Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaster

1991 ◽  
Vol 230 (1-2) ◽  
pp. 97-103 ◽  
Author(s):  
Francisco J. Silva ◽  
Baltasar Escriche ◽  
Eugenio Ordoño ◽  
Juan Ferré
Keyword(s):  
Drosophila Melanogaster ◽  
Oxidase Activity ◽  
Biochemical Characterization

Soluble expression, purification and biochemical characterization of a C-7 cholesterol dehydrogenase from Drosophila melanogaster

Steroids ◽  
2019 ◽  
Vol 152 ◽  
pp. 108495
Author(s):  
Zhangliang Zhu ◽  
Chao Li ◽  
Xiaotao Cheng ◽  
Ying Chen ◽  
Menglu Zhu ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization ◽  
Soluble Expression

Genetic location and biochemical characterization of eye-colour mutants from natural populations of Drosophila melanogaster

Genome ◽  
1990 ◽  
Vol 33 (2) ◽  
pp. 203-208 ◽  
Author(s):  
M. Luisa Aparisi ◽  
Carmen Nájera
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization ◽  
Natural Populations ◽  
High Variability ◽  
Genetic Location ◽  
Eye Colour ◽  
Different Seasons ◽  
Allelism Tests ◽  
Mutation And Selection

From six captures of Drosophila melanogaster carried out in three different habitats (cellar, vineyard, and pinewood) in two different seasons of the year (spring and autumn), 60 eye-colour mutations were isolated, which were reduced to 29 loci by means of allelism tests within and between populations. Forty-five of these mutations were analyzed genetically and biochemically; of these 33 turned out to be previously described mutants and mapped to a total of 17 loci. Twelve new mutants were discovered and they mapped to 12 new loci, distributed on chromosomes X, II, and III. The eye-colour mutants show large effects on the red and brown pigments. The high variability of the eye-colour loci is discussed in relation to the mutation and selection hypotheses.Key words: eye-colour mutants, variability, mapping, Drosophila melanogaster, pigment patterns.

Molecular and Biochemical Characterization of the aaNATl (Dat) Locus in Drosophila melanogaster: Differential Expression of Two Gene Products

1998 ◽  
Vol 17 (7) ◽  
pp. 621-633 ◽  
Author(s):  
DANIELA BRODBECK ◽  
REMO AMHERD ◽  
PATRICK CALLAERTS ◽  
EDITH HINTERMANN ◽  
URS A. MEYER ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Differential Expression ◽  
Biochemical Characterization ◽  
Gene Products

GENETIC LOCALIZATION AND BIOCHEMICAL CHARACTERIZATION OF A TRANS-ACTING REGULATORY EFFECT IN DROSOPHILA

Genetics ◽  
1983 ◽  
Vol 105 (1) ◽  
pp. 55-69
Author(s):  
Joseph J King ◽  
John F McDonald
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization ◽  
Regulatory Gene ◽  
Regulatory Effect ◽  
Protein Levels ◽  
The Third ◽  
Genetic Localization ◽  
Glycerophosphate Dehydrogenase

ABSTRACT A region-specific, trans-acting regulatory gene that alters in vivo protein levels of α-glycerophosphate dehydrogenase (α-GPDH) has been mapped to position 55.4 on the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of α-GPDH in adult thoracic tissue but has no effect on α-GPDH levels in the abdomen. Although no other thoracic proteins were found to be influenced by the locus, it appears to modify the level of one additional abdominal protein. The action of the gene over development and its possible mode of control are discussed.

scholarly journals Cyclic nucleotide phosphodiesterases in Drosophila melanogaster

2005 ◽  
Vol 388 (1) ◽  
pp. 333-342 ◽  
Author(s):  
Jonathan P. DAY ◽  
Julian A. T. DOW ◽  
Miles D. HOUSLAY ◽  
Shireen-A. DAVIES
Keyword(s):  
Drosophila Melanogaster ◽  
Cyclic Nucleotide ◽  
Biochemical Characterization ◽  
Genetic Model ◽  
Renal Tubules ◽  
Drosophila Genome ◽  
Dual Specificity ◽  
And Function ◽  
High Degree

Cyclic nucleotide PDEs (phosphodiesterases) are important enzymes that regulate intracellular levels of cAMP and cGMP. In the present study, we identify and characterize novel PDEs in the genetic model, Drosophila melanogaster. The Drosophila genome encodes five novel PDE genes in addition to dunce. Predicted PDE sequences of Drosophila show highly conserved critical domains when compared with human PDEs. Thus PDE-encoding genes of D. melanogaster are CG14940-PDE1C, CG8279-PDE6β, CG5411-PDE8A, CG32648-PDE9 and CG10231-PDE11. Reverse transcriptase–PCRs of adult tissues reveal widespread expression of PDE genes. Drosophila Malpighian (renal) tubules express all the six PDEs: Drosophila PDE1, dunce (PDE4), PDE6, PDE8, PDE9 and PDE11. Antipeptide antibodies were raised against PDE1, PDE6, PDE9 and PDE11. Verification of antibody specificity by Western blotting of cloned and expressed PDE constructs allowed the immunoprecipitation studies of adult Drosophila lysates. Biochemical characterization of immunoprecipitated endogenous PDEs showed that PDE1 is a dual-specificity PDE (Michaelis constant Km for cGMP: 15.3±1 μM; Km cAMP: 20.5±1.5 μM), PDE6 is a cGMP-specific PDE (Km cGMP: 37±13 μM) and PDE11 is a dual-specificity PDE (Km cGMP: 6±2 μM; Km cAMP: 18.5±5.5 μM). Drosophila PDE1, PDE6 and PDE11 display sensitivity to vertebrate PDE inhibitors, zaprinast (IC50 was 71±39 μM for PDE1, 0.65±0.015 μM for PDE6 and 1.6±0.5 μM for PDE11) and sildenafil (IC50 was 1.3±0.9 μM for PDE1, 0.025±0.005 μM for PDE6 and 0.12±0.06 μM for PDE11). We provide the first characterization of a cGMP-specific PDE and two dual-specificity PDEs in Drosophila, and show a high degree of similarity in structure and function between human and Drosophila PDEs.

scholarly journals Molecular and biochemical characterization of two P450 enzymes in the ecdysteroidogenic pathway of Drosophila melanogaster

2002 ◽  
Vol 99 (17) ◽  
pp. 11043-11048 ◽  
Author(s):  
J. T. Warren ◽  
A. Petryk ◽  
G. Marques ◽  
M. Jarcho ◽  
J.-P. Parvy ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization

Biochemical-Characterization of Drosophila melanogaster Acetylcholinesterase Expressed by Recombinant Baculoviruses

1994 ◽  
Vol 203 (1) ◽  
pp. 734-742 ◽  
Author(s):  
H. Chaabihi ◽  
D. Fournier ◽  
Y. Fedon ◽  
J.P. Bossy ◽  
M. Ravallec ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization ◽  
Recombinant Baculoviruses

Molecular and biochemical characterization of Paragonimus westermani tyrosinase

Parasitology ◽  
2015 ◽  
Vol 142 (6) ◽  
pp. 807-815 ◽  
Author(s):  
Y.-A. BAE ◽  
S.-H. KIM ◽  
C.-S. AHN ◽  
J.-G. KIM ◽  
Y. KONG
Keyword(s):  
Oxidase Activity ◽  
Biochemical Characterization ◽  
Hydroxyl Groups ◽  
Reading Frame ◽  
Paragonimus Westermani ◽  
Rate Limiting Step ◽  
Tanning Process ◽  
Weak Activity ◽  
Rate Limiting

SUMMARYTrematode tyrosinases (TYRs) play a major role in the tanning process during eggshell formation. We investigated the molecular and biochemical features of Paragonimus westermani TYR (PwTYR). The PwTYR cDNA was composed of 1568-bp encompassing a 1422-bp-long open reading frame (474-amino acid polypeptide). A strong phylogenetic relationship with Platyhelminthes and Deuterostomian orthologues was evident. The recombinant PwTYR expressed in prokaryotic cells promptly oxidized diphenol substrates, with a preferential affinity toward ortho-positioned hydroxyl groups. It demonstrated fairly weak activity for monophenol compounds. Diphenol oxidase activity was augmented with an increase of pH from 5·0 to 8·0, while monophenol oxidase activity was highest at an acidic pH and gradually decreased as pH increased. Transcription profile of PwTYR was temporally upregulated along with worm development. PwTYR was specifically localized in vitellocytes and eggs. The results suggested that conversion of tyrosine to L-dihydroxyphenylalanine by PwTYR monophenol oxidase activity might be rate-limiting step during the sclerotization process of P. westermani eggs. The pH-dependent pattern of monophenol and diphenol oxidase activity further proposes that the initial hydroxylation might slowly but steadily progress in acidic secreted vesicles of vitellocytes and the second oxidation process might be rapidly accelerated by neural or weak alkaline pH environments within the ootype.

scholarly journals Biochemical characterization of a new mitochondrial transporter of dephosphocoenzyme A in Drosophila melanogaster

2017 ◽  
Vol 1858 (2) ◽  
pp. 137-146 ◽  
Author(s):  
Angelo Vozza ◽  
Francesco De Leonardis ◽  
Eleonora Paradies ◽  
Anna De Grassi ◽  
Ciro Leonardo Pierri ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Biochemical Characterization ◽  
Mitochondrial Transporter
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