title: Daylily protein constituents of the pollen and stigma a proteomics approach.
abstract: This study was aimed at the identification and quantification of the protein components of the pollen grains in parallel with the distal stigmatic tissue of tetraploid cultivars. Proteomes were analyzed using iTRAQ 4plex labeling, peptides separation by online RP-nano-LC and analysis by ESI-MS/MS. Protein identification and quantification were made using the Asparagales database as a reference. A total of 524,037 MS/MS spectra were produced from pollen and stigma samples. From these, a total of 8368 peptides wereidentified corresponding to 994 unique peptides and 432 protein groups. Among them, 128 differentially expressed proteins were retained for further analysis. In absence of the daylily genome availability, we exploited numerous databases and bioinformatics resources to exploring the putative biological functions of these proteins. The profile of differentially expressed proteins suggests an important representation of functions associated to the signalling and response against endogenous and environmental stresses, including several enzymes implicated in the biosynthesis of antibiotics. The abundance in stigma of several structural proteins of the ribosomal sub-units as well as of the core histones suggest that the translation processes and the regulation of gene expression in stigma is a more active mechanism than in pollen. In addition, pollen prioritizes the synthesis of fructose and glucose as opposed to sucrose in stigma as a source of energy. Finally, the modulated proteins in Hemerocallis point to several pathways that give potential clues concerning the molecular mechanisms underlying the functions of the pollen and the stigmatic fluid in daylily reproduction.
authors.affiliation: CHUL Research Center in Reproduction, Centre de Recherche du CHU de Québec,2705 Boulevard Laurier, Suite T3-67, Quebec City, QC, G1 V 4G2, Canada. Electronic address: roland.r.tremblay@crchudequebec.ulaval.ca.
authors.forename: Roland R
authors.initials: RR
authors.lastname: Tremblay
authors.affiliation: Proteomics Platform Quebec Genomics Center, CRCHUL, Centre de Recherche du CHU de Quebec, Canada. Electronic address: bourassa@crchudequebec.ulaval.ca.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Bourassa
authors.affiliation: Proteomics Platform Quebec Genomics Center, CRCHUL, Centre de Recherche du CHU de Quebec, Canada. Electronic address: Nehme@crchudequebec.ulaval.ca.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Nehmé
authors.affiliation: Scientific Consultant in Genomics, 701 Leonard, Quebec City, QC, G1X 4C9, Canada. Electronic address: ecalvo.omics@gmail.com.
authors.forename: Ezequiel L
authors.initials: EL
authors.lastname: Calvo
mesh_terms: D019295:Computational Biology; D035264:Flowers / Q000378:metabolism*; D005632:Fructose / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D005947:Glucose / Q000378:metabolism; D031421:Hemerocallis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D053858:Metabolic Networks and Pathways; D053147:Plant Exudates / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000502:physiology; D011058:Pollen / Q000378:metabolism*; D060066:Protein Interaction Maps; D020543:Proteome / Q000378:metabolism; D040901:Proteomics; D013395:Sucrose / Q000378:metabolism; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D053147:Plant Exudates; D010940:Plant Proteins; D020543:Proteome; D005632:Fructose; D013395:Sucrose; D005947:Glucose
keywords: Daylily; Hemerocallis; Pollen; Proteome; Stigma