Identification of S-RNase and peroxidase in petunia nectar.

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.

journal_name

J Plant Physiol

authors

Hillwig MS,Kanobe C,Thornburg RW,Macintosh GC

doi

10.1016/j.jplph.2010.10.002

subject

Has Abstract

pub_date

2011-05-01 00:00:00

pages

734-8

issue

7

eissn

0176-1617

issn

1618-1328

pii

S0176-1617(10)00479-7

journal_volume

168

pub_type

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