Surface structure of the compound eye of various Drosophila species and eye mutants of Drosophila melanogaster

1974 ◽  
Vol 44 (6) ◽  
pp. 262-265 ◽  
Author(s):  
Bertha F. A. Stumm-Tegethoff ◽  
A. W. Dicke
Keyword(s):  
Drosophila Melanogaster ◽  
Surface Structure ◽  
Compound Eye ◽  
Drosophila Species

Encapsulation ability: Are all Drosophila species equally armed? An investigation in the obscura group

2009 ◽  
Vol 87 (7) ◽  
pp. 635-641 ◽  
Author(s):  
S. Havard ◽  
P. Eslin ◽  
G. Prévost ◽  
G. Doury
Keyword(s):  
Drosophila Melanogaster ◽  
Related Species ◽  
Unusual Case ◽  
Foreign Bodies ◽  
Drosophila Subobscura ◽  
Drosophila Species ◽  
Drosophila Persimilis ◽  
Obscura Group ◽  
Encapsulation Ability

Unable to form cellular capsules around large foreign bodies, the species Drosophila subobscura Collin in Gordon, 1936 was previously shown devoid of lamellocytes, the capsule-forming hemocytes in Drosophila melanogaster Meigen, 1830. This unusual case of deficiency in encapsulation ability was remarkable enough to motivate further investigations in phylogenetically related species of the obscura group. Like D. subobscura, the species Drosophila azteca Sturtevant and Dobzhansky, 1936, Drosophila bifasciata Pomini, 1940, Drosophila guanche Monclus, 1976, Drosophila miranda Dobzhansky, 1935, Drosophila persimilis Dobzhansky and Epling, 1944, and Drosophila pseudoobcura Frovola and Astaurov, 1929 were found to be unable to encapsulate large foreign bodies and also to lack lamellocytes. Surprisingly, Drosophila affinis Sturtevant, 1916, Drosophila tolteca Patterson and Mainland, 1944, and Drosophila obscura Fallen, 1823 were capable of mounting cellular capsules, although their encapsulation abilities remained weak. These three species were free of lamellocytes but possessed small pools of never before described “atypical hemocytes” present in the hemolymph when capsules were formed.

The transmembrane protein, Tincar, is involved in the development of the compound eye in Drosophila melanogaster

2005 ◽  
Vol 215 (2) ◽  
pp. 90-96 ◽  
Author(s):  
Yuki Hirota ◽  
Kazunobu Sawamoto ◽  
Kuniaki Takahashi ◽  
Ryu Ueda ◽  
Hideyuki Okano
Keyword(s):  
Drosophila Melanogaster ◽  
Compound Eye ◽  
Transmembrane Protein

S elements: a family of Tc1-like transposons in the genome of Drosophila melanogaster.

Genetics ◽  
1995 ◽  
Vol 141 (4) ◽  
pp. 1425-1438 ◽  
Author(s):  
P J Merriman ◽  
C D Grimes ◽  
J Ambroziak ◽  
D A Hackett ◽  
P Skinner ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Transposable Elements ◽  
Sibling Species ◽  
Inverted Repeat ◽  
Open Reading Frame ◽  
Drosophila Species ◽  
Insertion Mutation ◽  
Reading Frame ◽  
Diploid Genome

Abstract The S elements form a diverse family of long-inverted-repeat transposons within the genome of Drosophila melanogaster. These elements vary in size and sequence, the longest consisting of 1736 bp with 234-bp inverted terminal repeats. The longest open reading frame in an intact S element could encode a 345-amino acid polypeptide. This polypeptide is homologous to the transposases of the mariner-Tc1 superfamily of transposable elements. S elements are ubiquitous in D. melanogaster populations and also appear to be present in the genomes of two sibling species; however, they seem to be absent from 17 other Drosophila species that were examined. Within D. melanogaster strains, there are, on average, 37.4 cytologically detectable S elements per diploid genome. These elements are scattered throughout the chromosomes, but several sites in both the euchromatin and beta heterochromatin are consistently occupied. The discovery of an S-element-insertion mutation and a reversion of this mutation indicates that S elements are at least occasionally mobile in the D. melanogaster genome. These elements seem to insert at an AT dinucleotide within a short palindrome and apparently duplicate that dinucleotide upon insertion.

A concave microwell array fabricated using the ommatidium of the common fruit fly for efficient cell culture

RSC Advances ◽  
2016 ◽  
Vol 6 (69) ◽  
pp. 64266-64270 ◽  
Author(s):  
Bhupendra Shravage ◽  
Shefali Ramteke ◽  
Prasad Kulkarni ◽  
Dhananjay Bodas
Keyword(s):  
Cell Culture ◽  
Drosophila Melanogaster ◽  
Compound Eye ◽  
Fruit Fly ◽  
Microwell Array ◽  
The Common ◽  
Bottom Left ◽  
Mcf 7

Top left: SEM of compound eye of Drosophila melanogaster replica in PDMS. Bottom left: SEM of MCF-7 cell grown in the micro well. Bottom right: confocal of the MCF-7 cells grown for 72 h.

scholarly journals The unexpected recovery of hybrids in a Drosophila species cross: a genetic analysis

1996 ◽  
Vol 67 (1) ◽  
pp. 11-18 ◽  
Author(s):  
H. Allen Orr
Keyword(s):  
Drosophila Melanogaster ◽  
Genetic Analysis ◽  
Drosophila Species ◽  
Male Progeny ◽  
Embryonic Lethal ◽  
The Difference ◽  
Species Cross

SummaryThe species cross between Drosophila melanogaster and D. simulans was first described by Sturtevant in the 1920s. According to his description, the hybridization of D. simulans females and D. melanogaster males produces only (or almost only) male progeny. Female hybrids are embryonic lethal. Here it is shown that these traditional results no longer hold. Instead, D. simulans is polymorphic for factor(s) that qualitatively affect the outcome of species crosses to D. melanogaster. Remarkably, many, if not most, strains of D. simulans produce abundant female hybrids when crossed to D. melanogaster males. Genetic analysis of the difference between D. simulans strains that produce many versus few hybrid females shows that recovery of hybrid females depends on autosomal, maternally acting gene(s).

scholarly journals The brown protein of Drosophila melanogaster is similar to the white protein and to components of active transport complexes.

1988 ◽  
Vol 8 (12) ◽  
pp. 5206-5215 ◽  
Author(s):  
T D Dreesen ◽  
D H Johnson ◽  
S Henikoff
Keyword(s):  
Drosophila Melanogaster ◽  
Active Transport ◽  
Compound Eye ◽  
Structural Similarity ◽  
Genomic Region ◽  
White Gene ◽  
Nucleotide Sequencing ◽  
Terminal Portion ◽  
Membrane Components ◽  
Sequence Similarities

The brown gene of Drosophila melanogaster is required for deposition of pteridine pigments in the compound eye and other tissues. We isolated a ca. 150-kilobase region including brown by microdissection and chromosome walking using cosmids. Among the cDNAs identified by hybridization to the cosmids, one class hybridized to a genomic region that is interrupted in two brown mutants, bw and In(2LR)CK, and to 2.8- and 3.0-kilobase poly(A)+ RNAs which are altered in the mutants. Nucleotide sequencing of these cDNAs revealed that the two transcripts differ as a consequence of alternative poly(A) addition and that both encode the same predicted protein of 675 amino acids. Searches of available databases for amino acid sequence similarities detected a striking overall similarity of this predicted protein to that of the D. melanogaster white gene. The N-terminal portion aligned with the HisP family of membrane-associated ATP-binding proteins, most of which are subunits of active transport complexes in bacteria, and to two regions of the multidrug resistance P-glycoprotein. The C-terminal portion showed a structural similarity to integral membrane components of the same complexes. Taken together with earlier biochemical evidence that brown and white gene products are necessary for uptake of a pteridine precursor and genetic evidence that brown and white proteins interact, our results are consistent with suggestions that these proteins are subunits of a pteridine precursor permease.

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