Evolutionary changes in non-histone chromosomal proteins within the Drosophila melanogaster group revealed by monoclonal antibodies

Chromosoma ◽  
1982 ◽  
Vol 85 (4) ◽  
pp. 531-538 ◽  
Author(s):  
Rainer Kabisch ◽  
J�rg Krause ◽  
Ekkehard K. F. Bautz
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Chromosomal Proteins ◽  
Evolutionary Changes

Monoclonal antibodies against chromosomal proteins of Drosophila melanogaster

Chromosoma ◽  
1980 ◽  
Vol 80 (3) ◽  
pp. 253-275 ◽  
Author(s):  
Harald Saumweber ◽  
Peter Symmons ◽  
Rainer Kabisch ◽  
Hans Will ◽  
F. Bonhoeffer
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Chromosomal Proteins

scholarly journals Characterization of components of Z-bands in the fibrillar flight muscle of Drosophila melanogaster.

1989 ◽  
Vol 109 (5) ◽  
pp. 2157-2167 ◽  
Author(s):  
J D Saide ◽  
S Chin-Bow ◽  
J Hogan-Sheldon ◽  
L Busquets-Turner ◽  
J O Vigoreaux ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Flight Muscle ◽  
Cross Reactivity ◽  
Antigenic Determinants ◽  
Immunogold Staining ◽  
Thick Filaments ◽  
The Matrix ◽  
Flight Muscles

Twelve monoclonal antibodies have been raised against proteins in preparations of Z-disks isolated from Drosophila melanogaster flight muscle. The monoclonal antibodies that recognized Z-band components were identified by immunofluorescence microscopy of flight muscle myofibrils. These antibodies have identified three Z-disk antigens on immunoblots of myofibrillar proteins. Monoclonal antibodies alpha:1-4 recognize a 90-100-kD protein which we identify as alpha-actinin on the basis of cross-reactivity with antibodies raised against honeybee and vertebrate alpha-actinins. Monoclonal antibodies P:1-4 bind to the high molecular mass protein, projectin, a component of connecting filaments that link the ends of thick filaments to the Z-band in insect asynchronous flight muscles. The anti-projectin antibodies also stain synchronous muscle, but, surprisingly, the epitopes here are within the A-bands, not between the A- and Z-bands, as in flight muscle. Monoclonal antibodies Z(210):1-4 recognize a 210-kD protein that has not been previously shown to be a Z-band structural component. A fourth antigen, resolved as a doublet (approximately 400/600 kD) on immunoblots of Drosophila fibrillar proteins, is detected by a cross reacting antibody, Z(400):2, raised against a protein in isolated honeybee Z-disks. On Lowicryl sections of asynchronous flight muscle, indirect immunogold staining has localized alpha-actinin and the 210-kD protein throughout the matrix of the Z-band, projectin between the Z- and A-bands, and the 400/600-kD components at the I-band/Z-band junction. Drosophila alpha-actinin, projectin, and the 400/600-kD components share some antigenic determinants with corresponding honeybee proteins, but no honeybee protein interacts with any of the Z(210) antibodies.

The Short antennae gene of Tribolium is required for limb development and encodes the orthologue of the Drosophila Distal-less protein

Development ◽  
2001 ◽  
Vol 128 (2) ◽  
pp. 287-297 ◽  
Author(s):  
A. Beermann ◽  
D.G. Jay ◽  
R.W. Beeman ◽  
M. Hulskamp ◽  
D. Tautz ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Drosophila Melanogaster ◽  
Genetic Mapping ◽  
Tribolium Castaneum ◽  
Limb Development ◽  
Distal Region ◽  
Distal Limb ◽  
Functional Conservation ◽  
Young Embryo ◽  
Evolutionary Changes

Insects bear a stereotyped set of limbs, or ventral body appendages. In the highly derived dipteran Drosophila melanogaster, the homeodomain transcription factor encoded by the Distal-less (Dll) gene plays a major role in establishing distal limb structures. We have isolated the Dll orthologue (TcDll) from the beetle Tribolium castaneum, which, unlike Drosophila, develops well-formed limbs during embryogenesis. TcDll is initially expressed at the sites of limb primordia formation in the young embryo and subsequently in the distal region of developing legs, antennae and mouthparts except the mandibles. Mutations in the Short antennae (Sa) gene of Tribolium delete distal limb structures, closely resembling the Dll phenotype in Drosophila. TcDll expression is severely reduced or absent in strong Sa alleles. Genetic mapping and molecular analysis of Sa alleles also support the conclusion that TcDll corresponds to the Sa gene. Our data indicate functional conservation of the Dll gene in evolutionarily distant insect species. Implications for evolutionary changes in limb development are discussed.

Interspecific hybridization between Drosophila species group melanogaster sibling species: isozymic patterns and reproductive relationships

Genome ◽  
1989 ◽  
Vol 32 (1) ◽  
pp. 146-154 ◽  
Author(s):  
G. N. Goulielmos ◽  
S. N. Alahiotis
Keyword(s):  
Drosophila Melanogaster ◽  
Sex Ratio ◽  
Interspecific Hybrids ◽  
Aldehyde Oxidase ◽  
Species Group ◽  
Fitness Components ◽  
Phosphogluconate Dehydrogenase ◽  
Evolutionary Changes ◽  
Fertile Hybrids ◽  
Male Genital

In spite of previous consensus that no F1 fertile hybrids (of both sexes) could be produced between any mating combination of Drosophila melanogaster, D. simulans, and D. mauritiana, the present data indicate that such hybrids were obtained. Thus, some crosses between D. mauritiana females and D. simulans or D. melanogaster males yield F1 fertile hybrids (of both sexes) which have been named Masi (or Masi-2 and Masi-3) and Mame, respectively. Electrophoretic studies, using the species-diagnostic genes for 6-phosphogluconate dehydrogenase, alcohol dehydrogenase, and aldehyde oxidase (6-Pgd, Adh, and Aldox, respectively), were used to investigate the hybrid status, taking into consideration (i) their reproductive relationships, (ii) the coexistence of electromorphs from different species in the same hybrid, within the same generation, and (iii) the expression of the above electromorphs in the hybrids as well as in progeny from backcrosses, where unexpected irregularities and abnormalities were observed. These interspecific hybrids have been kept in our laboratory (as stocks) for 50 generations, to date, and have also been tested for various characteristics that contributed to the verification of their hybrid status (mating abilities, enzyme activities, hybrid sex ratio, the morphology of male genital arches and other fitness components). The finding of major genetic phenomena (e.g., allozymic repression) in these hybrid genomes gives some idea of the nature of events that could be associated with strong evolutionary changes, thus controlling speciation processes.Key words: Drosophila, electrophoresis, electromorphs, interspecific hybrids.

scholarly journals Two Drosophila melanogaster proteins related to intermediate filament proteins of vertebrate cells.

1981 ◽  
Vol 91 (1) ◽  
pp. 175-183 ◽  
Author(s):  
F G Falkner ◽  
H Saumweber ◽  
H Biessmann
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Heat Shock ◽  
Indirect Immunofluorescence ◽  
Intermediate Filament ◽  
Cross Reaction ◽  
Cytoplasmic Protein ◽  
Baby Hamster Kidney ◽  
Intermediate Filament Proteins ◽  
Bhk Cells

Monoclonal antibodies were prepared against a 46,000 mol wt major cytoplasmic protein from Drosophila melanogaster Kc cells. These antibodies reacted with the 46,000 and a 40,000 mol wt protein from Kc cells. Some antibodies showed cross-reaction with 55,000 (vimentin) and 52,000 mol wt (desmin) proteins from baby hamster kidney (BHK) cells that form intermediate sized filaments in vertebrate cells. In indirect immunofluorescence, the group of cross reacting antibodies stained a filamentous meshwork in the cytoplasm of vertebrate cells. In Kc cells the fluorescence seemed to be localized in a filamentous meshwork that became more obvious after the cells had flattened out on a surface. These cytoskeletal structures are heat-labile; the proteins in Kc or BHK cells rearrange after a brief heat shock, forming juxtanuclear cap structures.

scholarly journals Expression and localization of Drosophila melanogaster hsp70 cognate proteins.

1986 ◽  
Vol 6 (4) ◽  
pp. 1187-1203 ◽  
Author(s):  
K B Palter ◽  
M Watanabe ◽  
L Stinson ◽  
A P Mahowald ◽  
E A Craig
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Heat Shock ◽  
Developmental Stages ◽  
Antigenic Determinants ◽  
Heat Shock Cognate Protein ◽  
Maximal Induction ◽  
Shock Proteins ◽  
Related Proteins

Monoclonal antibodies have been used to identify three proteins in Drosophila melanogaster that share antigenic determinants with the major heat shock proteins hsp70 and hsp68. While two of the proteins are major proteins at all developmental stages, one heat shock cognate protein, hsc70, is especially enriched in embryos. hsc70 is shown to be the product of a previously identified gene, Hsc4. We have examined the levels of hsp70-related proteins in adult flies and larvae during heat shock and recovery. At maximal induction in vivo, hsp70 and hsp68 never reach the basal levels of the major heat shock cognate proteins. Monoclonal antibodies to hsc70 have been used to localize it to a meshwork of cytoplasmic fibers that are heavily concentrated around the nucleus.

scholarly journals Monoclonal antibodies to a phosphoprotein from chromatin of rat liver

1985 ◽  
Vol 225 (2) ◽  
pp. 357-363 ◽  
Author(s):  
M J Halikowski ◽  
C C Liew
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Bovine Serum Albumin ◽  
Rat Liver ◽  
High Specificity ◽  
Cross Reactivity ◽  
Dot Blot ◽  
Chromosomal Proteins ◽  
Rat Liver Nuclei ◽  
Liver Nuclei

Three monoclonal antibody subclasses (IgG1, IgG2a, and IgM) were raised to the phosphoprotein B2 (Mr 68000, pI6.5-8.2) which has been shown previously to be associated with the nucleosomes of rat liver nuclei. These antibodies do not show any significant cross reactivity with CM-cellulose ‘unbound’ non-histone chromosomal proteins, bovine serum albumin or histones. Further verification of the specificity of these antibodies to this phosphoprotein was carried out using both ‘dot’ blot and immunological transfer analysis (‘Western blot‘). The monoclonal antibodies (IgG1 and IgG2a) could also be used to semi-quantify the phosphoprotein B2 in rat liver nuclei. The high specificity and unlimited availability of this type of probe provides a means to study the role(s) of this phosphoprotein in the overall scheme of actively transcribed chromatin.

Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene

1986 ◽  
Vol 6 (11) ◽  
pp. 3862-3872
Author(s):  
T C James ◽  
S C Elgin
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Fusion Protein ◽  
Cdna Clone ◽  
Nuclear Protein ◽  
Cdna Expression Library ◽  
General Strategy ◽  
Chromosomal Protein ◽  
Western Blots ◽  
Single Chromosome

Monoclonal antibodies were prepared against a fraction of nuclear proteins of Drosophila melanogaster identified as tightly binding to DNA. Four of these antibodies were directed against a 19-kilodalton nuclear protein; immunofluorescence staining of the polytene chromosomes localized the antigen to the alpha, beta, and intercalary heterochromatic regions. Screening of a lambda gt11 cDNA expression library with one of the monoclonal antibodies identified a recombinant DNA phage clone that produced a fusion protein immunologically similar to the heterochromatin-associated protein. Polyclonal sera directed against the bacterial lacZ fusion protein recognized the same nuclear protein on Western blots. A full-length cDNA clone was isolated from a lambda gt10 library, and its DNA sequence was obtained. Analysis of the open reading frame revealed an 18,101-dalton protein encoded by this cDNA. Two overlapping genomic DNA clones were isolated from a Charon 4 library of D. melanogaster with the cDNA clone, and a restriction map was obtained. In situ hybridization with these probes indicated that the gene maps to a single chromosome location at 29A on the 2L chromosome. This general strategy should be effective for cloning the genes and identifying the genetic loci of chromosomal proteins which cannot be readily assayed by other means.

Expression and localization of Drosophila melanogaster hsp70 cognate proteins

1986 ◽  
Vol 6 (4) ◽  
pp. 1187-1203
Author(s):  
K B Palter ◽  
M Watanabe ◽  
L Stinson ◽  
A P Mahowald ◽  
E A Craig
Keyword(s):  
Drosophila Melanogaster ◽  
Monoclonal Antibodies ◽  
Heat Shock ◽  
Developmental Stages ◽  
Antigenic Determinants ◽  
Heat Shock Cognate Protein ◽  
Maximal Induction ◽  
Shock Proteins ◽  
Related Proteins

Monoclonal antibodies have been used to identify three proteins in Drosophila melanogaster that share antigenic determinants with the major heat shock proteins hsp70 and hsp68. While two of the proteins are major proteins at all developmental stages, one heat shock cognate protein, hsc70, is especially enriched in embryos. hsc70 is shown to be the product of a previously identified gene, Hsc4. We have examined the levels of hsp70-related proteins in adult flies and larvae during heat shock and recovery. At maximal induction in vivo, hsp70 and hsp68 never reach the basal levels of the major heat shock cognate proteins. Monoclonal antibodies to hsc70 have been used to localize it to a meshwork of cytoplasmic fibers that are heavily concentrated around the nucleus.

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