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Science 16 March 1990:
Vol. 247. no. 4948, pp. 1333 - 1335
DOI: 10.1126/science.2315701
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Articles

Science, Vol 247, Issue 4948, 1333-1335
Copyright © 1990 by American Association for the Advancement of Science

articles

Molecular cloning of the Bombyx mori prothoracicotropic hormone

A Kawakami, H Kataoka, T Oka, A Mizoguchi, M Kimura-Kawakami, T Adachi, M Iwami, H Nagasawa, A Suzuki, and H Ishizaki

Department of Biology, School of Science, Nagoya University, Japan.

Prothoracicotropic hormone (PTTH), a brain secretory polypeptide of insects, stimulates the prothoracic glands to produce and release ecdysone, the steroid essential to insect development. The complementary DNAs encoding PTTH of the silkmoth Bombyx mori were cloned and characterized, and the complete amino acid sequence was deduced. The data indicated that PTTH is first synthesized as a 224-amino acid polypeptide precursor containing three proteolytic cleavage signals. The carboxyl-terminal component (109 amino acids) that follows the last cleavage signal represents one PTTH subunit. Two PTTH subunits are linked together by disulfide bonds, before or after cleavage from prepro-PTTH, to form a homodimeric PTTH. When introduced into Escherichia coli cells, the complementary DNA directed the expression of an active substance that was functionally indistinguishable from natural PTTH. In situ hybridization showed the localization of the prepro-PTTH mRNA to two dorsolateral neurosecretory cells of the Bombyx brain.


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Identification of a Prothoracicostatic Peptide in the Larval Brain of the Silkworm, Bombyx mori.
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