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Genetics and physiological expression of beta-hydroxy acid dehydrogenase in Drosophila
A mutant Hadnl was induced in Drosophila melanogaster and found to be deficient in beta-hydroxy acid dehydrogenase. This mutation was utilized to study the genetics and physiological expression of Had+ . Had+ was mapped to the X chromosome at 54.4 and seems to be the structural gene for the enzyme....
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Published in: | Biochemical genetics 1978-01, Vol.16 (3-4), p.333-342 |
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container_title | Biochemical genetics |
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creator | Tobler, J E Grell, E H |
description | A mutant Hadnl was induced in Drosophila melanogaster and found to be deficient in beta-hydroxy acid dehydrogenase. This mutation was utilized to study the genetics and physiological expression of Had+ . Had+ was mapped to the X chromosome at 54.4 and seems to be the structural gene for the enzyme. Enzyme activity in male and female flies indicates that the gene shows both dosage compensation independent from dose effect and differential activity during ontogeny. Electrophoretic mobility data indicate that the enzyme is a dimer which forms by random association of subunits. The fact that the mutant shows no detrimental effect implies that the enzyme is dispensable, at least under laboratory conditions. The biological and technical implications of this gene--enzyme system are discussed. |
doi_str_mv | 10.1007/BF00484089 |
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This mutation was utilized to study the genetics and physiological expression of Had+ . Had+ was mapped to the X chromosome at 54.4 and seems to be the structural gene for the enzyme. Enzyme activity in male and female flies indicates that the gene shows both dosage compensation independent from dose effect and differential activity during ontogeny. Electrophoretic mobility data indicate that the enzyme is a dimer which forms by random association of subunits. The fact that the mutant shows no detrimental effect implies that the enzyme is dispensable, at least under laboratory conditions. The biological and technical implications of this gene--enzyme system are discussed.</description><identifier>ISSN: 0006-2928</identifier><identifier>DOI: 10.1007/BF00484089</identifier><identifier>PMID: 28119</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Carbohydrate Dehydrogenases - genetics ; Carbohydrate Dehydrogenases - metabolism ; Chromosome Mapping ; Drosophila melanogaster - enzymology ; Drosophila melanogaster - genetics ; Female ; Genes ; Genetic Linkage ; Hydrogen-Ion Concentration ; Kinetics ; Male ; Substrate Specificity ; X Chromosome</subject><ispartof>Biochemical genetics, 1978-01, Vol.16 (3-4), p.333-342</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tobler, J E</creatorcontrib><creatorcontrib>Grell, E H</creatorcontrib><title>Genetics and physiological expression of beta-hydroxy acid dehydrogenase in Drosophila</title><title>Biochemical genetics</title><addtitle>Biochem Genet</addtitle><description>A mutant Hadnl was induced in Drosophila melanogaster and found to be deficient in beta-hydroxy acid dehydrogenase. This mutation was utilized to study the genetics and physiological expression of Had+ . Had+ was mapped to the X chromosome at 54.4 and seems to be the structural gene for the enzyme. Enzyme activity in male and female flies indicates that the gene shows both dosage compensation independent from dose effect and differential activity during ontogeny. Electrophoretic mobility data indicate that the enzyme is a dimer which forms by random association of subunits. The fact that the mutant shows no detrimental effect implies that the enzyme is dispensable, at least under laboratory conditions. The biological and technical implications of this gene--enzyme system are discussed.</description><subject>Animals</subject><subject>Carbohydrate Dehydrogenases - genetics</subject><subject>Carbohydrate Dehydrogenases - metabolism</subject><subject>Chromosome Mapping</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Female</subject><subject>Genes</subject><subject>Genetic Linkage</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Male</subject><subject>Substrate Specificity</subject><subject>X Chromosome</subject><issn>0006-2928</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNotkL1PwzAUxD1QQSksrCye2ALPH0mdEQotSJVYKtboOX5pjdI4xInU_PeU0ul0p59Op2PsTsCjAJg_vSwBtNFg8gs2BYAskbk0V-w6xu-jzUHrSzaRRoh8yr5W1FDvy8ixcbzdjdGHOmx9iTWnQ9tRPAYNDxW31GOyG10XDiPH0jvu6GS31GAk7hv-2oUY2p2v8YZNKqwj3Z51xjbLt83iPVl_rj4Wz-skSCX6JMfMZqjImQyc0O64s3SCpEWhlZMaUsidtUJBilpWDpSshEJlnTNmnqoZe_ivbbvwM1Dsi72PJdU1NhSGWMy1gFTqP_D-DA52T65oO7_HbixOL6hfOudcig</recordid><startdate>19780101</startdate><enddate>19780101</enddate><creator>Tobler, J E</creator><creator>Grell, E H</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19780101</creationdate><title>Genetics and physiological expression of beta-hydroxy acid dehydrogenase in Drosophila</title><author>Tobler, J E ; Grell, E H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-o231t-9a6b6a3ed860d14d928cd1e2ba143d240509dbb1305a42fd032f13a3bdd88753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Animals</topic><topic>Carbohydrate Dehydrogenases - genetics</topic><topic>Carbohydrate Dehydrogenases - metabolism</topic><topic>Chromosome Mapping</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Female</topic><topic>Genes</topic><topic>Genetic Linkage</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Male</topic><topic>Substrate Specificity</topic><topic>X Chromosome</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tobler, J E</creatorcontrib><creatorcontrib>Grell, E H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tobler, J E</au><au>Grell, E H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetics and physiological expression of beta-hydroxy acid dehydrogenase in Drosophila</atitle><jtitle>Biochemical genetics</jtitle><addtitle>Biochem Genet</addtitle><date>1978-01-01</date><risdate>1978</risdate><volume>16</volume><issue>3-4</issue><spage>333</spage><epage>342</epage><pages>333-342</pages><issn>0006-2928</issn><abstract>A mutant Hadnl was induced in Drosophila melanogaster and found to be deficient in beta-hydroxy acid dehydrogenase. 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subjects | Animals Carbohydrate Dehydrogenases - genetics Carbohydrate Dehydrogenases - metabolism Chromosome Mapping Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Female Genes Genetic Linkage Hydrogen-Ion Concentration Kinetics Male Substrate Specificity X Chromosome |
title | Genetics and physiological expression of beta-hydroxy acid dehydrogenase in Drosophila |
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