Tags

Type your tag names separated by a space and hit enter

The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae.
Rice (N Y). 2017 Dec; 10(1):5.R

Abstract

BACKGROUND

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.

CONCLUSIONS

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.

Authors+Show Affiliations

Institute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China. Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.Institute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.Institute of Nuclear-Agricultural Sciences, Zhejiang University, Hangzhou, China.Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China.Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China. Department of Plant Pathology, the Ohio State University, Columbus, 43210, USA.Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China. b.zhou@irri.org. The Division of Genetics and Biotechnology, International Rice Research Institute, Los Baños, 4031, Philippines. b.zhou@irri.org.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28205154

Citation

Tang, Mingzhi, et al. "The Nup98 Homolog APIP12 Targeted By the Effector AvrPiz-t Is Involved in Rice Basal Resistance Against Magnaporthe Oryzae." Rice (New York, N.Y.), vol. 10, no. 1, 2017, p. 5.
Tang M, Ning Y, Shu X, et al. The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae. Rice (N Y). 2017;10(1):5.
Tang, M., Ning, Y., Shu, X., Dong, B., Zhang, H., Wu, D., Wang, H., Wang, G. L., & Zhou, B. (2017). The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae. Rice (New York, N.Y.), 10(1), 5. https://doi.org/10.1186/s12284-017-0144-7
Tang M, et al. The Nup98 Homolog APIP12 Targeted By the Effector AvrPiz-t Is Involved in Rice Basal Resistance Against Magnaporthe Oryzae. Rice (N Y). 2017;10(1):5. PubMed PMID: 28205154.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The Nup98 Homolog APIP12 Targeted by the Effector AvrPiz-t is Involved in Rice Basal Resistance Against Magnaporthe oryzae. AU - Tang,Mingzhi, AU - Ning,Yuese, AU - Shu,Xiaoli, AU - Dong,Bo, AU - Zhang,Hongyan, AU - Wu,Dianxing, AU - Wang,Hua, AU - Wang,Guo-Liang, AU - Zhou,Bo, Y1 - 2017/02/15/ PY - 2016/10/21/received PY - 2017/02/10/accepted PY - 2017/2/17/entrez PY - 2017/2/17/pubmed PY - 2017/2/17/medline KW - APIP12 KW - AvrPiz-t KW - Blast resistance KW - Nup98 KW - Protein-protein interaction SP - 5 EP - 5 JF - Rice (New York, N.Y.) JO - Rice (N Y) VL - 10 IS - 1 N2 - BACKGROUND: 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. CONCLUSIONS: 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. SN - 1939-8425 UR - https://www.unboundmedicine.com/medline/citation/28205154/The_Nup98_Homolog_APIP12_Targeted_by_the_Effector_AvrPiz_t_is_Involved_in_Rice_Basal_Resistance_Against_Magnaporthe_oryzae_ L2 - https://dx.doi.org/10.1186/s12284-017-0144-7 DB - PRIME DP - Unbound Medicine ER -
Try the Free App:
Prime PubMed app for iOS iPhone iPad
Prime PubMed app for Android
Prime PubMed is provided
free to individuals by:
Unbound Medicine.