Tags

Type your tag names separated by a space and hit enter

Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility.
Plant Cell. 2007 Nov; 19(11):3593-609.PC

Abstract

Petunia inflata possesses S-RNase-based self-incompatibility (SI), which prevents inbreeding and promotes outcrossing. Two polymorphic genes at the S-locus, S-RNase and P. inflata S-locus F-box (Pi SLF), determine the pistil and pollen specificity, respectively. To understand how the interactions between Pi SLF and S-RNase result in SI responses, we identified four Pi SLF-like (Pi SLFL) genes and used them, along with two previously identified Pi SLFLs, for comparative studies with Pi SLF(2). We examined the in vivo functions of three of these Pi SLFLs and found that none functions in SI. These three Pi SLFLs and two other Pi SLFs either failed to interact with S(3)-RNase (a non-self S-RNase for all of them) or interacted much more weakly than did Pi SLF(2) in vitro. We divided Pi SLF(2) into FD1 (for Functional Domain1), FD2, and FD3, each containing one of the Pi SLF-specific regions, and used truncated Pi SLF(2), chimeric proteins between Pi SLF(2) and one of the Pi SLFLs that did not interact with S(3)-RNase, and chimeric proteins between Pi SLF(1) and Pi SLF(2) to address the biochemical roles of these three domains. The results suggest that FD2, conserved among three allelic variants of Pi SLF, plays a major role in the strong interaction with S-RNase; additionally, FD1 and FD3 (each containing one of the two variable regions of Pi SLF) together negatively modulate this interaction, with a greater effect on interactions with self S-RNase than with non-self S-RNases. A model for how an allelic product of Pi SLF determines the fate of its self and non-self S-RNases in the pollen tube is presented.

Authors+Show Affiliations

Pensylvania State University, University Park, Pensylvania 16802, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

18024566

Citation

Hua, Zhihua, et al. "Comparison of Petunia Inflata S-Locus F-box Protein (Pi SLF) With Pi SLF Like Proteins Reveals Its Unique Function in S-RNase Based Self-incompatibility." The Plant Cell, vol. 19, no. 11, 2007, pp. 3593-609.
Hua Z, Meng X, Kao TH. Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility. Plant Cell. 2007;19(11):3593-609.
Hua, Z., Meng, X., & Kao, T. H. (2007). Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility. The Plant Cell, 19(11), 3593-609.
Hua Z, Meng X, Kao TH. Comparison of Petunia Inflata S-Locus F-box Protein (Pi SLF) With Pi SLF Like Proteins Reveals Its Unique Function in S-RNase Based Self-incompatibility. Plant Cell. 2007;19(11):3593-609. PubMed PMID: 18024566.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Comparison of Petunia inflata S-Locus F-box protein (Pi SLF) with Pi SLF like proteins reveals its unique function in S-RNase based self-incompatibility. AU - Hua,Zhihua, AU - Meng,Xiaoying, AU - Kao,Teh-Hui, Y1 - 2007/11/16/ PY - 2007/11/21/pubmed PY - 2008/3/8/medline PY - 2007/11/21/entrez SP - 3593 EP - 609 JF - The Plant cell JO - Plant Cell VL - 19 IS - 11 N2 - Petunia inflata possesses S-RNase-based self-incompatibility (SI), which prevents inbreeding and promotes outcrossing. Two polymorphic genes at the S-locus, S-RNase and P. inflata S-locus F-box (Pi SLF), determine the pistil and pollen specificity, respectively. To understand how the interactions between Pi SLF and S-RNase result in SI responses, we identified four Pi SLF-like (Pi SLFL) genes and used them, along with two previously identified Pi SLFLs, for comparative studies with Pi SLF(2). We examined the in vivo functions of three of these Pi SLFLs and found that none functions in SI. These three Pi SLFLs and two other Pi SLFs either failed to interact with S(3)-RNase (a non-self S-RNase for all of them) or interacted much more weakly than did Pi SLF(2) in vitro. We divided Pi SLF(2) into FD1 (for Functional Domain1), FD2, and FD3, each containing one of the Pi SLF-specific regions, and used truncated Pi SLF(2), chimeric proteins between Pi SLF(2) and one of the Pi SLFLs that did not interact with S(3)-RNase, and chimeric proteins between Pi SLF(1) and Pi SLF(2) to address the biochemical roles of these three domains. The results suggest that FD2, conserved among three allelic variants of Pi SLF, plays a major role in the strong interaction with S-RNase; additionally, FD1 and FD3 (each containing one of the two variable regions of Pi SLF) together negatively modulate this interaction, with a greater effect on interactions with self S-RNase than with non-self S-RNases. A model for how an allelic product of Pi SLF determines the fate of its self and non-self S-RNases in the pollen tube is presented. SN - 1040-4651 UR - https://www.unboundmedicine.com/medline/citation/18024566/Comparison_of_Petunia_inflata_S_Locus_F_box_protein__Pi_SLF__with_Pi_SLF_like_proteins_reveals_its_unique_function_in_S_RNase_based_self_incompatibility_ DB - PRIME DP - Unbound Medicine ER -