN2 and SM PROTEIN E1/PORCUPINE (SME1/PCP), low temperature, which increases PICLN expression, aggravates morphological and molecular defects of picln mutants. Taken together, these results establish a key role for PICLN in the regulation of pre-mRNA splicing and in mediating plant adaptation to daily and seasonal fluctuations in environmental conditions.

Place, publisher, year, edition, pages
Oxford University Press, 2023. Vol. 191, no 2, p. 1036-1051
National Category
Botany
Identifiers
URN: urn:nbn:se:umu:diva-205183DOI: 10.1093/plphys/kiac527ISI: 000911677600001PubMedID: 36423226Scopus ID: 2-s2.0-85148076794OAI: oai:DiVA.org:umu-205183DiVA, id: diva2:1739927
Funder
Knut and Alice Wallenberg Foundation, 2018.0202EU, Horizon 2020, SIGNAT-644435Available from: 2023-02-28 Created: 2023-02-28 Last updated: 2023-02-28Bibliographically approved

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Goretti, DanielaSchmid, Markus

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