Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat
The heterotrimeric G-protein mediates growth and development by perceiving and transmitting signals in multiple organisms. Alternative splicing (AS), a vital process for regulating gene expression at the post-transcriptional level, plays a significant role in plant adaptation and evolution. Here, we...
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2021
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oai:doaj.org-article:a6d7be55fa5448728a7d993e79bcfa2b2021-11-11T17:09:36ZAlternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat10.3390/ijms2221116921422-00671661-6596https://doaj.org/article/a6d7be55fa5448728a7d993e79bcfa2b2021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11692https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The heterotrimeric G-protein mediates growth and development by perceiving and transmitting signals in multiple organisms. Alternative splicing (AS), a vital process for regulating gene expression at the post-transcriptional level, plays a significant role in plant adaptation and evolution. Here, we identified five splicing variants of G<sub>γ</sub> subunit gene <i>TaGS3</i> (<i>TaGS3.1</i> to <i>TaGS3.5</i>), which showed expression divergence during wheat polyploidization, and differential function in grain weight and size determination. <i>TaGS3.1</i> overexpression significantly reduced grain weight by 5.89% and grain length by 5.04%, while <i>TaGS3.2</i>–<i>3.4</i> overexpression did not significantly alter grain size compared to wild type. Overexpressing <i>TaGS3.5</i> significantly increased the grain weight by 5.70% and grain length by 4.30%. Biochemical assays revealed that <i>TaGS3</i> isoforms (TaGS3.1–3.4) with an intact OSR domain interact with WGB1 to form active G<sub>βγ</sub> heterodimers that further interact with WGA1 to form inactive G<sub>αβγ</sub> heterotrimers. Truncated isoforms <i>TaGS3.2–3.4</i> , which lack the C-terminal Cys-rich region but have enhanced binding affinity to WGB1, antagonistically compete with <i>TaGS3.1</i> to bind WGB1, while <i>TaGS3.5</i> with an incomplete OSR domain does not interact with WGB1. Taking these observations together, we proposed that <i>TaGS3</i> differentially regulates grain size via AS, providing a strategy by which the grain size is fine-tuned and regulated at the post-transcriptional level.Xiaoli RenLiya ZhiLei LiuDeyuan MengQiannan SuAamana BatoolJun JiLiqiang SongNa ZhangLin GuoXigang LiuJunming LiWei ZhangMDPI AGarticlebread wheat<i>TaGS3</i>alternative splicinggrain weightgrain sizeBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11692, p 11692 (2021) |
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bread wheat <i>TaGS3</i> alternative splicing grain weight grain size Biology (General) QH301-705.5 Chemistry QD1-999 |
| spellingShingle |
bread wheat <i>TaGS3</i> alternative splicing grain weight grain size Biology (General) QH301-705.5 Chemistry QD1-999 Xiaoli Ren Liya Zhi Lei Liu Deyuan Meng Qiannan Su Aamana Batool Jun Ji Liqiang Song Na Zhang Lin Guo Xigang Liu Junming Li Wei Zhang Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| description |
The heterotrimeric G-protein mediates growth and development by perceiving and transmitting signals in multiple organisms. Alternative splicing (AS), a vital process for regulating gene expression at the post-transcriptional level, plays a significant role in plant adaptation and evolution. Here, we identified five splicing variants of G<sub>γ</sub> subunit gene <i>TaGS3</i> (<i>TaGS3.1</i> to <i>TaGS3.5</i>), which showed expression divergence during wheat polyploidization, and differential function in grain weight and size determination. <i>TaGS3.1</i> overexpression significantly reduced grain weight by 5.89% and grain length by 5.04%, while <i>TaGS3.2</i>–<i>3.4</i> overexpression did not significantly alter grain size compared to wild type. Overexpressing <i>TaGS3.5</i> significantly increased the grain weight by 5.70% and grain length by 4.30%. Biochemical assays revealed that <i>TaGS3</i> isoforms (TaGS3.1–3.4) with an intact OSR domain interact with WGB1 to form active G<sub>βγ</sub> heterodimers that further interact with WGA1 to form inactive G<sub>αβγ</sub> heterotrimers. Truncated isoforms <i>TaGS3.2–3.4</i> , which lack the C-terminal Cys-rich region but have enhanced binding affinity to WGB1, antagonistically compete with <i>TaGS3.1</i> to bind WGB1, while <i>TaGS3.5</i> with an incomplete OSR domain does not interact with WGB1. Taking these observations together, we proposed that <i>TaGS3</i> differentially regulates grain size via AS, providing a strategy by which the grain size is fine-tuned and regulated at the post-transcriptional level. |
| format |
article |
| author |
Xiaoli Ren Liya Zhi Lei Liu Deyuan Meng Qiannan Su Aamana Batool Jun Ji Liqiang Song Na Zhang Lin Guo Xigang Liu Junming Li Wei Zhang |
| author_facet |
Xiaoli Ren Liya Zhi Lei Liu Deyuan Meng Qiannan Su Aamana Batool Jun Ji Liqiang Song Na Zhang Lin Guo Xigang Liu Junming Li Wei Zhang |
| author_sort |
Xiaoli Ren |
| title |
Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| title_short |
Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| title_full |
Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| title_fullStr |
Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| title_full_unstemmed |
Alternative Splicing of <i>TaGS3</i> Differentially Regulates Grain Weight and Size in Bread Wheat |
| title_sort |
alternative splicing of <i>tags3</i> differentially regulates grain weight and size in bread wheat |
| publisher |
MDPI AG |
| publishDate |
2021 |
| url |
https://doaj.org/article/a6d7be55fa5448728a7d993e79bcfa2b |
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