Dual roles of the serine/arginine-rich splicing factor SR45a in promoting and interacting with nuclear cap-binding complex to modulate the salt-stress response in Arabidopsis

© 2021 The Authors. New Phytologist © 2021 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 230(2021), 2 vom: 15. Apr., Seite 641-655
1. Verfasser: Li, Ying (VerfasserIn)
Weitere Verfasser: Guo, Qianhuan, Liu, Peng, Huang, Jinguang, Zhang, Shizhong, Yang, Guodong, Wu, Changai, Zheng, Chengchao, Yan, Kang
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't CBP20 SR45a alternative splicing cap-binding complex post-transcriptional regulation salt stress serine/arginine-rich protein Arabidopsis Proteins mehr... RNA Splicing Factors RNA-Binding Proteins SR45a protein, Arabidopsis Serine 452VLY9402 Arginine 94ZLA3W45F
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245 1 0 |a Dual roles of the serine/arginine-rich splicing factor SR45a in promoting and interacting with nuclear cap-binding complex to modulate the salt-stress response in Arabidopsis 
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520 |a Alternative splicing (AS) is emerging as a critical co-transcriptional regulation for plants in response to environmental stresses. Although multiple splicing factors have been linked to the salt-sensitive signaling network, the molecular mechanism remains unclear. We discovered that a conserved serine/arginine-rich (SR)-like protein, SR45a, as a component of the spliceosome, was involved in post-transcriptional regulation of salinity tolerance in Arabidopsis thaliana. Furthermore, SR45a was required for the AS and messenger RNA (mRNA) maturation of several salt-tolerance genes. Two alternatively spliced variants of SR45a were induced by salt stress, full-length SR45a-1a and the truncated isoform SR45a-1b, respectively. Lines with overexpression of SR45a-1a and SR45a-1b exhibited hypersensitive to salt stress. Our data indicated that SR45a directly interacted with the cap-binding complex (CBC) subunit cap-binding protein 20 (CBP20) which mediated salt-stress responses. Instead of binding to other spliceosome components, SR45a-1b promoted the association of SR45a-1a with CBP20, therefore mediating salt-stress signal transduction pathways. Additionally, the mutations in SR45a and CBP20 led to different salt-stress phenotypes. Together, these results provide the evidence that SR45a-CBP20 acts as a regulatory complex to regulate the plant response to salt stress, through a regulatory mechanism to fine-tune the splicing factors, especially in stressful conditions 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a CBP20 
650 4 |a SR45a 
650 4 |a alternative splicing 
650 4 |a cap-binding complex 
650 4 |a post-transcriptional regulation 
650 4 |a salt stress 
650 4 |a serine/arginine-rich protein 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a RNA Splicing Factors  |2 NLM 
650 7 |a RNA-Binding Proteins  |2 NLM 
650 7 |a SR45a protein, Arabidopsis  |2 NLM 
650 7 |a Serine  |2 NLM 
650 7 |a 452VLY9402  |2 NLM 
650 7 |a Arginine  |2 NLM 
650 7 |a 94ZLA3W45F  |2 NLM 
700 1 |a Guo, Qianhuan  |e verfasserin  |4 aut 
700 1 |a Liu, Peng  |e verfasserin  |4 aut 
700 1 |a Huang, Jinguang  |e verfasserin  |4 aut 
700 1 |a Zhang, Shizhong  |e verfasserin  |4 aut 
700 1 |a Yang, Guodong  |e verfasserin  |4 aut 
700 1 |a Wu, Changai  |e verfasserin  |4 aut 
700 1 |a Zheng, Chengchao  |e verfasserin  |4 aut 
700 1 |a Yan, Kang  |e verfasserin  |4 aut 
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773 1 8 |g volume:230  |g year:2021  |g number:2  |g day:15  |g month:04  |g pages:641-655 
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