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Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility.
Plant Cell. 2006 Oct; 18(10):2531-53.PC

Abstract

Petunia inflata S-locus F-box (Pi SLF) is thought to function as a typical F-box protein in ubiquitin-mediated protein degradation and, along with Skp1, Cullin-1, and Rbx1, could compose an SCF complex mediating the degradation of nonself S-RNase but not self S-RNase. We isolated three P. inflata Skp1s (Pi SK1, -2, and -3), two Cullin-1s (Pi CUL1-C and -G), and an Rbx1 (Pi RBX1) cDNAs and found that Pi CUL1-G did not interact with Pi RBX1 and that none of the three Pi SKs interacted with Pi SLF(2). We also isolated a RING-HC protein, S-RNase Binding Protein1 (Pi SBP1), almost identical to Petunia hybrida SBP1, which interacts with Pi SLFs, S-RNases, Pi CUL1-G, and an E2 ubiquitin-conjugating enzyme, suggesting that Pi CUL1-G, SBP1, and SLF may be components of a novel E3 ligase complex, with Pi SBP1 playing the roles of Skp1 and Rbx1. S-RNases interact more with nonself Pi SLFs than with self Pi SLFs, and Pi SLFs also interact more with nonself S-RNases than with self S-RNases. Bacterially expressed S(1)-, S(2)-, and S(3)-RNases are degraded by the 26S proteasomal pathway in a cell-free system, albeit not in an S-allele-specific manner. Native glycosylated S(3)-RNase is not degraded to any significant extent; however, deglycosylated S(3)-RNase is degraded as efficiently as the bacterially expressed S-RNases. Finally, S-RNases are ubiquitinated in pollen tube extracts, but whether this is mediated by the Pi SLF-containing E3 complex is unknown.

Authors+Show Affiliations

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

Pub Type(s)

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

Language

eng

PubMed ID

17028207

Citation

Hua, Zhihua, and Teh-Hui Kao. "Identification and Characterization of Components of a Putative Petunia S-locus F-box-containing E3 Ligase Complex Involved in S-RNase-based Self-incompatibility." The Plant Cell, vol. 18, no. 10, 2006, pp. 2531-53.
Hua Z, Kao TH. Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility. Plant Cell. 2006;18(10):2531-53.
Hua, Z., & Kao, T. H. (2006). Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility. The Plant Cell, 18(10), 2531-53.
Hua Z, Kao TH. Identification and Characterization of Components of a Putative Petunia S-locus F-box-containing E3 Ligase Complex Involved in S-RNase-based Self-incompatibility. Plant Cell. 2006;18(10):2531-53. PubMed PMID: 17028207.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification and characterization of components of a putative petunia S-locus F-box-containing E3 ligase complex involved in S-RNase-based self-incompatibility. AU - Hua,Zhihua, AU - Kao,Teh-Hui, Y1 - 2006/10/06/ PY - 2006/10/10/pubmed PY - 2006/12/21/medline PY - 2006/10/10/entrez SP - 2531 EP - 53 JF - The Plant cell JO - Plant Cell VL - 18 IS - 10 N2 - Petunia inflata S-locus F-box (Pi SLF) is thought to function as a typical F-box protein in ubiquitin-mediated protein degradation and, along with Skp1, Cullin-1, and Rbx1, could compose an SCF complex mediating the degradation of nonself S-RNase but not self S-RNase. We isolated three P. inflata Skp1s (Pi SK1, -2, and -3), two Cullin-1s (Pi CUL1-C and -G), and an Rbx1 (Pi RBX1) cDNAs and found that Pi CUL1-G did not interact with Pi RBX1 and that none of the three Pi SKs interacted with Pi SLF(2). We also isolated a RING-HC protein, S-RNase Binding Protein1 (Pi SBP1), almost identical to Petunia hybrida SBP1, which interacts with Pi SLFs, S-RNases, Pi CUL1-G, and an E2 ubiquitin-conjugating enzyme, suggesting that Pi CUL1-G, SBP1, and SLF may be components of a novel E3 ligase complex, with Pi SBP1 playing the roles of Skp1 and Rbx1. S-RNases interact more with nonself Pi SLFs than with self Pi SLFs, and Pi SLFs also interact more with nonself S-RNases than with self S-RNases. Bacterially expressed S(1)-, S(2)-, and S(3)-RNases are degraded by the 26S proteasomal pathway in a cell-free system, albeit not in an S-allele-specific manner. Native glycosylated S(3)-RNase is not degraded to any significant extent; however, deglycosylated S(3)-RNase is degraded as efficiently as the bacterially expressed S-RNases. Finally, S-RNases are ubiquitinated in pollen tube extracts, but whether this is mediated by the Pi SLF-containing E3 complex is unknown. SN - 1040-4651 UR - https://www.unboundmedicine.com/medline/citation/17028207/Identification_and_characterization_of_components_of_a_putative_petunia_S_locus_F_box_containing_E3_ligase_complex_involved_in_S_RNase_based_self_incompatibility_ L2 - http://www.plantcell.org/cgi/pmidlookup?view=long&pmid=17028207 DB - PRIME DP - Unbound Medicine ER -