The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae
The effector AvrPiz-t of Magnaporthe oryzae has virulence function in rice. However, the mechanism underlying its virulence in host is not fully understood. Results In this study, we analyzed the function of AvrPiz-t interacting protein 12 (APIP12) in rice immunity. APIP12 significantly bound to Avr...
| Autores principales: | , , , , , , , , |
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| Formato: | Journal Article |
| Lenguaje: | Inglés |
| Publicado: |
Springer
2017
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| Acceso en línea: | https://hdl.handle.net/10568/165097 |
| _version_ | 1855526246991003648 |
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| author | Tang, Mingzhi Ning, Yuese Shu, Xiaoli Dong, Bo Zhang, Hong Yan Wu, Dianxing Wang, Hua Wang, Guo-Liang Zhou, Bo |
| author_browse | Dong, Bo Ning, Yuese Shu, Xiaoli Tang, Mingzhi Wang, Guo-Liang Wang, Hua Wu, Dianxing Zhang, Hong Yan Zhou, Bo |
| author_facet | Tang, Mingzhi Ning, Yuese Shu, Xiaoli Dong, Bo Zhang, Hong Yan Wu, Dianxing Wang, Hua Wang, Guo-Liang Zhou, Bo |
| author_sort | Tang, Mingzhi |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | The effector AvrPiz-t of Magnaporthe oryzae has virulence function in rice. However, the mechanism underlying its virulence in host is not fully understood. Results In this study, we analyzed the function of AvrPiz-t interacting protein 12 (APIP12) in rice immunity. APIP12 significantly bound to AvrPiz-t and APIP6 in its middle portion and N-terminus, respectively, in yeast two-hybrid assay. Glutathione S-transferase (GST) pull-down assay further verified the interactions of APIP12 with AvrPiz-t and APIP6. APIP12 encodes a homologue of nucleoporin protein Nup98 without the conserved domain of Phe-Gly repeats and has no orthologue in other plants. Both knockout and knockdown of APIP12 caused enhanced susceptibility of rice plants to virulent isolates of M. oryzae. The expression of some pathogenesis-related (PR) genes was reduced in both knockout and knockdown mutants, suggesting that APIP12 is required for the accumulation of transcripts of PR genes upon the infection. It is worth noting that neither knockout/knockdown nor overexpression of APIP12 attenuates Piz-t resistance. Taken together, our results demonstrate that APIP12 is a virulence target of AvrPiz-t and is involved in the basal resistance against M. oryzae in rice |
| format | Journal Article |
| id | CGSpace165097 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 2017 |
| publishDateRange | 2017 |
| publishDateSort | 2017 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | CGSpace1650972025-05-14T10:24:10Z The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae Tang, Mingzhi Ning, Yuese Shu, Xiaoli Dong, Bo Zhang, Hong Yan Wu, Dianxing Wang, Hua Wang, Guo-Liang Zhou, Bo The effector AvrPiz-t of Magnaporthe oryzae has virulence function in rice. However, the mechanism underlying its virulence in host is not fully understood. Results In this study, we analyzed the function of AvrPiz-t interacting protein 12 (APIP12) in rice immunity. APIP12 significantly bound to AvrPiz-t and APIP6 in its middle portion and N-terminus, respectively, in yeast two-hybrid assay. Glutathione S-transferase (GST) pull-down assay further verified the interactions of APIP12 with AvrPiz-t and APIP6. APIP12 encodes a homologue of nucleoporin protein Nup98 without the conserved domain of Phe-Gly repeats and has no orthologue in other plants. Both knockout and knockdown of APIP12 caused enhanced susceptibility of rice plants to virulent isolates of M. oryzae. The expression of some pathogenesis-related (PR) genes was reduced in both knockout and knockdown mutants, suggesting that APIP12 is required for the accumulation of transcripts of PR genes upon the infection. It is worth noting that neither knockout/knockdown nor overexpression of APIP12 attenuates Piz-t resistance. Taken together, our results demonstrate that APIP12 is a virulence target of AvrPiz-t and is involved in the basal resistance against M. oryzae in rice 2017-12 2024-12-19T12:54:42Z 2024-12-19T12:54:42Z Journal Article https://hdl.handle.net/10568/165097 en Open Access Springer Tang, Mingzhi; Ning, Yuese; Shu, Xiaoli; Dong, Bo; Zhang, Hongyan; Wu, Dianxing; Wang, Hua; Wang, Guo-Liang and Zhou, Bo. 2017. The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae. Rice, Volume 10, no. 1 |
| spellingShingle | Tang, Mingzhi Ning, Yuese Shu, Xiaoli Dong, Bo Zhang, Hong Yan Wu, Dianxing Wang, Hua Wang, Guo-Liang Zhou, Bo The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title | The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title_full | The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title_fullStr | The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title_full_unstemmed | The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title_short | The Nup98 homolog APIP12 targeted by the effector AvrPiz-t is involved in rice basal resistance against Magnaporthe oryzae |
| title_sort | nup98 homolog apip12 targeted by the effector avrpiz t is involved in rice basal resistance against magnaporthe oryzae |
| url | https://hdl.handle.net/10568/165097 |
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