The activity of two heat shock loci of Drosophila hydei in tissue culture cells and salivary gland cells as analyzed by in situ hybridization of complementary DNA

Chromosoma ◽  
1979 ◽  
Vol 72 (3) ◽  
pp. 281-291 ◽  
Author(s):  
P. J. A. Sondermeijer ◽  
N. H. Lubsen
1988 ◽  
Vol 8 (5) ◽  
pp. 1877-1886
Author(s):  
B M Benton ◽  
S Berrios ◽  
P A Fisher

A 75-kilodalton polypeptide has been identified which copurifies with karyoskeletal protein-enriched fractions prepared from Drosophila melanogaster embryos. Results of indirect immunofluorescence experiments suggest that this protein, here designated p75, is primarily associated with puffed regions of larval salivary gland polytene chromosomes. In nonpolytenized Schneider 2 tissue culture cells, p75 appeared to be localized throughout the nuclear interior during interphase. In mitotic cells, p75 was redistributed diffusely. A possible role for karyoskeletal elements in transcriptional regulation is discussed.


1988 ◽  
Vol 8 (1) ◽  
pp. 91-95 ◽  
Author(s):  
J Bell ◽  
L Neilson ◽  
M Pellegrini

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.


1986 ◽  
Vol 6 (12) ◽  
pp. 4767-4769
Author(s):  
A A Vivino ◽  
M D Smith ◽  
K W Minton

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.


Microbiology ◽  
1983 ◽  
Vol 129 (11) ◽  
pp. 3379-3384
Author(s):  
H. Takayama ◽  
T. Katsumoto ◽  
K. Ohno ◽  
A. Nakaso ◽  
A. Takagi ◽  
...  

2007 ◽  
Vol 2 (5) ◽  
pp. 1180-1184 ◽  
Author(s):  
T D Allen ◽  
S A Rutherford ◽  
S Murray ◽  
F Gardiner ◽  
E Kiseleva ◽  
...  

1988 ◽  
Vol 8 (5) ◽  
pp. 1877-1886 ◽  
Author(s):  
B M Benton ◽  
S Berrios ◽  
P A Fisher

A 75-kilodalton polypeptide has been identified which copurifies with karyoskeletal protein-enriched fractions prepared from Drosophila melanogaster embryos. Results of indirect immunofluorescence experiments suggest that this protein, here designated p75, is primarily associated with puffed regions of larval salivary gland polytene chromosomes. In nonpolytenized Schneider 2 tissue culture cells, p75 appeared to be localized throughout the nuclear interior during interphase. In mitotic cells, p75 was redistributed diffusely. A possible role for karyoskeletal elements in transcriptional regulation is discussed.


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