Open AccessApplication of proteomics to the study of pollination drops
Author(s) -
Prior Natalie,
Little Stefan A.,
Pirone Cary,
Gill Julia E.,
Smith Derek,
Han Jun,
Hardie Darryl,
O'Leary Stephen J. B.,
Wagner Rebecca E.,
Cross Tyra,
Coulter Andrea,
Borchers Christoph,
Olafson Robert W.,
von Aderkas Patrick
Publication year - 2013
Publication title -
applications in plant sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 23
ISSN - 2168-0450
DOI - 10.3732/apps.1300008
Subject(s) - biology , gymnosperm , pollination , proteomics , botany , shotgun proteomics , proteome , pollen , biochemistry , gene
• Premise of the study: Pollination drops are a formative component in gymnosperm pollen‐ovule interactions. Proteomics offers a direct method for the discovery of proteins associated with this early stage of sexual reproduction. • Methods: Pollination drops were sampled from eight gymnosperm species: Chamaecyparis lawsoniana (Port Orford cedar), Ephedra monosperma, Ginkgo biloba, Juniperus oxycedrus (prickly juniper), Larix × marschlinsii, Pseudotsuga menziesii (Douglas‐fir), Taxus × media , and Welwitschia mirabilis . Drops were collected by micropipette using techniques focused on preventing sample contamination. Drop proteins were separated using both gel and gel‐free methods. Tandem mass spectrometric methods were used including a triple quadrupole and an Orbitrap. • Results: Proteins are present in all pollination drops. Consistency in the protein complement over time was shown in L . × marschlinsii . Representative mass spectra from W. mirabilis chitinase peptide and E. monosperma serine carboxypeptidase peptide demonstrated high quality results. We provide a summary of gymnosperm pollination drop proteins that have been discovered to date via proteomics. • Discussion: Using proteomic methods, a dozen classes of proteins have been identified to date. Proteomics presents a way forward in deepening our understanding of the biological function of pollination drops.