Abstract
Pectin lyases are a group of enzymes that are thought to contribute to many biological processes, such as the degradation of pectin. However, until this study, no comprehensive study incorporating phylogeny, chromosomal location, gene duplication, gene organization, functional divergence, adaptive evolution, expression profiling and functional networks has been reported for Arabidopsis. Sixty-seven pectin lyase genes have been identified, and most of them possess signal sequences targeting the secretory pathway. Phylogenetic analyses identified five gene groups with considerable conservation among groups. Pectin lyase genes were non-randomly distributed across chromosomes and clustering was evident. Functional divergence and adaptive evolution analyses suggested that purifying selection was the main force driving pectin lyase evolution, although some critical sites responsible for functional divergence might be the consequence of positive selection. A stigma- and receptacle-specific expression promoter was identified, and it had increased expression in response to wounding. Two hundred and eighty-eight interactions were identified by functional network analyses, and most of these were involved in cellular metabolism, cellular transport and localization, and stimulus responses. This investigation contributes to an improved understanding of the complexity of the Arabidopsis pectin lyase gene family.
Highlights
Pectins are major primary cell walls components of land plants that are important for maintaining cellular structural integrity [1,2]
67 pectin lyase genes were identified in Arabidopsis (Table 1)
The results indicated that 50 members of pectin lyases possess signal peptide
Summary
Pectins are major primary cell walls components of land plants that are important for maintaining cellular structural integrity [1,2]. Pectins are a family of complex polysaccharides with 1,4linked a-D-galactosyluronic acid residues [1], and they can be degraded by pectinases. Polygalacturonases degrade polygalacturonan by hydrolysis of the glycosidic bonds that link galacturonic acid residues. Pectin lyases are the only known pectinase capable of degrading pectin polymers directly via a b-elimination mechanism that results in the formation of 4,5unsaturated oligogalacturonides without methanol production [3]. This is very important because methanol’s toxicity and unpleasant, volatile off flavors are a concern for the paper, food and textile industries [4,5]. Correlative studies about production, biochemical characterization, and applications of pectin lyases were recently reviewed [6]
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