AI Article Synopsis
- Previous SDS PAGE gel analysis showed distinct protein patterns in floral nectars from petunia and tobacco, with petunia nectar containing significant RNase activities.
- To identify the active proteins, RNase bands were excised, digested with trypsin, and analyzed through LC-MS/MS, revealing S-RNases and other proteins like peroxidases and fructokinases.
- RT-PCR assays confirmed the expression of these proteins in petunia floral nectary, highlighting their potential role in antimicrobial activity within nectar.
Article Abstract
Previous SDS PAGE gel analysis of the floral nectars from petunia and tobacco plants revealed significant differences in the protein patterns. Petunia floral nectar was shown to contain a number of RNase activities by in gel RNase activity assay. To identify these proteins in more detail, the bands with RNase activity were excised from gel and subjected to trypsin digestion followed by LC-MS/MS analysis. This analysis revealed that S-RNases accumulate in nectar from Petunia hybrida, where they should carry out a biological function different from self-pollen rejection. In addition, other proteins were identified by the LC-MS/MS analysis. These proteins include a peroxidase, an endochitinase, and a putative fructokinase. Each of these proteins contained a secretory signal sequence that marked them as potential nectar proteins. We developed RT-PCR assays for each of these five proteins and demonstrated that each of these proteins was expressed in the petunia floral nectary. A discussion of the role of these proteins in antimicrobial activity in nectar is presented.
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| http://dx.doi.org/10.1016/j.jplph.2010.10.002 | DOI Listing |
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