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Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro.
Plant J. 2008 Jun; 54(6):1094-104.PJ

Abstract

S-RNase-based self-incompatibility has been identified in three flowering plant families, including the Solanaceae, and this self/non-self recognition mechanism between pollen and pistil is controlled by two polymorphic genes at the S-locus, S-RNase and S-locus F-box (SLF). S-RNase is produced in the pistil and taken up by pollen tubes in a non-S-haplotype-specific manner. How an allelic product of SLF interacts with self and non-self S-RNases to result in growth inhibition of self pollen tubes is not completely understood. One model predicts that SLF targets non-self S-RNases for ubiquitin/26S proteasome-mediated degradation, thereby only allowing self S-RNase to exert cytotoxic activity inside a pollen tube. To test this model, we studied whether any of the 20 lysine residues in S(3)-RNase of Petunia inflata might be targets for ubiquitination. We identified six lysines near the C-terminus for which mutation to arginine significantly reduced ubiquitination and degradation of the mutant S(3)-RNase, GST:S(3)-RNase (K141-164R) in pollen tube extracts. We further showed that GST:S(3)-RNase (K141-164R) and GST:S(3)-RNase had similar RNase activity, suggesting that their degradation was probably not caused by an ER-associated protein degradation pathway that removes mis-folded proteins. Finally, we showed that PiSBP1 (P. inflata S-RNase binding protein 1), a potential RING-HC subunit of the PiSLF (P. inflata SLF)-containing E3-like complex, could target S-RNase for ubiquitination in vitro. All these results suggest that ubiquitin/26S proteasome-dependent degradation of S-RNase may be an integral part of the S-RNase-based self-incompatibility mechanism.

Authors+Show Affiliations

Intercollege Graduate Degree Program in Plant Biology, The Pennsylvania State University, University Park, PA 16802, USA.No affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

18346191

Citation

Hua, Zhihua, and Teh-Hui Kao. "Identification of Major Lysine Residues of S(3)-RNase of Petunia Inflata Involved in ubiquitin-26S Proteasome-mediated Degradation in Vitro." The Plant Journal : for Cell and Molecular Biology, vol. 54, no. 6, 2008, pp. 1094-104.
Hua Z, Kao TH. Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro. Plant J. 2008;54(6):1094-104.
Hua, Z., & Kao, T. H. (2008). Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro. The Plant Journal : for Cell and Molecular Biology, 54(6), 1094-104. https://doi.org/10.1111/j.1365-313X.2008.03487.x
Hua Z, Kao TH. Identification of Major Lysine Residues of S(3)-RNase of Petunia Inflata Involved in ubiquitin-26S Proteasome-mediated Degradation in Vitro. Plant J. 2008;54(6):1094-104. PubMed PMID: 18346191.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of major lysine residues of S(3)-RNase of Petunia inflata involved in ubiquitin-26S proteasome-mediated degradation in vitro. AU - Hua,Zhihua, AU - Kao,Teh-Hui, Y1 - 2008/03/13/ PY - 2008/3/19/pubmed PY - 2009/7/1/medline PY - 2008/3/19/entrez SP - 1094 EP - 104 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 54 IS - 6 N2 - S-RNase-based self-incompatibility has been identified in three flowering plant families, including the Solanaceae, and this self/non-self recognition mechanism between pollen and pistil is controlled by two polymorphic genes at the S-locus, S-RNase and S-locus F-box (SLF). S-RNase is produced in the pistil and taken up by pollen tubes in a non-S-haplotype-specific manner. How an allelic product of SLF interacts with self and non-self S-RNases to result in growth inhibition of self pollen tubes is not completely understood. One model predicts that SLF targets non-self S-RNases for ubiquitin/26S proteasome-mediated degradation, thereby only allowing self S-RNase to exert cytotoxic activity inside a pollen tube. To test this model, we studied whether any of the 20 lysine residues in S(3)-RNase of Petunia inflata might be targets for ubiquitination. We identified six lysines near the C-terminus for which mutation to arginine significantly reduced ubiquitination and degradation of the mutant S(3)-RNase, GST:S(3)-RNase (K141-164R) in pollen tube extracts. We further showed that GST:S(3)-RNase (K141-164R) and GST:S(3)-RNase had similar RNase activity, suggesting that their degradation was probably not caused by an ER-associated protein degradation pathway that removes mis-folded proteins. Finally, we showed that PiSBP1 (P. inflata S-RNase binding protein 1), a potential RING-HC subunit of the PiSLF (P. inflata SLF)-containing E3-like complex, could target S-RNase for ubiquitination in vitro. All these results suggest that ubiquitin/26S proteasome-dependent degradation of S-RNase may be an integral part of the S-RNase-based self-incompatibility mechanism. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/18346191/Identification_of_major_lysine_residues_of_S_3__RNase_of_Petunia_inflata_involved_in_ubiquitin_26S_proteasome_mediated_degradation_in_vitro_ L2 - https://doi.org/10.1111/j.1365-313X.2008.03487.x DB - PRIME DP - Unbound Medicine ER -