- THIS ARTICLE
- Full Text (PDF)
- Alert me when this article is cited
- Alert me if a correction is posted
- SERVICES
- Similar articles in this journal
- Similar articles in PubMed
- Alert me to new issues of the journal
- Download to citation manager
- Reprints & Permissions
- CITING ARTICLES
- Citing Articles via HighWire
- Citing Articles via Google Scholar
- GOOGLE SCHOLAR
- Articles by Choudhary, M.
- Articles by Laurie, C. C.
- Search for Related Content
- PUBMED
- PubMed Citation
- Articles by Choudhary, M.
- Articles by Laurie, C. C.
Genetics, Vol 129, 481-488, Copyright © 1991
INVESTIGATIONS |
Use of in Vitro Mutagenesis to Analyze the Molecular Basis of the Difference in Adh Expression Associated With the Allozyme Polymorphism in Drosophila melanogaster
M. Choudhary and C. C. Laurie
Present address: Department of Ecology and Evolutionary Biology, Rice University, P.O. Box 1892, Houston, Texas 77251
In natural populations of Drosophila melanogaster, the alcohol dehydrogenase (Adh) locus is polymorphic for two allozymes, designated Slow and Fast. Fast homozygotes generally have a two- to threefold higher ADH activity level than Slow homozygotes for two reasons: they have a higher concentration of ADH protein and the Fast protein has a higher catalytic efficiency. DNA sequencing studies have shown that the two allozymes generally differ by only a single amino acid at residue 192, which must therefore be the cause of the catalytic efficiency difference. A previous P element-transformation experiment mapped the difference in ADH protein level to a 2.3-kb HpaI/ClaI restriction fragment, which contains all of the Adh coding sequences but excludes all of the 5' flanking region of the distal transcriptional unit. Here we report the results of a site-directed in vitro mutagenesis experiment designed to investigate the effects of the amino acid replacement. This replacement has the expected effect on catalytic efficiency, but there is no detectable effect on the concentration of ADH protein estimated immunologically. This result shows that the average difference in ADH protein level between the allozymic classes is due to linkage disequilibrium between the amino acid replacement and one or more other polymorphisms within the HpaI/ClaI fragment. Sequence analysis of several Fast and Slow alleles suggested that the other polymorphism might be a silent substitution at nucleotide 1443, but another in vitro mutagenesis experiment reported here shows that this is not the case. Therefore, the molecular basis of the difference in ADH protein concentration between the allozymic classes remains an open question.
This article has been cited by other articles:
 |
|
 |
|
  A. M. Glazier, J. H. Nadeau, and T. J. Aitman Finding Genes That Underlie Complex Traits Science, December 20, 2002; 298(5602): 2345 - 2349. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. A. Odgers, C. F. Aquadro, C. W. Coppin, M. J. Healy, and J. G. Oakeshott Nucleotide Polymorphism in the Est6 Promoter, Which Is Widespread in Derived Populations of Drosophila melanogaster, Changes the Level of Esterase 6 Expressed in the Male Ejaculatory Duct Genetics, October 1, 2002; 162(2): 785 - 797. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Parsch, J. A. Russell, I. Beerman, D. L. Hartl, and W. Stephan Deletion of a Conserved Regulatory Element in the Drosophila Adh Gene Leads to Increased Alcohol Dehydrogenase Activity but Also Delays Development Genetics, September 1, 2000; 156(1): 219 - 227. [Abstract] [Full Text]
|
|
|
|
|
|
J. Parsch, W. Stephan, and S. Tanda A Highly Conserved Sequence in the 3'-Untranslated Region of the Drosophila Adh Gene Plays a Functional Role in Adh Expression Genetics, February 1, 1999; 151(2): 667 - 674. [Abstract] [Full Text]
|
|
|
|
 |
|
 J. Parsch, S. Tanda, and W. Stephan Site-directed mutations reveal long-range compensatory interactions in the Adh gene of Drosophila melanogaster PNAS, February 4, 1997; 94(3): 928 - 933. [Abstract] [Full Text] [PDF]
|
|