Abstract
Acyl-CoA binding protein (ACBP) is a highly conserved 10-kDa intracellular lipid-binding protein that binds straight-chain (C14-C22) acyl-CoA esters with high affinity and is expressed in a wide variety of species ranging from yeast to mammals. Functionally, ACBP can act as an acyl-CoA carrier or as an acyl-CoA pool maker within the cell. Much work on the biochemical properties regarding the ACBP has been performed using various vertebrate and plant tissues, as well as different types of cells in culture, the regulatory mechanisms underlying ACBP gene expression have remained poorly understood. By exploiting the unique sex pheromone production system in the moth pheromone gland (PG), we report that transcription of a specific ACBP termed pheromone gland ACBP is triggered by a hemolymph-based humoral factor. Following purification and structure elucidation by means of high resolution electrospray ionization mass spectrometry and NMR analyses, in conjunction with stereochemical analyses using acid hydrolysates, the humoral factor was identified to be beta-D-glucosyl-O-L-tyrosine. Examination of the hemolymph titers during development revealed that the amount of beta-D-glucosyl-O-L-tyrosine dramatically rose prior to eclosion and reached a maximum of 5 mg/ml (about 1 mg/pupa) on the day preceding eclosion, which was consistent with the effective dose of beta-D-glucosyl-O-L-tyrosine in stimulating pheromone gland ACBP transcription in vivo. Furthermore, in vitro assays using trimmed PG indicated that beta-D-glucosyl-O-L-tyrosine acts directly on the PG. These results provide the first evidence that transcription of some ACBPs can be triggered by specific humoral factors.
Highlights
Ally highly conserved from yeast to mammals as well as insects (1)
We have demonstrated that two distinct Acyl-CoA binding protein (ACBP) are expressed in the pheromone gland (PG) during pheromonogenesis and undergo up-regulation on the day prior to eclosion in the female B. mori moth (18)
In the PGs of many moth species, various long chain fatty acyl-CoAs participate as precursors or intermediates in the biosynthesis of species-specific sex pheromones (30), suggesting that ACBPs expressed in the PG could possibly function as carriers or cellular deposits for the acyl-CoAs utilized in pheromone biosynthesis
Summary
Ally highly conserved from yeast to mammals as well as insects (1). the in vivo function of this protein has yet to be clarified in detail, in vitro investigations have revealed that ACBP protects acyl-CoA esters from hydrolysis (2– 4); it can function as both an acceptor and a donor of acyl-CoA esters (3) by regulating their availability for various metabolic purposes such as mitochondrial -oxidation (4 – 6), microsomal glycerolipid synthesis (4), and phospholipid synthesis (7, 8). Examination of the hemolymph titers during development revealed that the amount of -D-glucosyl-O-L-tyrosine dramatically rose prior to eclosion and reached a maximum of 5 mg/ml (about 1 mg/pupa) on the day preceding eclosion, which was consistent with the effective dose of -D-glucosyl-OL-tyrosine in stimulating pheromone gland ACBP transcription in vivo.
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