Differential protein expression in compatible and incompatible pollen-pistil interactions in almond [Prunus dulcis (Miller) DA Webb] by 2D-DIGE and HPLC-MS/MS

Martinez-Garcia, P. J.; Gomez, E. M.; Casado-Vela, J.; Elortza, F.; Dicenta, F.; Ortega, E.

Journal of Horticultural Science and Biotechnology 90(1): 71-77

2015


ISSN/ISBN: 1462-0316
DOI: 10.1080/14620316.2015.11513155
Accession: 066296496

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Abstract
Self-incompatibility (SI) in almond [Prunus dulcis (Miller) D.A. Webb] is of the gametophytic-type and is controlled by the S-locus, which is highly polymorphic and includes two tightly-linked genes expressed in the pistil (as an S-RNase) and in the pollen [as an S haplotype-specific F-box (SFB) protein]. Experimental evidence indicates that other proteins are also needed for the functioning of self-incompatibility. However, to date, S-RNase and SFB are the only components of the SI system identified in almond. Moreover, the cause(s) of a lack of S-RNase activity in self-compatible almonds remain(s) unclear. This work aimed to identify the other proteins involved in the self(in)compatible response in almond by comparative quantitative analysis of the differential expression of proteins following incompatible and compatible pollinations. Four self-incompatible almond cultivars were self-pollinated or cross-pollinated, and a homozygous self-compatible almond selection was self-pollinated. Proteins were extracted from the pollinated pistils and analysed by two-dimensional difference gel electrophoresis (2D-DIGE) and high performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS). Searches were performed against the NCBI database using the MASCOT and SEQUEST search engines and Proteome Discoverer v1.4 software. A total of 43 proteins, some with a key role in pollen-pistil interactions, were identified as being differentially expressed following incompatible or compatible pollination. These results provide the first profiles of differential protein expression during self-(in)compatibility in almond.