A deletion of the 3' end of the Drosophila melanogaster hsp70 gene increases stability of mutant mRNA during recovery from heat shock

1985 ◽  
Vol 5 (12) ◽  
pp. 3397-3402
Author(s):  
A A Simcox ◽  
C M Cheney ◽  
E P Hoffman ◽  
A Shearn
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Gene ◽  
Hsp70 Mrna ◽  
X Ray ◽  
Culture Cells ◽  
Hsp70 Protein ◽  
Tissue Culture Cells ◽  
High Level ◽  
Hsp40 Protein

hsp40, an X-ray-induced deletion mutant of the major Drosophila melanogaster heat shock protein gene hsp70, was shown to be incorrectly regulated at the translational level. hsp40 protein synthesis persisted at a high level after the release from heat shock, whereas hsp70 protein production was rapidly repressed. This result was observed both in flies heterozygous for the hsp40 gene and in tissue culture cells transfected with the truncated gene. Analysis of the transcription of the hsp40 gene indicated that its mRNA, unlike hsp70 mRNA, was not actively destabilized after a return to control temperatures, permitting prolonged production of the mutant protein.

scholarly journals A deletion of the 3' end of the Drosophila melanogaster hsp70 gene increases stability of mutant mRNA during recovery from heat shock.

1985 ◽  
Vol 5 (12) ◽  
pp. 3397-3402 ◽  
Author(s):  
A A Simcox ◽  
C M Cheney ◽  
E P Hoffman ◽  
A Shearn
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protein Gene ◽  
Hsp70 Mrna ◽  
X Ray ◽  
Culture Cells ◽  
Hsp70 Protein ◽  
Tissue Culture Cells ◽  
High Level ◽  
Hsp40 Protein

hsp40, an X-ray-induced deletion mutant of the major Drosophila melanogaster heat shock protein gene hsp70, was shown to be incorrectly regulated at the translational level. hsp40 protein synthesis persisted at a high level after the release from heat shock, whereas hsp70 protein production was rapidly repressed. This result was observed both in flies heterozygous for the hsp40 gene and in tissue culture cells transfected with the truncated gene. Analysis of the transcription of the hsp40 gene indicated that its mRNA, unlike hsp70 mRNA, was not actively destabilized after a return to control temperatures, permitting prolonged production of the mutant protein.

scholarly journals Effect of heat shock on ribosome synthesis in Drosophila melanogaster.

1988 ◽  
Vol 8 (1) ◽  
pp. 91-95 ◽  
Author(s):  
J Bell ◽  
L Neilson ◽  
M Pellegrini
Keyword(s):  
Tissue Culture ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Ribosomal Protein Synthesis ◽  
Correct Processing

In Drosophila tissue culture cells, the synthesis of ribosomal proteins was inhibited by a 1-h 37 degrees C heat shock. Ribosomal protein synthesis was repressed to a greater extent than that of most other proteins synthesized by these cells at 25 degrees C. After a 1-h heat shock, when the cells were returned to 25 degrees C, the ribosomal proteins were much slower than most other 25 degrees C proteins to return to pre-heat shock levels of synthesis. Relative to one another, all the ribosomal proteins were inhibited and later recovered to normal levels of synthesis at the same rate and to the same extent. Unlike the ribosomal proteins, the precursor to the large rRNAs was continually synthesized during heat shock, although at a slightly reduced level, but was not processed. It was rapidly degraded, with a half-life of approximately 16 min. Pre-heat shock levels of synthesis, stability, and correct processing were restored only when ribosomal protein synthesis returned to at least 50% of that seen in non-heat-shocked cells.

A DNA damage-responsive Drosophila melanogaster gene is also induced by heat shock

1986 ◽  
Vol 6 (12) ◽  
pp. 4767-4769
Author(s):  
A A Vivino ◽  
M D Smith ◽  
K W Minton
Keyword(s):  
Dna Damage ◽  
Tissue Culture ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Uv Irradiation ◽  
Transcriptional Level ◽  
Restriction Map ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Heat Shock Induction

A gene isolated by screening Drosophila melanogaster tissue culture cells for DNA damage regulation was also found to be regulated by heat shock. After UV irradiation or heat shock, induction is at the transcriptional level and results in the accumulation of a 1.0-kilobase polyadenylated transcript. The restriction map of the clone bears no resemblance to the known heat shock genes, which are shown to be uninduced by UV irradiation.

Effect of heat shock on ribosome synthesis in Drosophila melanogaster

1988 ◽  
Vol 8 (1) ◽  
pp. 91-95
Author(s):  
J Bell ◽  
L Neilson ◽  
M Pellegrini
Keyword(s):  
Tissue Culture ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Ribosomal Protein Synthesis ◽  
Correct Processing

In Drosophila tissue culture cells, the synthesis of ribosomal proteins was inhibited by a 1-h 37 degrees C heat shock. Ribosomal protein synthesis was repressed to a greater extent than that of most other proteins synthesized by these cells at 25 degrees C. After a 1-h heat shock, when the cells were returned to 25 degrees C, the ribosomal proteins were much slower than most other 25 degrees C proteins to return to pre-heat shock levels of synthesis. Relative to one another, all the ribosomal proteins were inhibited and later recovered to normal levels of synthesis at the same rate and to the same extent. Unlike the ribosomal proteins, the precursor to the large rRNAs was continually synthesized during heat shock, although at a slightly reduced level, but was not processed. It was rapidly degraded, with a half-life of approximately 16 min. Pre-heat shock levels of synthesis, stability, and correct processing were restored only when ribosomal protein synthesis returned to at least 50% of that seen in non-heat-shocked cells.

scholarly journals A DNA damage-responsive Drosophila melanogaster gene is also induced by heat shock.

1986 ◽  
Vol 6 (12) ◽  
pp. 4767-4769 ◽  
Author(s):  
A A Vivino ◽  
M D Smith ◽  
K W Minton
Keyword(s):  
Dna Damage ◽  
Tissue Culture ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Uv Irradiation ◽  
Transcriptional Level ◽  
Restriction Map ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Heat Shock Induction

A gene isolated by screening Drosophila melanogaster tissue culture cells for DNA damage regulation was also found to be regulated by heat shock. After UV irradiation or heat shock, induction is at the transcriptional level and results in the accumulation of a 1.0-kilobase polyadenylated transcript. The restriction map of the clone bears no resemblance to the known heat shock genes, which are shown to be uninduced by UV irradiation.

scholarly journals DNA replication of histone gene repeats in Drosophila melanogaster tissue culture cells: multiple initiation sites and replication pause sites.

1993 ◽  
Vol 13 (7) ◽  
pp. 4098-4106 ◽  
Author(s):  
T Shinomiya ◽  
S Ina
Keyword(s):  
Tissue Culture ◽  
Drosophila Melanogaster ◽  
Dna Replication ◽  
Present Report ◽  
Polymerase Chain Reaction Method ◽  
Mapping Method ◽  
Histone Gene ◽  
Culture Cells ◽  
Tissue Culture Cells ◽  
Replication Intermediates

We showed previously that DNA replication initiates at multiple sites in the 5-kb histone gene repeating unit in early embryos of Drosophila melanogaster. The present report shows evidence that replication in the same chromosomal region initiates at multiple sites in tissue culture cells as well. First, we analyzed replication intermediates by the two-dimensional gel electrophoretic replicon mapping method and detected bubble-form replication intermediates for all fragments restricted at different sites in the repeating unit. Second, we analyzed bromodeoxyuridine-labeled nascent strands amplified by the polymerase chain reaction method and detected little differences in the size distribution of nascent strands specific to six short segments located at different sites in the repeating unit. These results strongly suggest that DNA replication initiates at multiple sites located within the repeating unit. We also found several replication pause sites located at 5' upstream regions of some histone genes.

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