Theadenosine2 locus ofDrosophila melanogaster: Clarification of the map position and eye phenotype of theade2 1 mutant

Keizer, C.; Nash, David R.; Tiong, Stanley

doi:10.1007/bf00554169

Cited by 4 publications

(2 citation statements)

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“…To better ascertain the sequence structure of bw D , first we precisely mapped the mutation. bw D was originally reported to be an insertion ( Hinton and Goodsmith, 1950 ; Slatis, 1955 ), and was later localized to within the coding region of the brown gene ( Dreesen et al, 1988 ), which maps to the polytene band 59E1-2 or the interband just distal ( Keizer et al, 1989 ). This mapping of the insertion to 59E1-2 is consistent with the appearance of a dense wedge-shaped region fused to 59E1-2 in bw D / + heterozygotes (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In a recent cytological study of bw D , the insertion was seen to lie just distal of the 59E1-2 band under conditions that reduce heterochromatin condensation ( Belyaeva et al, 1997 ). The brown gene had been previously mapped to the distal edge of the 59E1-2 band or the adjacent interband ( Keizer et al, 1989 ). These cytological observations are consistent with our FISH mapping and sequencing of the junctions, which suggest that bw D is a simple insertion into the brown coding region.…”

Section: Discussionmentioning

confidence: 99%

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Changes in Chromosomal Localization of Heterochromatin-binding Proteins during the Cell Cycle in Drosophila

Platero

Csink

Quintanilla

et al. 1998

The Journal of Cell Biology

142

131

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We examined the heterochromatic binding of GAGA factor and proliferation disrupter (Prod) proteins during the cell cycle in Drosophila melanogaster and sibling species. GAGA factor binding to the brownD ominant AG-rich satellite sequence insertion was seen at metaphase, however, no binding of GAGA factor to AG-rich sequences was observed at interphase in polytene or diploid nuclei. Comparable mitosis-specific binding was found for Prod protein to its target satellite in pericentric heterochromatin. At interphase, these proteins bind numerous dispersed sites in euchromatin, indicating that they move from euchromatin to heterochromatin and back every cell cycle. The presence of Prod in heterochromatin for a longer portion of the cell cycle than GAGA factor suggests that they cycle between euchromatin and heterochromatin independently. We propose that movement of GAGA factor and Prod from high affinity sites in euchromatin occurs upon condensation of metaphase chromosomes. Upon decondensation, GAGA factor and Prod shift from low affinity sites within satellite DNA back to euchromatic sites as a self-assembly process.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Changes in Chromosomal Localization of Heterochromatin-binding Proteins during the Cell Cycle in Drosophila

Platero

Csink

Quintanilla

et al. 1998

The Journal of Cell Biology

142

131

View full text Add to dashboard Cite

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Drosophila purine auxotrophy: New alleles ofadenosine2 exhibiting a complex visible phenotype

et al. 1989

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New mutant alleles of the adenosine2 locus (ade2; 2-17.7) have been isolated using the eye-color phenotype exhibited by the prototype auxotrophic allele ade2 as the screening criterion. The new mutants form a single complementation group, suggesting that they all exhibit purine auxotrophy and defective formylglycineamide ribotide amidotransferase enzyme, like ade2. Tests carried out on particular new alleles confirm these suggestions. The new mutants all exhibit more extreme physical defects than the prototype. They have wing abnormalities like mutants defective in pyrmidine biosynthesis and reduced bristles like those defective in protein synthesis; thus they exhibit the combined visible phenotype of rudimentary wings, rosy eyes, and bobbed bristles. Cytogenetic analysis places the locus in the interband proximal to 26B1-2.

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Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis.

Clark¹

1994

Genetics

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The Drosophila Prat gene encodes phosphoribosylamidotransferase (PRAT), the enzyme that performs the first committed step of the de novo purine nucleotide biosynthesis pathway. Using information from amino acid sequence alignments of PRAT from other organisms, a polymerase chain reaction-based approach was employed to clone Prat. Amino acid sequence alignment of Drosophila PRAT with PRAT from bacteria, yeast, and vertebrates indicates that it is most identical (at least 60%) to the vertebrate PRATs. It shares putative amino-terminal propeptide and iron-binding domains seen only in Bacillus subtilis and vertebrate PRATs. Prat was localized to the right arm of chromosome 3 at polytene band 84E1-2. Owing to the fact that this region had been well characterized previously, Prat was localized to a 30-kilobase region between two deficiency breakpoints. By making the prediction that Prat would have a similar "purine syndrome" phenotype as mutations in the genes ade2 and ade3, which encode enzymes downstream in the pathway, five alleles of Prat were isolated. Three of the alleles were identified as missense mutations. A comparison of PRAT enzyme activity with phenotype in three of the mutants indicates that a reduction to 40% of the wild-type allele's activity is sufficient to cause the purine syndrome, suggesting that PRAT activity is limiting in Drosophila.

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Theadenosine2 locus ofDrosophila melanogaster: Clarification of the map position and eye phenotype of theade2 1 mutant

Cited by 4 publications

References 4 publications

Changes in Chromosomal Localization of Heterochromatin-binding Proteins during the Cell Cycle in Drosophila

Changes in Chromosomal Localization of Heterochromatin-binding Proteins during the Cell Cycle in Drosophila

Drosophila purine auxotrophy: New alleles ofadenosine2 exhibiting a complex visible phenotype

Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis.

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