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

5 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
Externally publishedYes


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

ASJC Scopus subject areas

  • Animal Science and Zoology


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