StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato
The OVATE family proteins (OFPs) are plant-specific proteins that modulate diverse aspects of plant growth and development. In tomato, OFP20 has been shown to interact with TONNEAU1 Recruiting Motif (TRM) proteins to regulate fruit shape. In this study, we demonstrated that the mutation of StOFP20 c...
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KeAi Communications Co., Ltd.
2023-03-01
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Online Access: | http://www.sciencedirect.com/science/article/pii/S2095311922001472 |
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author | Ju AI Ye WANG Ya-wen YAN Chen-xiao LI Wei LUO Ling MA Yi SHANG Dong-li GAO |
author_facet | Ju AI Ye WANG Ya-wen YAN Chen-xiao LI Wei LUO Ling MA Yi SHANG Dong-li GAO |
author_sort | Ju AI |
collection | DOAJ |
description | The OVATE family proteins (OFPs) are plant-specific proteins that modulate diverse aspects of plant growth and development. In tomato, OFP20 has been shown to interact with TONNEAU1 Recruiting Motif (TRM) proteins to regulate fruit shape. In this study, we demonstrated that the mutation of StOFP20 caused a shift from round to oval shaped tubers in a diploid accession C151, supporting the role of StOFP20 in controlling tuber shape. Its expression reached a maximum in the tuber initiation stage and then decreased as the tuber develops. To help elucidate the mechanism of tuber shape regulation by StOFP20, 27 TONNEAU1 Recruiting Motif (TRM) proteins were identified and 23 of them were successfully amplified in C151. A yeast two-hybrid assay identified three TRM proteins that interacted with StOFP20, which was confirmed by firefly luciferase complementation in tobacco leaves. The OVATE domain was indispensable for the interactions, while the necessity of the M10 motif in TRM proteins varied among the interactions between StOFP20 and the three TRMs. In summary, both StOFP20 and SlOFP20 directed interactions with TRM proteins, but the corresponding interactants were not completely consistent, implying that they exert regulatory roles through mechanisms that are only partially overlapping. |
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language | English |
publishDate | 2023-03-01 |
publisher | KeAi Communications Co., Ltd. |
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spelling | doaj-art-a9639db3220740a59e7b1084b78c84d42025-08-02T16:13:54ZengKeAi Communications Co., Ltd.Journal of Integrative Agriculture2095-31192023-03-01223752761StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potatoJu AI0Ye WANG1Ya-wen YAN2Chen-xiao LI3Wei LUO4Ling MA5Yi SHANG6Dong-li GAO7Yunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaYunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaCorrespondence GAO Dong-li, Tel/Fax: +86-871-65941383; Yunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.ChinaThe OVATE family proteins (OFPs) are plant-specific proteins that modulate diverse aspects of plant growth and development. In tomato, OFP20 has been shown to interact with TONNEAU1 Recruiting Motif (TRM) proteins to regulate fruit shape. In this study, we demonstrated that the mutation of StOFP20 caused a shift from round to oval shaped tubers in a diploid accession C151, supporting the role of StOFP20 in controlling tuber shape. Its expression reached a maximum in the tuber initiation stage and then decreased as the tuber develops. To help elucidate the mechanism of tuber shape regulation by StOFP20, 27 TONNEAU1 Recruiting Motif (TRM) proteins were identified and 23 of them were successfully amplified in C151. A yeast two-hybrid assay identified three TRM proteins that interacted with StOFP20, which was confirmed by firefly luciferase complementation in tobacco leaves. The OVATE domain was indispensable for the interactions, while the necessity of the M10 motif in TRM proteins varied among the interactions between StOFP20 and the three TRMs. In summary, both StOFP20 and SlOFP20 directed interactions with TRM proteins, but the corresponding interactants were not completely consistent, implying that they exert regulatory roles through mechanisms that are only partially overlapping.http://www.sciencedirect.com/science/article/pii/S2095311922001472potatotuber shapeOFP20TRM |
spellingShingle | Ju AI Ye WANG Ya-wen YAN Chen-xiao LI Wei LUO Ling MA Yi SHANG Dong-li GAO StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato Journal of Integrative Agriculture potato tuber shape OFP20 TRM |
title | StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato |
title_full | StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato |
title_fullStr | StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato |
title_full_unstemmed | StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato |
title_short | StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato |
title_sort | stofp20 regulates tuber shape and interacts with tonneau1 recruiting motif proteins in potato |
topic | potato tuber shape OFP20 TRM |
url | http://www.sciencedirect.com/science/article/pii/S2095311922001472 |
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