A flax fibre proteome: identification of proteins enriched in bast fibres.
BACKGROUND
Bast fibres from the phloem tissues of flax are scientifically interesting and economically useful due in part to a dynamic system of secondary cell wall deposition. To better understand the molecular mechanisms underlying the process of cell wall development in flax, we extracted proteins from individually dissected phloem fibres (i.e. individual cells) at an early stage of secondary cell wall development, and compared these extracts to protein extracts from surrounding, non-fibre cells of the cortex, using fluorescent (DiGE) labels and 2D-gel electrophoresis, with identities assigned to some proteins by mass spectrometry.


RESULTS
The abundance of many proteins in fibres was notably different from the surrounding non-fibre cells of the cortex, with approximately 13% of the 1,850 detectable spots being significantly (> 1.5 fold, p < or = 0.05) enriched in fibres. Following mass spectrometry, we assigned identity to 114 spots, of which 51 were significantly enriched in fibres. We observed that a K+ channel subunit, annexins, porins, secretory pathway components, beta-amylase, beta-galactosidase and pectin and galactan biosynthetic enzymes were among the most highly enriched proteins detected in developing flax fibres, with many of these proteins showing electrophoretic patterns consistent with post-translational modifications.


CONCLUSIONS
The fibre-enriched proteins we identified are consistent with the dynamic process of secondary wall deposition previously suggested by histological and biochemical analyses, and particularly the importance of galactans and the secretory pathway in this process. The apparent abundance of beta-amylase suggests that starch may be an unappreciated source of materials for cell wall biogenesis in flax bast fibres. Furthermore, our observations confirm previous reports that correlate accumulation proteins such as annexins, and specific heat shock proteins with secondary cell wall deposition.
Hotte
Naomi S C
NS
Department of Biological Sciences, Edmonton, T6G 2E9, Canada. nhotte@ualberta.ca
Deyholos
Michael K
MK
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism; D002244:Carbon / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D002853:Chromatography, Liquid; D003599:Cytoskeleton / Q000378:metabolism; D030562:Databases, Protein; D015180:Electrophoresis, Gel, Two-Dimensional; D004734:Energy Metabolism; D019597:Flax / Q000737:chemistry* / Q000166:cytology / Q000201:enzymology; D020869:Gene Expression Profiling; D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry; D010940:Plant Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D020543:Proteome / Q000032:analysis*
D000596:Amino Acids; D010455:Peptides; D010940:Plant Proteins; D011134:Polysaccharides; D020543:Proteome; D002244:Carbon; D000251:Adenosine Triphosphatases