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PICLN modulates alternative splicing and light/temperature responses in plants

Authors :
Julieta L Mateos
Sabrina E Sanchez
Martina Legris
David Esteve-Bruna
Jeanette C Torchio
Ezequiel Petrillo
Daniela Goretti
Noel Blanco-Touriñán
Danelle K Seymour
Markus Schmid
Detlef Weigel
David Alabadí
Marcelo J Yanovsky
Source :
Plant physiology.
Publication Year :
2022

Abstract

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.

Subjects

Subjects :
Physiology
Genetics
Plant Science

Details

ISSN :
15322548
Database :
OpenAIRE
Journal :
Plant physiology
Accession number :
edsair.doi.dedup.....e3a2e4ac506a4765dec1b0c5132795e3