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Transcription, export and turnover ofHsp70and αβ twoDrosophilaheat shock genes sharing a 400 nucleotide 5′ upstream region
Author(s) -
Judith A. Lengyel,
Melissa Graham
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.14.5719
Subject(s) - biology , transcription (linguistics) , rna , hsp70 , gene , microbiology and biotechnology , heat shock protein , genetics , philosophy , linguistics
A highly homologous 400 nucleotide sequence flanks the 5' end and extends 64 NT into the transcribed portion of all five hsp70 and seven alpha beta heat shock genes in Drosophila melanogaster (1-4). To determine the extent to which this sequence dictates coordinate regulation, we compared the total mass, continuous labeling and pulse-labeling of hsp70 and alpha beta RNAs at different times and temperatures of heat shock. By all these measurements, expression of both hsp70 and alpha beta genes increased and decreased in parallel. Hsp70 RNA was generally synthesized at a higher rate and accumulated to a greater extent than alpha beta RNA. As the temperature of heat shock increased, however, the rate of synthesis and accumulation of hsp70 relative to alpha beta RNA decreased. Another difference was that a larger fraction of hsp 70, as compared to alpha beta RNA was exported from the nucleus. For both RNAs, export decreased as the heat shock temperature was increased. The hsp70 and alpha beta genes are thus expressed in parallel, but the homologous 5' upstream sequences do not dictate equal rates of transcription or export from the nucleus.

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