The ommochrome biosynthetic pathway in Drosophila melanogaster: The head particulate phenoxazinone synthase and the developmental onset of xanthommatin synthesis

1976 ◽  
Vol 14 (11-12) ◽  
pp. 1077-1090 ◽  
Author(s):  
M. Yamamoto ◽  
A. J. Howells ◽  
Rosemary L. Ryall
Keyword(s):  
Drosophila Melanogaster ◽  
Biosynthetic Pathway ◽  
Phenoxazinone Synthase ◽  
Xanthommatin Synthesis

scholarly journals relA Is Required for Actinomycin Production in Streptomyces antibioticus

1999 ◽  
Vol 181 (12) ◽  
pp. 3824-3829 ◽  
Author(s):  
Shannan Hoyt ◽  
George H. Jones
Keyword(s):  
Biosynthetic Pathway ◽  
Wild Type Strain ◽  
Streptomyces Coelicolor ◽  
Production Medium ◽  
Wild Type ◽  
Streptomyces Antibioticus ◽  
Phenoxazinone Synthase ◽  
Key Enzyme ◽  
In The Wild ◽  
Phosphate Medium

ABSTRACT The relA gene from Streptomyces antibioticus has been cloned and sequenced. The gene encodes a protein with an M r of 93,653, which is 91% identical to the corresponding protein from Streptomyces coelicolor. Disruption of S. antibioticus relAproduces a strain which grows significantly more slowly on actinomycin production medium than the wild type or a disruptant to which the intact relA gene was restored. Moreover, the disruptant was unable to accumulate ppGpp to the levels observed during the normal course of growth and actinomycin production in the wild type. The strain containing the disrupted relA gene did not produce actinomycin and contained significantly lower levels of the enzyme phenoxazinone synthase than the wild-type strain. Actinomycin synthetase I, a key enzyme in the actinomycin biosynthetic pathway, was undetectable in the relA disruptant. Growth of the disruptant on low-phosphate medium did not restore actinomycin production.

scholarly journals TERMINAL SYNTHESIS OF XANTHOMMATIN IN DROSOPHILA MELANOGASTER. III. MUTATIONAL PLEIOTROPY AND PIGMENT GRANULE ASSOCIATION OF PHENOXAZINONE SYNTHETASE

Genetics ◽  
1973 ◽  
Vol 73 (1) ◽  
pp. 45-56
Author(s):  
John P Phillips ◽  
Hugh S Forrest ◽  
Anil D Kulkarni
Keyword(s):  
Drosophila Melanogaster ◽  
Pigment Granule ◽  
Synthetase Activity ◽  
Type I ◽  
Developmental Control ◽  
Eye Color ◽  
Xanthommatin Synthesis ◽  
Eye Color Mutants ◽  
Low Levels

ABSTRACT Phenoxazinone synthetase, which catalyzes the condensation of 3-hydroxykynurenine to xanthommatin, the brown eye pigment of Drosophila, is shown to exist in association with a particle which resembles the cytologically defined Type I pigment granule. Several classical eye color mutants (v, cn, st, ltd, cd, w), including two which effect other enzymes in the xanthommatin pathway (v, cn), have low levels of phenoxazinone synthetase activity and disrupt the normal association of the enzyme with the pigment granule. A model is proposed depicting several structural and enzymatic interrelationships involved in the developmental control of xanthommatin synthesis in Drosophila.

scholarly journals Cloning and molecular characterization of a metabolic gene with development functions in Drosophila. I. Analysis of the head function of Punch.

Genetics ◽  
1990 ◽  
Vol 126 (4) ◽  
pp. 1007-1019
Author(s):  
J R McLean ◽  
R Boswell ◽  
J O'Donnell
Keyword(s):  
Drosophila Melanogaster ◽  
Young Adult ◽  
Biosynthetic Pathway ◽  
In Vitro Translation ◽  
Initial Examination ◽  
Vital Functions ◽  
Eye Pigmentation ◽  
Adult Head

Abstract In an effort to understand the functions of pterins throughout development we have been studying Punch (Pu), the structural gene for the enzyme GTP cyclohydrolase in Drosophila melanogaster. This enzyme catalyzes the first step in the pterin biosynthetic pathway. The Pu gene product is required for vital functions at two distinct stages in embryogenesis, and a pigmentation function in the eye of the young adult. We have localized the Pu region to 29 kb of DNA through the analysis of lesions present in Pu mutants. Since all of the mutations that were mapped affect the eye pigmentation function of Pu, and since this function is the best defined biochemically, we have concentrated on identifying and characterizing Pu products required for eye pigmentation in our initial examination of the cloned region. Four different transcripts from this region are expressed in the adult head. We show that one of these transcripts, the 1.7-kb species, is responsible for the pigmentation function through the analysis of mutant transcripts and the use of an in vitro translation assay. A 2-kb region lying within the locus is specifically required for this eye pigmentation function.

scholarly journals CHARACTERIZATION OF AN AUTOSOMAL RUDIMENTARY-SHAPED WING MUTATION IN DROSOPHILA MELANOGASTER THAT AFFECTS PYRIMIDINE SYNTHESIS

Genetics ◽  
1980 ◽  
Vol 96 (2) ◽  
pp. 471-478
Author(s):  
Donna M Lastowski ◽  
D R Falk
Keyword(s):  
Drosophila Melanogaster ◽  
Biosynthetic Pathway ◽  
Wild Type ◽  
Aspartate Transcarbamylase ◽  
Ems Mutagenesis ◽  
Carbamyl Phosphate Synthetase ◽  
Pyrimidine Synthesis ◽  
Complex Locus ◽  
The Right

ABSTRACT A new autosomal mutation, rudimental (ral), which causes rudimentary-shaped wings in Drosophila melanogaster, has been isolated following ethyl methanesulfonate (EMS) mutagenesis. The wing phenotype of rudimental is identical to that of the X-linked rudimentary (r) mutation, which affects the first three enzymes in the pyrimidine biosynthetic pathway. The autosomal mutant maps very close to ebony (3—70.7) at 70.42 on the right arm of chromosome 3. Analysis of the enzyme activities of orotate phosphoribosyltransferase (OPRTase) and orotidylate decarboxylase (ODCase) indicates that the rala26a allele has less than wild-type activity for both enzymes. This result is discussed in light of the fact that the OPRTase and ODCase activities are part of an enzyme complex, as are the carbamyl phosphate synthetase (CPSase), aspartate transcarbamylase (ATCase) and dihydroorotase (DHOase) activities, which are encoded by the complex rudimentary locus. We suggest that rudimental is also a complex locus.

Purification, crystallization and preliminary X-ray analysis of Drosophila melanogaster ferrochelatase

1999 ◽  
Vol 55 (6) ◽  
pp. 1201-1203 ◽  
Author(s):  
Kai-Fen Wang ◽  
Chia-Kuei Wu ◽  
Vera M. Sellers ◽  
John P. Rose ◽  
Bi-Cheng Wang ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Biosynthetic Pathway ◽  
Protoporphyrin Ix ◽  
Asymmetric Unit ◽  
Inner Mitochondrial Membrane ◽  
X Ray ◽  
Amino Terminal ◽  
Highly Sensitive ◽  
Cell Dimensions ◽  
Unit Cell Dimensions

Ferrochelatase (protoheme ferrolyase, E.C. 4.99.1.1), the terminal enzyme in the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme. In eukaryotes, the protein is associated with the inner surface of the inner mitochondrial membrane, and in higher animals the enzyme contains a [2Fe–2S] cluster. This cluster is highly sensitive to NO and is coordinated by four Cys residues whose spacing in the primary sequence is unique. Ferrochelatase from Drosophila melanogaster has been expressed in Escherichia coli with an amino-terminal six-histidine tag and purified to homogeneity. The protein has been crystallized with the [2Fe–2S] cluster intact. The crystals belong to space group I422, with unit-cell dimensions a = b = 158.1, c = 171.2 Å and two molecules in the asymmetric unit, and diffract to 3.0 Å resolution.

scholarly journals ORGANIZATION OF THE RUDIMENTARY WING LOCUS IN DROSOPHILA MELANOGASTER. I. THE ISOLATION AND PARTIAL CHARACTERIZATION OF MUTANTS INDUCED WITH ETHYL METHANESULFONATE, ICR–170 AND X RAYS

Genetics ◽  
1979 ◽  
Vol 93 (1) ◽  
pp. 143-161
Author(s):  
John M Rawls ◽  
Lawrence A Porter
Keyword(s):  
Drosophila Melanogaster ◽  
Biosynthetic Pathway ◽  
De Novo ◽  
Ethyl Methanesulfonate ◽  
Genetic Complementation ◽  
Partial Characterization ◽  
Enzyme Assays ◽  
Enzyme Complex ◽  
X Rays

ABSTRACT New rudimentary (r) mutants have been isolated following mutagenesis with ethyl methanesulfonate (rLE), ICR-170 (rLI) and X rays (rLX) . From wing phenotype measurements on hamoallelic females, it has been shown that the rLE mutant series includes several leaky alleles, as well as alleles that produce moderate and strong r phenotypes. All of the tested rLI alleles yielded strong r phenotypes in homoallelic females, whereas the rLX series was found to include both moderate and strong alleles. Based on allele complementation for the wing phenotype, it was found that all three mutant series include both complementing and noncomplementing alleles, but the relative frequencies of these two types of alleles differ considerably among the three series. Complementing alleles comprise most of the rLE mutant series (19 of 25) and almost one-half of the rLX series (five of 12), while only one of 16 rLI mutants is a complementing allele. Data from enzyme assays of mutants mostly support the direct correlation of genetic complementation units with the activities of the first three enzymes in the de novo pyrimidine biosynthetic pathway. All of these findings are discussed in light of evidence that these three enzymes are contained within a tri-enzyme complex in animals. We conclude that the available genetic evidence supports the contention that the trienzyme complex is encoded by a single mRNA.

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