Characterization of acyl-CoA-binding protein (ACBP) in the pheromone gland of the silkworm, Bombyx mori

Shogo Matsumoto, Toyoshi Yoshiga, Norihiro Yokoyama, Masashi Iwanaga, Seizo Koshiba, Takanori Kigawa, Hiroshi Hirota, Shigeyuki Yokoyama, Kazuhiro Okano, Kazuei Mita, Toru Shimada, Sadahiro Tatsuki

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)

Abstract

Various fatty acyl-CoAs are involved as intermediates or precursors of sex pheromone components in the biosynthetic pathway of the pheromones in many lepidopteran insects. We have purified a 10-kDa protein from the cytosolic fraction of Bombyx mori pheromone glands by using affinity chromatography with a palmitoyl-CoA-agarose column and reversed-phase HPLC. Amino acid sequence analysis of the fragment peptides obtained from the purified protein, and a homology search, revealed that this protein was a member of acyl-CoA-binding proteins (ACBPs). MALDI-TOF mass spectral analysis of the purified protein and cloning of the gene from a pheromone gland cDNA library confirmed B. mori ACBP to be a 90 amino acid protein with 78.9% identity to that of Manduca sexta ACBP. The secondary structure of the recombinant B. mori ACBP was determined by NMR spectroscopy. Northern blot analysis demonstrated that B. mori ACBP was predominantly expressed in the pheromone gland and the corresponding transcript was expressed from the day before adult eclosion. Present results suggest that ACBP plays a significant role in the production of sex pheromones regulated by the neurohormone, pheromone biosynthesis activating neuropeptide (PBAN).

Original languageEnglish
Pages (from-to)603-609
Number of pages7
JournalInsect Biochemistry and Molecular Biology
Volume31
Issue number6-7
DOIs
Publication statusPublished - 2001 Apr 27
Externally publishedYes

Keywords

  • Acyl-CoA-binding protein
  • Bombyx mori
  • PBAN
  • Pheromone gland

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Insect Science

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