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Background  Microorganisms produce cell-wall-degrading enzymes as part of their strategies for plant invasion/nutrition. Among these, pectin lyases (PNLs) catalyze the depolymerization of esterified pectin by a β-elimination mechanism. PNLs are grouped together with pectate lyases (PL) in Family 1 of the polysaccharide lyases, as they share a conserved structure in a parallel β-helix. The best-characterized fungal pectin lyases are obtained from saprophytic/opportunistic fungi in the genera  Aspergillus  and  Penicillium  and from some pathogens such as  Colletotrichum gloeosporioides .  The organism used in the present study,  Colletotrichum lindemuthianum , is a phytopathogenic fungus that can be subdivided into different physiological races with different capacities to infect its host,  Phaseolus vulgaris . These include the non-pathogenic and pathogenic strains known as races 0 and 1472, respectively.    Results  Here we report the isolation and sequence analysis of the  Clpnl2  gene, which encodes the pectin lyase 2 of  C. lindemuthianum , and its expression in pathogenic and non-pathogenic races of  C. lindemuthianum  grown on different carbon sources. In addition, we performed a phylogenetic analysis of the deduced amino acid sequence of Clpnl2 based on reported sequences of PNLs from other sources and compared the three-dimensional structure of Clpnl2, as predicted by homology modeling, with those of other organisms. Both analyses revealed an early separation of bacterial pectin lyases from those found in fungi and oomycetes. Furthermore, two groups could be distinguished among the enzymes from fungi and oomycetes: one comprising enzymes from mostly saprophytic/opportunistic fungi and the other formed mainly by enzymes from pathogenic fungi and oomycetes. Clpnl2 was found in the latter group and was grouped together with the pectin lyase from  C. gloeosporioides .    Conclusions  The  Clpnl2  gene of  C. lindemuthianum  shares the characteristic elements of genes coding for pectin lyases. A time-course analysis revealed significant differences between the two fungal races in terms of the expression of  Clpnl2  encoding for pectin lyase 2. According to the results, pectin lyases from bacteria and fungi separated early during evolution. Likewise, the enzymes from fungi and oomycetes diverged in accordance with their differing lifestyles. It is possible that the diversity and nature of the assimilatory carbon substrates processed by these organisms played a determinant role in this phenomenon.

bmc microbiology

Cloning and characterization of a pectin lyase gene from Colletotrichum lindemuthianumand comparative phylogenetic/structural analyses with genes from phytopathogenic and saprophytic/opportunistic microorganisms