Isolation and characterization of nuclear ribonucleoprotein complexes from Drosophila melanogaster

1981 ◽  
Vol 7 (1-3) ◽  
pp. 5-13 ◽  
Author(s):  
J. C. Wooley ◽  
R. Cone ◽  
Su-yun Chung
Keyword(s):  
Drosophila Melanogaster ◽  
Ribonucleoprotein Complexes ◽  
Isolation And Characterization ◽  
Nuclear Ribonucleoprotein

scholarly journals Isolation and characterization of the dopa decarboxylase gene of Drosophila melanogaster

1981 ◽  
Vol 1 (6) ◽  
pp. 475-485
Author(s):  
J Hirsh ◽  
N Davidson
Keyword(s):  
Drosophila Melanogaster ◽  
Ribonucleic Acid ◽  
Deoxyribonucleic Acid ◽  
Isolation Procedure ◽  
Chromosome Band ◽  
Dopa Decarboxylase ◽  
Developmental Profile ◽  
Isolation And Characterization

We have isolated chromosomal deoxyribonucleic acid clones containing the Drosophila dopa decarboxylase gene. We describe an isolation procedure which can be applied to other nonabundantly expressed Drosophila genes. The dopa decarboxylase gene lies within or very near polytene chromosome band 37C1-2. The gene is interrupted by at least one intron, and the primary mode of regulation is pretranslational. At least two additional sequences hybridized by in vivo ribonucleic acid-derived probes are found within a 35-kilobase region surrounding the gene. The developmental profile of ribonucleic acid transcribed from one of these regions differs from that of the dopa decarboxylase transcript.

Heterogeneous nuclear ribonucleoprotein complexes and proteins in Drosophila melanogaster

1992 ◽  
Vol 12 (2) ◽  
pp. 847-855
Author(s):  
G Raychaudhuri ◽  
S R Haynes ◽  
A L Beyer
Keyword(s):  
Tissue Culture ◽  
Drosophila Melanogaster ◽  
Rna Sequences ◽  
Heterogeneous Nuclear Ribonucleoprotein ◽  
Culture Cells ◽  
Ribonucleoprotein Complexes ◽  
Tissue Culture Cells ◽  
Hnrnp Proteins ◽  
Nuclear Ribonucleoprotein ◽  
Basic Region

Pre-mRNAs cotranscriptionally associate with a small group of proteins to form heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. We have previously identified two genes in Drosophila melanogaster, Hrb98DE and Hrb87F (i.e., genes at 98DE and 87F encoding putative hnRNA binding proteins), which encode five protein species homologous to the mammalian A-B hnRNP proteins. The studies presented herein show that antibodies against the RNP domains of Hrb98DE reacted with 10 to 15 distinct spots of 38 to 40 kDa in the basic region of two-dimensional gels. These nuclear proteins bound single-stranded nucleic acids and were extracted from Drosophila tissue culture cells as 40 to 80S hnRNP complexes in association with 300 to 800 nucleotide fragments of RNA. The peak of poly(A)+ RNA sequences was coincident with the peak of HRB proteins in sucrose gradients, strongly suggesting that the HRB complexes identified are Drosophila hnRNP complexes. The repertoire of HRB proteins did not change significantly during embryogenesis and was similar to that observed in Drosophila tissue culture cells. Analyses with peptide-specific antisera demonstrated that the major proteins in the hnRNP complex were encoded by the two genes previously identified. Although the Drosophila HRB proteins are only approximately 60% identical throughout the RNP domains to the mammalian A-B hnRNP proteins, features of the basic pre-mRNA packaging mechanism appear to be highly conserved between D. melanogaster and mammals.

Isolation and characterization of a mitochondrial RNA polymerase from Drosophila melanogaster

1987 ◽  
Vol 65 (2) ◽  
pp. 173-182 ◽  
Author(s):  
Michael Goldenthal ◽  
James T. Nishiura
Keyword(s):  
Drosophila Melanogaster ◽  
Rna Polymerase ◽  
Nuclear Dna ◽  
Gradient Centrifugation ◽  
Mitochondrial Rna ◽  
Mitochondrial Rna Polymerase ◽  
Isolation And Characterization ◽  
Cscl Gradient ◽  
Nuclear Rna

A DNA-dependent RNA polymerase was solubilized from sucrose gradient isolated, DNase-treated mitochrondria of Drosophila melanogaster. The isolated mitochondria were not detectably contaminated with nuclear DNA as shown by CsCl gradient centrifugation and polylysine Kieselguhr chromatography. The detergent-solubilized RNA polymerase was sensitive to rifampicin, resistant to α-amanitin, had an apparent molecular mass of about 60 kilodaltons, and displayed a tendency to aggregate, both in crude extracts or when purified. The mitochondrial RNA polymerase could be distinguished from nuclear RNA polymerases on the basis of size, salt optima, rifampicin sensitivity, and α-amanitin resistance.

Isolation and characterization of the Bactrocera oleae genes orthologous to the sex determining Sex-lethal and doublesex genes of Drosophila melanogaster

Gene ◽  
2005 ◽  
Vol 348 ◽  
pp. 111-121 ◽  
Author(s):  
Dimitrios Lagos ◽  
M. Fernanda Ruiz ◽  
Lucas Sánchez ◽  
Katia Komitopoulou
Keyword(s):  
Drosophila Melanogaster ◽  
Bactrocera Oleae ◽  
Isolation And Characterization ◽  
Sex Lethal
Sign in / Sign up

Export Citation Format

Share Document