Crowley, Thomas E. and Bond, Martha W. and Meyerowitz, Elliot M. (1983) The structural genes for three Drosophila glue proteins reside at a single polytene chromosome puff locus. Molecular and Cellular Biology, 3 (4). pp. 623-634. ISSN 0270-7306 http://resolver.caltech.edu/CaltechAUTHORS:CROmcb83
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The polytene chromosome puff at 68C on the Drosophila melanogaster third chromosome is thought from genetic experiments to contain the structural gene for one of the secreted salivary gland glue polypeptides, sgs-3. Previous work has demonstrated that the DNA included in this puff contains sequences that are transcribed to give three different polyadenylated RNAs that are abundant in third-larval-instar salivary glands. These have been called the group II, group III, and group IV RNAs. In the experiments reported here, we used the nucleotide sequence of the DNA coding for these RNAs to predict some of the physical and chemical properties expected of their protein products, including molecular weight, amino acid composition, and amino acid sequence. Salivary gland polypeptides with molecular weights similar to those expected for the 68C RNA translation products, and with the expected degree of incorporation of different radioactive amino acids, were purified. These proteins were shown by amino acid sequencing to correspond to the protein products of the 68C RNAs. It was further shown that each of these proteins is a part of the secreted salivary gland glue: the group IV RNA codes for the previously described sgs-3, whereas the group II and III RNAs code for the newly identified glue polypeptides sgs-8 and sgs-7.
|Additional Information:||Copyright © 1983 by the American Society for Microbiology. Received 27 September 1982/Accepted 14 January 1983 We thank M. Garfinkel and R. Pruitt for DNA sequence information and discussions during the course of this work, H. Mitchell for performing the larval injections, J. Bell for assistance with the protein sequencing, M. McMillan for providing the computer program used to convert counts per minute to disintegrations per minute, and E. Lujan for performing the protein electrodialysis before sequencing. We also thank J. Kobori and S. Scherer for their critical reading of this manuscript. This work was supported by a Public Health Service grant to E.M.M. from the National Institute of General Medical Sciences. M.W.B. was supported by a Public Health Service individual postdoctoral fellowship from the National Institutes of Health, and T.E.C. was supported by a National Research Service Award from the National Institute of General Medical Sciences.|
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