Open AccessFour small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.
Author(s) -
Thomas D. Ingolia,
Elizabeth A. Craig
Publication year - 1982
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.79.7.2360
Subject(s) - heat shock protein , gene , amino acid , biology , open reading frame , crystallin , homology (biology) , drosophila melanogaster , peptide sequence , genetics , locus (genetics) , protein primary structure , hspa12a , microbiology and biotechnology , heat shock
The primary base sequence of the protein coding regions of the four small heat shock genes of Drosophila melanogaster present at cytological locus 67B has been determined. A single open reading frame large enough to encode a small heat shock protein is found for each gene. The molecular weights of the predicted proteins are in good agreement with experimentally determined values obtained from gel electrophoresis. The predicted amino acid sequences of the four small heat shock genes show striking homologies over approximately 50% of their lengths. This region of extensive homology extends from about amino acid 85 to amino acid 195 out of a total of approximately 200 amino acids. Comparison of the predicted sequence with the known sequences of other proteins revealed a remarkable similarity between this region of homology and the corresponding region of mammalian alpha-crystallin. The possible functional significance of this structural similarity is discussed.