Abstract
Genome-wide comparisons across 10 species from algae Guillardia theta to mammal human indicated that Caenorhabditis elegans and Caenorhabditis briggsae were highly enriched for glycine-rich secreted peptides (GRSPs) (110 GRSPs in C. elegans and 93 in C. briggsae) in this study. Chromosomal mapping showed that most GRSPs were clustered on the two nematode genomes [103 (93.64%) in C. elegans and 82 (88.17%) in C. briggsae], which could be divided into 18 cluster units in C. elegans and 13 in C. briggsae, respectively. Except for four C. elegans GRSPs clusters without matching clusters in C. briggsae, all other GRSPs clusters had paired synteny block between the two nematode genomes. Analyzing transcriptome datasets quantified by microarray indicated extensive genome-wide co-expression of GRSPs clusters after C. elegans infections. Highly homologous coding sequences and conserved exon–intron structures indicated that GRSPs tight clusters were likely derived from local DNA duplications. Phylogenetic conservation of synteny blocks between their genomes, co-expression of GRSPs clusters after C. elegans infections, and strong purifying selections of coding sequences may indicate evolutionary constraints acting on C. elegans to guarantee that C. elegans could mount rapid systematic responses to infections by co-expression, co-regulation, and co-functionality of GRSPs clusters.
Highlights
According to the primary structure, glycine‐rich proteins can be classified into two classes: (1) consisting of large glycine‐rich proteins (GRPs >200 AA) with a length of over 200 aminoNematology - Concepts, Diagnosis and Control acids that typically function as cell wall structural components and (2) composed of small glycine‐rich secreted peptides (GRSPs,
To have a general knowledge of the two nematodes, in the present work, we focused on (1) genome‐wide identification and classification of GRSPs which would provide a global view of GRSPs evolution in the two nematodes, (2) mapping these GRSPs on their genomes which would provide a global view of GRSPs distributions on their chromosomes, (3) phylogenetic analyses based on signal
D. melano‐ gaster and A. thaliana are enriched for GRSPs when compared to the other species analyzed here, which may indicate that an evolutionary expansion of GRSPs happened in nematodes, arthropods, and plants over evolutionary adaption and speciation
Summary
According to the primary structure, glycine‐rich proteins can be classified into two classes: (1) consisting of large glycine‐rich proteins (GRPs >200 AA) with a length of over 200 aminoNematology - Concepts, Diagnosis and Control acids that typically function as cell wall structural components and (2) composed of small glycine‐rich secreted peptides (GRSPs,
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