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Pollen S-locus F-box proteins of Petunia involved in S-RNase-based self-incompatibility are themselves subject to ubiquitin-mediated degradation.
Plant J. 2015 Jul; 83(2):213-23.PJ

Abstract

Many flowering plants show self-incompatibility, an intra-specific reproductive barrier by which pistils reject self-pollen to prevent inbreeding and accept non-self pollen to promote out-crossing. In Petunia, the polymorphic S-locus determines self/non-self recognition. The locus contains a gene encoding an S-RNase, which controls pistil specificity, and multiple S-locus F-box (SLF) genes that collectively control pollen specificity. Each SLF is a component of an SCF (Skp1/Cullin/F-box) complex that is responsible for mediating degradation of non-self S-RNase(s), with which the SLF interacts, via the ubiquitin-26S proteasome pathway. A complete set of SLFs is required to detoxify all non-self S-RNases to allow cross-compatible pollination. Here, we show that SLF1 of Petunia inflata is itself subject to degradation via the ubiquitin-26S proteasome pathway, and identify an 18 amino acid sequence in the C-terminal region of S2 -SLF1 (SLF1 of S2 haplotype) that contains a degradation motif. Seven of the 18 amino acids are conserved among all 17 SLF proteins of S2 haplotype and S3 haplotype involved in pollen specificity, suggesting that all SLF proteins are probably subject to similar degradation. Deleting the 18 amino acid sequence from S2 -SLF1 stabilized the protein but abolished its function in self-incompatibility, suggesting that dynamic cycling of SLF proteins is an integral part of their function in self-incompatibility.

Authors+Show Affiliations

Intercollege Graduate Degree Program in Plant Biology, Pennsylvania State University, University Park, PA, 16802, USA.Intercollege Graduate Degree Program in Plant Biology, Pennsylvania State University, University Park, PA, 16802, USA.Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA.Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA.Intercollege Graduate Degree Program in Plant Biology, Pennsylvania State University, University Park, PA, 16802, USA. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

25990372

Citation

Sun, Penglin, et al. "Pollen S-locus F-box Proteins of Petunia Involved in S-RNase-based Self-incompatibility Are Themselves Subject to Ubiquitin-mediated Degradation." The Plant Journal : for Cell and Molecular Biology, vol. 83, no. 2, 2015, pp. 213-23.
Sun P, Li S, Lu D, et al. Pollen S-locus F-box proteins of Petunia involved in S-RNase-based self-incompatibility are themselves subject to ubiquitin-mediated degradation. Plant J. 2015;83(2):213-23.
Sun, P., Li, S., Lu, D., Williams, J. S., & Kao, T. H. (2015). Pollen S-locus F-box proteins of Petunia involved in S-RNase-based self-incompatibility are themselves subject to ubiquitin-mediated degradation. The Plant Journal : for Cell and Molecular Biology, 83(2), 213-23. https://doi.org/10.1111/tpj.12880
Sun P, et al. Pollen S-locus F-box Proteins of Petunia Involved in S-RNase-based Self-incompatibility Are Themselves Subject to Ubiquitin-mediated Degradation. Plant J. 2015;83(2):213-23. PubMed PMID: 25990372.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pollen S-locus F-box proteins of Petunia involved in S-RNase-based self-incompatibility are themselves subject to ubiquitin-mediated degradation. AU - Sun,Penglin, AU - Li,Shu, AU - Lu,Dihong, AU - Williams,Justin S, AU - Kao,Teh-Hui, Y1 - 2015/05/31/ PY - 2015/02/23/received PY - 2015/04/05/revised PY - 2015/04/24/accepted PY - 2015/5/21/entrez PY - 2015/5/21/pubmed PY - 2016/4/6/medline KW - Petunia inflata KW - S-locus F-box proteins KW - degron KW - protein degradation KW - self-incompatibility KW - ubiquitin-26S proteasome pathway SP - 213 EP - 23 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 83 IS - 2 N2 - Many flowering plants show self-incompatibility, an intra-specific reproductive barrier by which pistils reject self-pollen to prevent inbreeding and accept non-self pollen to promote out-crossing. In Petunia, the polymorphic S-locus determines self/non-self recognition. The locus contains a gene encoding an S-RNase, which controls pistil specificity, and multiple S-locus F-box (SLF) genes that collectively control pollen specificity. Each SLF is a component of an SCF (Skp1/Cullin/F-box) complex that is responsible for mediating degradation of non-self S-RNase(s), with which the SLF interacts, via the ubiquitin-26S proteasome pathway. A complete set of SLFs is required to detoxify all non-self S-RNases to allow cross-compatible pollination. Here, we show that SLF1 of Petunia inflata is itself subject to degradation via the ubiquitin-26S proteasome pathway, and identify an 18 amino acid sequence in the C-terminal region of S2 -SLF1 (SLF1 of S2 haplotype) that contains a degradation motif. Seven of the 18 amino acids are conserved among all 17 SLF proteins of S2 haplotype and S3 haplotype involved in pollen specificity, suggesting that all SLF proteins are probably subject to similar degradation. Deleting the 18 amino acid sequence from S2 -SLF1 stabilized the protein but abolished its function in self-incompatibility, suggesting that dynamic cycling of SLF proteins is an integral part of their function in self-incompatibility. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/25990372/Pollen_S_locus_F_box_proteins_of_Petunia_involved_in_S_RNase_based_self_incompatibility_are_themselves_subject_to_ubiquitin_mediated_degradation_ L2 - https://doi.org/10.1111/tpj.12880 DB - PRIME DP - Unbound Medicine ER -