Genome-Scale Identification of Wild Soybean Serine/Arginine-Rich Protein Family Genes and Their Responses to Abiotic Stresses
文献类型： 外文期刊
作者： Wang, Yanping 1 ; Wang, Xiaomei 1 ; Zhang, Rui 2 ; Chen, Tong 2 ; Xiao, Jialei 2 ; Li, Qiang 2 ; Ding, Xiaodong 2 ; Sun, Xiaohuan 1 ;
作者机构： 1.Heilongjiang Acad Agr Sci, Mudanjiang Branch, Mudanjiang 157000, Peoples R China
2.Northeast Agr Univ, Coll Life Sci, Key Lab Agr Biol Funct Genes, Harbin 150030, Peoples R China
关键词： wild soybean; SR protein; alternative splicing; abiotic stress
期刊名称：INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES （ 影响因子：4.9； 五年影响因子：5.7 ）
ISSN： 1661-6596
年卷期： 2024 年 25 卷 20 期
页码：
收录情况： SCI
摘要： Serine/arginine-rich (SR) proteins mostly function as splicing factors for pre-mRNA splicing in spliceosomes and play critical roles in plant development and adaptation to environments. However, detailed study about SR proteins in legume plants is still lacking. In this report, we performed a genome-wide investigation of SR protein genes in wild soybean (Glycine soja) and identified a total of 31 GsSR genes from the wild soybean genome. The analyses of chromosome location and synteny show that the GsSRs are unevenly distributed on 15 chromosomes and are mainly under the purifying selection. The GsSR proteins can be phylogenetically classified into six sub-families and are conserved in evolution. Prediction of protein phosphorylation sites indicates that GsSR proteins are highly phosphorylated proteins. The protein-protein interaction network implies that there exist numerous interactions between GsSR proteins. We experimentally confirmed their physical interactions with the representative SR proteins of spliceosome-associated components such as U1-70K or U2AF35 by yeast two-hybrid assays. In addition, we identified various stress-/hormone-responsive cis-acting elements in the promoter regions of these GsSR genes and verified their expression patterns by RT-qPCR analyses. The results show most GsSR genes are highly expressed in root and stem tissues and are responsive to salt and alkali stresses. Splicing analysis showed that the splicing patterns of GsSRs were in a tissue- and stress-dependent manner. Overall, these results will help us to further investigate the biological functions of leguminous plant SR proteins and shed new light on uncovering the regulatory mechanisms of plant SR proteins in growth, development, and stress responses.
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