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Biochemical models for S-RNase-based self-incompatibility.
Mol Plant. 2008 Jul; 1(4):575-85.MP

Abstract

S-RNase-based self-incompatibility (SI) is a genetically determined self/non-self-recognition process employed by many flowering plant species to prevent inbreeding and promote outcrosses. For the Plantaginaceae, Rosaceae and Solanaceae, it is now known that S-RNase and S-locus F-box (two multiple allelic genes at the S-locus) determine the female and male specificity, respectively, during SI interactions. However, how allelic products of these two genes interact inside pollen tubes to result in specific growth inhibition of self-pollen tubes remains to be investigated. Here, we review all the previously proposed biochemical models and discuss whether their predictions are consistent with all SI phenomena, including competitive interaction where SI breaks down in pollen that carries two different pollen S-alleles. We also discuss these models in light of the recent findings of compartmentalization of S-RNases in both incompatible and compatible pollen tubes. Lastly, we summarize the results from our recent biochemical studies of PiSLF (Petunia inflata SLF) and S-RNase, and present a new model for the biochemical mechanism of SI in the Solanaceae. The tenet of this model is that a PiSLF preferentially interacts with its non-self S-RNases in the cytoplasm of a pollen tube to result in the assembly of an E3-like complex, which then mediates ubiquitination and degradation of non-self S-RNases through the ubiquitin-26S proteasome pathway. This model can explain all SI phenomena and, at the same time, has raised new questions for further study.

Authors+Show Affiliations

The Pennsylvania State University, University Park, PA 16802, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

19825563

Citation

Hua, Zhi-Hua, et al. "Biochemical Models for S-RNase-based Self-incompatibility." Molecular Plant, vol. 1, no. 4, 2008, pp. 575-85.
Hua ZH, Fields A, Kao TH. Biochemical models for S-RNase-based self-incompatibility. Mol Plant. 2008;1(4):575-85.
Hua, Z. H., Fields, A., & Kao, T. H. (2008). Biochemical models for S-RNase-based self-incompatibility. Molecular Plant, 1(4), 575-85. https://doi.org/10.1093/mp/ssn032
Hua ZH, Fields A, Kao TH. Biochemical Models for S-RNase-based Self-incompatibility. Mol Plant. 2008;1(4):575-85. PubMed PMID: 19825563.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical models for S-RNase-based self-incompatibility. AU - Hua,Zhi-Hua, AU - Fields,Allison, AU - Kao,Teh-hui, Y1 - 2008/06/26/ PY - 2009/10/15/entrez PY - 2008/7/1/pubmed PY - 2010/1/12/medline SP - 575 EP - 85 JF - Molecular plant JO - Mol Plant VL - 1 IS - 4 N2 - S-RNase-based self-incompatibility (SI) is a genetically determined self/non-self-recognition process employed by many flowering plant species to prevent inbreeding and promote outcrosses. For the Plantaginaceae, Rosaceae and Solanaceae, it is now known that S-RNase and S-locus F-box (two multiple allelic genes at the S-locus) determine the female and male specificity, respectively, during SI interactions. However, how allelic products of these two genes interact inside pollen tubes to result in specific growth inhibition of self-pollen tubes remains to be investigated. Here, we review all the previously proposed biochemical models and discuss whether their predictions are consistent with all SI phenomena, including competitive interaction where SI breaks down in pollen that carries two different pollen S-alleles. We also discuss these models in light of the recent findings of compartmentalization of S-RNases in both incompatible and compatible pollen tubes. Lastly, we summarize the results from our recent biochemical studies of PiSLF (Petunia inflata SLF) and S-RNase, and present a new model for the biochemical mechanism of SI in the Solanaceae. The tenet of this model is that a PiSLF preferentially interacts with its non-self S-RNases in the cytoplasm of a pollen tube to result in the assembly of an E3-like complex, which then mediates ubiquitination and degradation of non-self S-RNases through the ubiquitin-26S proteasome pathway. This model can explain all SI phenomena and, at the same time, has raised new questions for further study. SN - 1674-2052 UR - https://www.unboundmedicine.com/medline/citation/19825563/Biochemical_models_for_S_RNase_based_self_incompatibility_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1674-2052(14)60365-8 DB - PRIME DP - Unbound Medicine ER -
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