Functional significance of some particular amino acid residues in Bombyx mori pyridoxal kinase

Author(s):  
ShuoHao Huang ◽  
Ting Shu ◽  
JianYun Zhang ◽  
Wang Ma ◽  
Shu Wei ◽  
...  
1992 ◽  
Vol 73 (8) ◽  
pp. 1977-1986 ◽  
Author(s):  
N. L. Teterina ◽  
K. M. Kean ◽  
A. E. Gorbalenya ◽  
V. I. Agol ◽  
M. Girard

2004 ◽  
Vol 380 (1) ◽  
pp. 255-263 ◽  
Author(s):  
Tian-Yi ZHANG ◽  
Le KANG ◽  
Zhi-Fang ZHANG ◽  
Wei-Hua XU

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.


1966 ◽  
Vol 19 (3) ◽  
pp. 489 ◽  
Author(s):  
FHC Stewart

The sequential polypeptide [Ala-Gly-Ala-Gly-Ser-Gly]n has been prepared by polymerization of a hexapeptide p-nitrophenyl ester. This polymer contains the repeating sequence of amino acid residues present in the crystalline regions of Bombyx mori silk fibroin. The o-nitrophenylsulphenyl amino-protecting group was used extensively in the synthesis of the hexapeptide active monomer from which the polypeptide was obtained.


1989 ◽  
Vol 12 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Martin J. Tymms ◽  
Beth McInnes ◽  
Gary J. Waine ◽  
Brian F. Cheetham ◽  
Anthony W. Linnane

1992 ◽  
Vol 13 (1) ◽  
pp. 38-40 ◽  
Author(s):  
Anthony R. Poteete ◽  
Dale Rennell ◽  
Suzanne E. Bouvier

2004 ◽  
Vol 57 (4) ◽  
pp. 839-849 ◽  
Author(s):  
Jia-Hau Shiu ◽  
Chiu-Yueh Chen ◽  
Long-Sen Chang ◽  
Yi-Chun Chen ◽  
Yen-Chin Chen ◽  
...  

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