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Mutation generating a fragment of the major heat shock-inducible polypeptide in Drosophila melanogaster
Author(s) -
Corrado Caggese,
Ruggiero Caizzi,
M. Morea,
Franco Scalenghe,
Ferruccio Ritossa
Publication year - 1979
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.5.2385
Subject(s) - drosophila melanogaster , locus (genetics) , heat shock protein , biology , gene , hspa4 , hspa14 , genetics , microbiology and biotechnology , hspa12a , mutant , heat shock , hsp70
Drosophila melanogaster tissues carrying a third chromosome with the deletionDf (3R )Kar D2 make a 40,000-dalton (Dal) heat shock protein not made by wild type. The unusual polypeptide was inducible in every tissue examined. Tryptic peptide fingerprints showed it to include part of the 70,000-Dal major heat shock protein. Mapping experiments placed the mutation responsible for the 40,000-Dal protein at or close to thekar D2 deletion. One break point of the deletion is in subdivision 87A, close to or at a heat shock locus that codes for the 70,000-Dal protein. The results are consistent with the possibility that this break point is within a gene for the 70,000-Dal protein, leaving only the initial portion of its coding sequence. This would specify the direction of transcription of the mutant gene as proximal to distal on the normal chromosome. The 87A heat shock locus should contain at least two genes for the 70,000-Dal protein, because embryos homozygous for thekar D2 deletion and lacking the heat shock locus at 87C, which also codes for the 70,000-Dal protein, nevertheless produced both the 40,000-Dal and the 70,000-Dal proteins upon temperature elevation. Using the presence of the 40,000-Dal protein to monitor chromosome segregation, we found that embryos homozygous for deletions of the heat shock puff site at 93D exhibited a normal electrophoretic pattern of heat shock proteins.

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