Abstract

BackgroundArthropod cuticle is composed predominantly of a self-assembling matrix of chitin and protein. Genes encoding structural cuticular proteins are remarkably abundant in arthropod genomes, yet there has been no systematic survey of conserved motifs across cuticular protein families.Methodology/Principal FindingsTwo short sequence motifs with conserved tyrosines were identified in Drosophila cuticular proteins that were similar to the GYR and YLP Interpro domains. These motifs were found in members of the CPR, Tweedle, CPF/CPFL, and (in Anopheles gambiae) CPLCG cuticular protein families, and the Dusky/Miniature family of cuticle-associated proteins. Tweedle proteins have a characteristic motif architecture that is shared with the Drosophila protein GCR1 and its orthologs in other species, suggesting that GCR1 is also cuticular. A resilin repeat, which has been shown to confer elasticity, matched one of the motifs; a number of other Drosophila proteins of unknown function exhibit a motif architecture similar to that of resilin. The motifs were also present in some proteins of the peritrophic matrix and the eggshell, suggesting molecular convergence among distinct extracellular matrices. More surprisingly, gene regulation, development, and proteolysis were statistically over-represented ontology terms for all non-cuticular matches in Drosophila. Searches against other arthropod genomes indicate that the motifs are taxonomically widespread.ConclusionsThis survey suggests a more general definition for GYR and YLP motifs and reveals their contribution to several types of extracellular matrix. They may define sites of protein interaction with DNA or other proteins, based on ontology analysis. These results can help guide experimental studies on the biochemistry of cuticle assembly.

Highlights

  • Like many extracellular matrix proteins, arthropod cuticular proteins frequently contain a large proportion of low-complexity sequence

  • I generated an initial set of position-specific scoring matrices (PSSMs) from the resulting sequence alignments by using the BLOCKS server

  • GYR- and YLP-like motifs are common in Drosophila cuticular proteins

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Summary

Introduction

Like many extracellular matrix proteins, arthropod cuticular proteins frequently contain a large proportion of low-complexity sequence. While the functional significance of these low-complexity sequences in cuticle is not well understood, hypotheses include modulating physical properties of the protein, serving as protein modification sites, or promoting specific protein-protein interactions. Short repeated motifs of some chorion proteins are sufficient to induce self-assembly of amyloid fibrils [5], and the contribution of glycine and proline/hydroxyproline repeats to collagen aggregates has been extensively studied (reviewed by [6]). Post-translational modification sites are frequently marked by short conserved motifs in a variety of protein matrices [7,8]), and sites of cuticular protein modification or cross-linking are likely to be conserved. Genes encoding structural cuticular proteins are remarkably abundant in arthropod genomes, yet there has been no systematic survey of conserved motifs across cuticular protein families

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