scholarly journals Amino acid sequence of pheromone biosynthesis activating neuropeptide-II(PBAN-II) of the silkmoth, Bombyx mori.

1990 ◽  
Vol 54 (9) ◽  
pp. 2495-2497 ◽  
Author(s):  
Akihiro KITAMURA ◽  
Hiromichi NAGASAWA ◽  
Hiroshi KATAOKA ◽  
Tetsu ANDO ◽  
Akinori SUZUKI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bombyx Mori ◽  
Pheromone Biosynthesis ◽  
Pheromone Biosynthesis Activating Neuropeptide

scholarly journals Amino Acid Sequence of Pheromone Biosynthesis Activating Neuropeptide-II (PBAN-II) of the Silkmoth,Bombyx mori

1990 ◽  
Vol 54 (9) ◽  
pp. 2495-2497 ◽  
Author(s):  
Akihiro Kitamura ◽  
Hiromichi Nagasawa ◽  
Hiroshi Kataoka ◽  
Tetsu Ando ◽  
Akinori Suzuki
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bombyx Mori ◽  
Pheromone Biosynthesis ◽  
Pheromone Biosynthesis Activating Neuropeptide

scholarly journals Identification of a POU factor involved in regulating the neuron-specific expression of the gene encoding diapause hormone and pheromone biosynthesis-activating neuropeptide in Bombyx mori

2004 ◽  
Vol 380 (1) ◽  
pp. 255-263 ◽  
Author(s):  
Tian-Yi ZHANG ◽  
Le KANG ◽  
Zhi-Fang ZHANG ◽  
Wei-Hua XU
Keyword(s):  
Amino Acid ◽  
Bombyx Mori ◽  
Pupal Stage ◽  
Pheromone Biosynthesis ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
Specific Expression ◽  
Binding Characteristics ◽  
Pheromone Biosynthesis Activating Neuropeptide ◽  
Diapause Hormone

Diapause hormone (DH) and PBAN (pheromone biosynthesis-activating neuropeptide) are two important insect neuropeptides regulating development and reproduction respectively. In the present study, we report two Bombyx mori transcription factors interacting specifically with the promoter of Bom-DH-PBAN (where Bom-DH stands for B. mori DH); we named them DHMBP-1 and -2 (DH-modulator-binding proteins 1 and 2). The developmental changes of DHMBP-1/-2 are closely correlated with that of Bom-DH-PBAN mRNA throughout the pupal stage. Competition assays indicate that DHMBP-1 from Chinese B. mori possesses binding characteristics similar to those of the POU-M1 protein from Japanese B. mori. POU-M1 cDNAs were cloned from various tissues of Chinese B. mori and were found to be distinct from the previously published POU-M1 in amino acid residues 108–136 because of insertion mutations. Owing to this difference in amino acid residues, we named this cDNA POU-M2. Even though POU-M2 differs from POU-M1 at the N-terminal, the POU domain and the binding properties of both POU-M1 and -M2 are the same. Functional analysis showed that overexpression of POU-M2 in the Bombyx cell line BmN activated the promoter of Bom-DH-PBAN, but failed to activate a promoter in which the POU-binding element was mutated. The transcriptional activity of POU-M2 is probably regulated by other factors binding to the upstream of the promoter sequence. We show that the POU-M2-binding site was able to activate the transcription of a heterologous promoter of the gene encoding B. mori larval serum protein. POU-M1 was found to exhibit the same transcriptional activities as POU-M2. Taken together, these results demonstrate that POU-M2 plays an important role in the transcriptional regulation of the Bom-DH-PBAN gene.

Amino acid sequence of pheromone-biosynthesis-activating neuropeptide (PBAN) of the silkworm, Bombyxmori

1989 ◽  
Vol 163 (1) ◽  
pp. 520-526 ◽  
Author(s):  
Akihiro Kitamura ◽  
Hiromichi Nagasawa ◽  
Hiroshi Kataoka ◽  
Takashi Inoue ◽  
Shogo Matsumoto ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Pheromone Biosynthesis ◽  
Pheromone Biosynthesis Activating Neuropeptide

scholarly journals Amino acid sequence of eclosion hormone of the silkworm, Bombyx mori.

1987 ◽  
Vol 51 (8) ◽  
pp. 2307-2308 ◽  
Author(s):  
Takaharu KONO ◽  
Hiromichi NAGASAWA ◽  
Akira ISOGAI ◽  
Hajime FUGO ◽  
Akinori SUZUKI
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bombyx Mori ◽  
Eclosion Hormone ◽  
Silkworm Bombyx Mori
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