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Example sentences for: meloidogyne
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Brugia, Meloidogyne and Caenorhabditis represent three separate major nematode clades (III, IV and V, respectively) [ 53 ] . Possible explanations for the discrepancy in matches are that the Brugia clusters contain a large fraction of non-coding sequences (that is, 5' and 3' UTR, unspliced introns) or have undergone more rapid molecular evolution and diversification.
Second, both organisms establish intimate developmental interactions with host plants, and mounting evidence suggests that the mechanisms for these interactions are also shared [ 31 ] . It seems a reasonable hypothesis that the origin of parasitism in Meloidogyne may have been facilitated by acquisition of genetic material from soil bacteria through horizontal transfer.
Following isolation from G. rostochiensis and H. glycines [ 5 ] , cellulases have been identified in M. incognita [ 6 ] , G. tabacum [ 68 ] , H. schachtii [ 69 ] , and P. penetrans [ 70 ] . Additional prokaryotic-like sequences identified in plant parasitic nematodes include other cell-wall-degrading enzymes such as xylanase [ 7 ] , pectate lyase [ 8 71 ] and polygalacturonase [ 72 ] , and evidence is accumulating that these sequences have been acquired by horizontal gene transfer [ 11 ] . The known Meloidogyne cellulase (MI00483.cl), potentially novel cellulases (MI00537.cl, MI01196.cl, MI01381.cl, MI01842.cl), and pectate lyase (MI00592.cl, MI00520.cl) were represented in the M. incognita EST clusters.
In particular, we considered how similar the Meloidogyne codon usage is to that of a 'typical' rhizobial protein by using the codon adaptation index (CAI) [ 44 ] . From an R. leguminosarum codon-usage table, we calculated the CAI for those amino acids precisely conserved between Mi-NodL and the rhizobial NodL protein to be 0.621 and 0.703 respectively.
In C. elegans , two genes each encode unusual bifunctional enzymes containing both isocitrate lyase and malate synthase domains [ 49 ] . Since the isocitrate lyase domain lies within the amino-terminal half of the C. elegans bifunctional enzyme and none of the Meloidogyne EST reads stretches across both domains, further sequencing of the 3' end of cDNA clones from the M. hapla or M. javanica isocitrate lyase ESTs will be necessary to determine whether the Meloidogyne genus contains a bifunctional glyoxylate enzyme homolog similar to that of
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