Purification and characterization of coacervate-forming cuticular proteins from papilio xuthus pupae

Masahiro Yamanaka, Yumi Ishizaki, Taro Nakagawa, Azuma Taoka, Yoshihiro Fukumori

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)


    The Papilio xuthus (Lepidoptera: Papilionidae) pupa expresses novel soluble proteins that undergo reversible temperature-dependent coacervate-formation. We purified two coacervate-forming proteins, PX-1 and PX-4, from the wings of pharate adults. PX-1 and PX-4 form coacervates upon warming. Transmission electron microscopy analysis revealed that these proteins assemble ordered bead-like ultrastructures. We cloned and sequenced PX-1 and PX-4 cDNAs. The PX-1 and PX-4 amino acid sequences contain many hydrophobic residues and show homologies to insect cuticular proteins. Moreover, when recombinant PX-1 and PX-4 were overexpressed in Escherichia coli, both recombinant proteins exhibited temperature-dependent coacervation. Furthermore, analyses of truncated mutants of PX-1 suggest that both the Val/Pro-rich region and Gly/lle-rich regions of PX-1 are involved in such coacervation.

    Original languageEnglish
    Pages (from-to)534-542
    Number of pages9
    JournalZoological science
    Issue number7
    Publication statusPublished - Jul 1 2013


    • Coacervation
    • Papilio xuthus
    • butterfly
    • cuticular protein
    • pharate adult

    ASJC Scopus subject areas

    • Animal Science and Zoology


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