RNA Binding Proteins RZ-1B and RZ-1C Play Critical Roles in Regulating Pre-mRNA Splicing and Gene Expression during Development in Arabidopsis. Issue 1 (31st December 2015)
- Record Type:
- Journal Article
- Title:
- RNA Binding Proteins RZ-1B and RZ-1C Play Critical Roles in Regulating Pre-mRNA Splicing and Gene Expression during Development in Arabidopsis. Issue 1 (31st December 2015)
- Main Title:
- RNA Binding Proteins RZ-1B and RZ-1C Play Critical Roles in Regulating Pre-mRNA Splicing and Gene Expression during Development in Arabidopsis
- Authors:
- Wu, Zhe
Zhu, Danling
Lin, Xiaoya
Miao, Jin
Gu, Lianfeng
Deng, Xian
Yang, Qian
Sun, Kangtai
Zhu, Danmeng
Cao, Xiaofeng
Tsuge, Tomohiko
Dean, Caroline
Aoyama, Takashi
Gu, Hongya
Qu, Li-Jia - Abstract:
- Abstract : Plant-specific RNA binding proteins RZ-1B and RZ-1C interact with a number of highly conserved serine/arginine-rich proteins to regulate RNA splicing and gene expression in Arabidopsis. Abstract: Nuclear-localized RNA binding proteins are involved in various aspects of RNA metabolism, which in turn modulates gene expression. However, the functions of nuclear-localized RNA binding proteins in plants are poorly understood. Here, we report the functions of two proteins containing RNA recognition motifs, RZ-1B and RZ-1C, in Arabidopsis thaliana . RZ-1B and RZ-1C were localized to nuclear speckles and interacted with a spectrum of serine/arginine-rich (SR) proteins through their C termini. RZ-1C preferentially bound to purine-rich RNA sequences in vitro through its N-terminal RNA recognition motif. Disrupting the RNA binding activity of RZ-1C with SR proteins through overexpression of the C terminus of RZ-1C conferred defective phenotypes similar to those observed in rz-1b rz-1c double mutants, including delayed seed germination, reduced stature, and serrated leaves. Loss of function of RZ-1B and RZ-1C was accompanied by defective splicing of many genes and global perturbation of gene expression. In addition, we found that RZ-1C directly targeted FLOWERING LOCUS C ( FLC ), promoting efficient splicing of FLC introns and likely also repressing FLC transcription. Our findings highlight the critical role of RZ-1B/1C in regulating RNA splicing, gene expression, and manyAbstract : Plant-specific RNA binding proteins RZ-1B and RZ-1C interact with a number of highly conserved serine/arginine-rich proteins to regulate RNA splicing and gene expression in Arabidopsis. Abstract: Nuclear-localized RNA binding proteins are involved in various aspects of RNA metabolism, which in turn modulates gene expression. However, the functions of nuclear-localized RNA binding proteins in plants are poorly understood. Here, we report the functions of two proteins containing RNA recognition motifs, RZ-1B and RZ-1C, in Arabidopsis thaliana . RZ-1B and RZ-1C were localized to nuclear speckles and interacted with a spectrum of serine/arginine-rich (SR) proteins through their C termini. RZ-1C preferentially bound to purine-rich RNA sequences in vitro through its N-terminal RNA recognition motif. Disrupting the RNA binding activity of RZ-1C with SR proteins through overexpression of the C terminus of RZ-1C conferred defective phenotypes similar to those observed in rz-1b rz-1c double mutants, including delayed seed germination, reduced stature, and serrated leaves. Loss of function of RZ-1B and RZ-1C was accompanied by defective splicing of many genes and global perturbation of gene expression. In addition, we found that RZ-1C directly targeted FLOWERING LOCUS C ( FLC ), promoting efficient splicing of FLC introns and likely also repressing FLC transcription. Our findings highlight the critical role of RZ-1B/1C in regulating RNA splicing, gene expression, and many key aspects of plant development via interaction with proteins including SR proteins. … (more)
- Is Part Of:
- The Plant Cell. Volume 28:Issue 1(2016)
- Journal:
- The Plant Cell
- Issue:
- Volume 28:Issue 1(2016)
- Issue Display:
- Volume 28, Issue 1 (2016)
- Year:
- 2016
- Volume:
- 28
- Issue:
- 1
- Issue Sort Value:
- 2016-0028-0001-0000
- Page Start:
- 55
- Page End:
- 73
- Publication Date:
- 2015-12-31
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00949 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16359.xml