Abstract
From a collection of electrophoretic variants of XDH obtained from laboratory strains and natural populations, a stock was isolated that was associated with much greater than normal levels of XDH activity. Preliminary recombination experiments demonstrated that this character maps to the rosy locus. While a series of observations failed to relate this phenotype to alteration in the structure of the XDH polypeptide, kinetic and immunological experiments did succeed in associating this character with variation in number of molecules of XDH/fly. Large scale fine structure recombination experiments locate the genetic basis for this variation in number of molecules of XDH/fly to a site very close to, but definitely outside of, the genetic boundaries of the XDH structural information. Observations are described which eliminate the possibility that we are dealing with a tandem duplication of the XDH structural element. Turning to a regulatory role for this genetic element located adjacent to the XDH structural information, a simple experiment is described which demonstrates that it functions as a "cis-acting" regulator of the XDH structural element.
Full Text
The Full Text of this article is available as a PDF (2.2 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Andres R. Y. Aldehyde oxidase and xanthine dehydrogenase from wild-type Drosophila melanogaster and immunologically cross-reacting material from ma-1 mutants. Purification by immunoadsorption and characterization. Eur J Biochem. 1976 Mar 1;62(3):591–600. doi: 10.1111/j.1432-1033.1976.tb10194.x. [DOI] [PubMed] [Google Scholar]
- Chovnick A. Genetic organization in higher organisms. Proc R Soc Lond B Biol Sci. 1966 Mar 22;164(995):198–208. doi: 10.1098/rspb.1966.0023. [DOI] [PubMed] [Google Scholar]
- Glassman E, Mitchell H K. Mutants of Drosophila Melanogaster Deficient in Xanthine Dehydrogenase. Genetics. 1959 Mar;44(2):153–162. doi: 10.1093/genetics/44.2.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 1966 Apr;15(1):45–52. doi: 10.1016/0003-2697(66)90246-6. [DOI] [PubMed] [Google Scholar]
- Lewin B. Units of transcription and translation: the relationship between heterogeneous nuclear RNA and messenger RNA. Cell. 1975 Jan;4(1):11–20. doi: 10.1016/0092-8674(75)90128-2. [DOI] [PubMed] [Google Scholar]
- MONOD J., JACOB F. Teleonomic mechanisms in cellular metabolism, growth, and differentiation. Cold Spring Harb Symp Quant Biol. 1961;26:389–401. doi: 10.1101/sqb.1961.026.01.048. [DOI] [PubMed] [Google Scholar]
- McCarron M., Gelbart W., Chovnick A. Intracistronic mapping of electrophoretic sites in Drosophila melanogaster: fidelity of information transfer by gene conversion. Genetics. 1974 Feb;76(2):289–299. doi: 10.1093/genetics/76.2.289. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ramirez F., Natta C., O'Donnell J. V., Canale V., Bailey G., Sanguensermsri T., Maniatis G. M., Marks P. A., Bank A. Relative numbers of human globin genes assayed with purified alpha and beta complementary human DNA. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1550–1554. doi: 10.1073/pnas.72.4.1550. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SCHALET A., KERNAGHAN R. P., CHOVNICK A. STRUCTURAL AND PHENOTYPIC DEFINITION OF THE ROSY CISTRON IN DROSOPHILA MELANOGASTER. Genetics. 1964 Dec;50:1261–1268. doi: 10.1093/genetics/50.6.1261. [DOI] [PMC free article] [PubMed] [Google Scholar]
