Spliceosomal protein U1A is involved in alternative splicing and salt stress tolerance in Arabidopsis thaliana
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Office of the VP
KAUST Grant NumberBAS/1/1007-01-01
Permanent link to this recordhttp://hdl.handle.net/10754/626379
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AbstractSoil salinity is a significant threat to sustainable agricultural production worldwide. Plants must adjust their developmental and physiological processes to cope with salt stress. Although the capacity for adaptation ultimately depends on the genome, the exceptional versatility in gene regulation provided by the spliceosome-mediated alternative splicing (AS) is essential in these adaptive processes. However, the functions of the spliceosome in plant stress responses are poorly understood. Here, we report the in-depth characterization of a U1 spliceosomal protein, AtU1A, in controlling AS of pre-mRNAs under salt stress and salt stress tolerance in Arabidopsis thaliana. The atu1a mutant was hypersensitive to salt stress and accumulated more reactive oxygen species (ROS) than the wild-type under salt stress. RNA-seq analysis revealed that AtU1A regulates AS of many genes, presumably through modulating recognition of 5′ splice sites. We showed that AtU1A is associated with the pre-mRNA of the ROS detoxification-related gene ACO1 and is necessary for the regulation of ACO1 AS. ACO1 is important for salt tolerance because ectopic expression of ACO1 in the atu1a mutant can partially rescue its salt hypersensitive phenotype. Our findings highlight the critical role of AtU1A as a regulator of pre-mRNA processing and salt tolerance in plants.
CitationGu J, Xia Z, Luo Y, Jiang X, Qian B, et al. (2017) Spliceosomal protein U1A is involved in alternative splicing and salt stress tolerance in Arabidopsis thaliana. Nucleic Acids Research. Available: http://dx.doi.org/10.1093/nar/gkx1229.
SponsorsWe acknowledge the ABRC for providing the T-DNA insertion lines. We thank Prof. Marvin Wickens (University of Wisconsin-Madison) for providing the yeast three-hybrid system. National Natural Science Foundation of China [31670250 to Z.W.]; Natural Science Foundation of Hainan Province [20163041 to Z.W.]; Hainan University Startup Fund [KYQD1562 to Z.W.]; YNTC [YNTC-2016YN22 to H.X.]; KAUST Faculty Baseline Funds [#BAS/1/1007-01-01 to L.M.X.]; National Key Technology Support Program [2015BAD01B02 to Y.H.L., X.Y.J.]; National Science Foundation [MCB0950242 to J.H.Z.]. Funding for open access charge: Hainan University Startup Fund [KYQD1562].
PublisherOxford University Press (OUP)
JournalNucleic Acids Research
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