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Cullin1-P is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia.
Plant Cell Physiol. 2016 Nov; 57(11):2403-2416.PC

Abstract

Self-incompatibility (SI) in flowering plants is a genetic reproductive barrier to distinguish self- and non-self pollen to promote outbreeding. In Solanaceae, self-pollen is rejected by the ribonucleases expressed in the styles (S-RNases), via its cytotoxic function. On the other side, the male-determinant is the S-locus F-box proteins (SLFs) expressed in pollen. Multiple SLFs collaboratively detoxify non-self S-RNases, therefore, non-self recognition is the mode of self-/non-self discrimination in Solanaceae. It is considered that SLFs function as a substrate-recognition module of the Skp1-Cullin1-F-box (SCF) complex that inactivates non-self S-RNases via their polyubiquitination, which leads to degradation by 26S proteasome. In fact, PhSSK1 (Petunia hybrida SLF-interacting Skp1-like1) was identified as a specific component of SCFSLF and was shown to be essential for detoxification of S-RNase in Petunia However, different molecules are proposed as the candidate Cullin1, another component of SCFSLF, and there is as yet no definite conclusion. Here, we identified five Cullin1s from the expressed sequence tags (ESTs) derived from the male reproductive organ in Petunia Among them, only PhCUL1-P was co-immunoprecipitated with S7-SLF2. In vitro protein-binding assay suggested that PhSSK1 specifically forms a complex with PhCUL1-P in an SLF-dependent manner. Knockdown of PhCUL1-P suppressed fertility of transgenic pollen in cross-compatible pollination in the functional S-RNase-dependent manner. These results suggested that SCFSLF selectively uses PhCUL1-P. Phylogeny of Cullin1s indicates that CUL1-P is recruited into the SI machinery during the evolution of Solanaceae, suggesting that the SI components have evolved differently among species in Solanaceae and Rosaceae, despite both families sharing the S-RNase-based SI.

Authors+Show Affiliations

Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan. Present address: The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan. Present address: The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567-0047, Japan.Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan takayama@bs.naist.jp.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

27565207

Citation

Kubo, Ken-Ichi, et al. "Cullin1-P Is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia." Plant & Cell Physiology, vol. 57, no. 11, 2016, pp. 2403-2416.
Kubo KI, Tsukahara M, Fujii S, et al. Cullin1-P is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia. Plant Cell Physiol. 2016;57(11):2403-2416.
Kubo, K. I., Tsukahara, M., Fujii, S., Murase, K., Wada, Y., Entani, T., Iwano, M., & Takayama, S. (2016). Cullin1-P is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia. Plant & Cell Physiology, 57(11), 2403-2416.
Kubo KI, et al. Cullin1-P Is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia. Plant Cell Physiol. 2016;57(11):2403-2416. PubMed PMID: 27565207.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cullin1-P is an Essential Component of Non-Self Recognition System in Self-Incompatibility in Petunia. AU - Kubo,Ken-Ichi, AU - Tsukahara,Mai, AU - Fujii,Sota, AU - Murase,Kohji, AU - Wada,Yuko, AU - Entani,Tetsuyuki, AU - Iwano,Megumi, AU - Takayama,Seiji, Y1 - 2016/08/26/ PY - 2016/06/29/received PY - 2016/08/22/accepted PY - 2016/8/28/pubmed PY - 2017/3/28/medline PY - 2016/8/28/entrez KW - Petunia hybrida KW - Evolution of self-incompatibility KW - Non-self recognition KW - S-RNase-based self-incompatibility KW - Skp1-Cullin1-F-box type E3 ubiquitin ligase KW - Solanaceae SP - 2403 EP - 2416 JF - Plant & cell physiology JO - Plant Cell Physiol VL - 57 IS - 11 N2 - Self-incompatibility (SI) in flowering plants is a genetic reproductive barrier to distinguish self- and non-self pollen to promote outbreeding. In Solanaceae, self-pollen is rejected by the ribonucleases expressed in the styles (S-RNases), via its cytotoxic function. On the other side, the male-determinant is the S-locus F-box proteins (SLFs) expressed in pollen. Multiple SLFs collaboratively detoxify non-self S-RNases, therefore, non-self recognition is the mode of self-/non-self discrimination in Solanaceae. It is considered that SLFs function as a substrate-recognition module of the Skp1-Cullin1-F-box (SCF) complex that inactivates non-self S-RNases via their polyubiquitination, which leads to degradation by 26S proteasome. In fact, PhSSK1 (Petunia hybrida SLF-interacting Skp1-like1) was identified as a specific component of SCFSLF and was shown to be essential for detoxification of S-RNase in Petunia However, different molecules are proposed as the candidate Cullin1, another component of SCFSLF, and there is as yet no definite conclusion. Here, we identified five Cullin1s from the expressed sequence tags (ESTs) derived from the male reproductive organ in Petunia Among them, only PhCUL1-P was co-immunoprecipitated with S7-SLF2. In vitro protein-binding assay suggested that PhSSK1 specifically forms a complex with PhCUL1-P in an SLF-dependent manner. Knockdown of PhCUL1-P suppressed fertility of transgenic pollen in cross-compatible pollination in the functional S-RNase-dependent manner. These results suggested that SCFSLF selectively uses PhCUL1-P. Phylogeny of Cullin1s indicates that CUL1-P is recruited into the SI machinery during the evolution of Solanaceae, suggesting that the SI components have evolved differently among species in Solanaceae and Rosaceae, despite both families sharing the S-RNase-based SI. SN - 1471-9053 UR - https://www.unboundmedicine.com/medline/citation/27565207/Cullin1_P_is_an_Essential_Component_of_Non_Self_Recognition_System_in_Self_Incompatibility_in_Petunia_ L2 - https://academic.oup.com/pcp/article-lookup/doi/10.1093/pcp/pcw152 DB - PRIME DP - Unbound Medicine ER -