Evidence for mutations in the structural gene for homocitrate synthase in Saccharomycopsis lipolytica

1979 ◽  
Vol 172 (2) ◽  
pp. 185-192 ◽  
Author(s):  
Claude Gaillardin ◽  
Henri Heslot
Keyword(s):  
Structural Gene ◽  
Saccharomycopsis Lipolytica ◽  
Homocitrate Synthase

Bt1, a structural gene for the major 39-44 kDa amyloplast membrane polypeptides

1995 ◽  
Vol 95 (2) ◽  
pp. 176-186 ◽  
Author(s):  
Heping Cao ◽  
Thomas D. Sullivan ◽  
Charles D. Boyer ◽  
Jack C. Shannon
Keyword(s):  
Structural Gene

scholarly journals A NEW MAP LOCATION FOR THE ilvB LOCUS OF ESCHERICHIA COLI

Genetics ◽  
1980 ◽  
Vol 96 (1) ◽  
pp. 59-77
Author(s):  
Thomas C Newman ◽  
Mark Levinthal
Keyword(s):  
Escherichia Coli ◽  
Structural Gene ◽  
Acetolactate Synthase ◽  
Deletion Mapping ◽  
Donor Strain ◽  
E Coli ◽  
Linkage Of Genes ◽  
Map Location ◽  
New Alleles

ABSTRACT We isolated, in E. coli K12, new alleles of the ilvB locus, the structural gene for acetolactate synthase isoenzyme I, and showed them to map at or near the ilvB619 site. The map position of the ilvB locus was redetermined because plasmids containing the ilvC-cya portion of the chromosome did not complement mutations at the ilvB locus. Furthermore, diploids for the ilvEDAC genes formed with these plasmids in an ilvHI background facilitated the isolation of the new ilvB alleles. The ilvB locus was remapped and found to be located at 81.5 minutes, between the uhp and dnaA loci. This location was determined by two- and three-point transductional crosses, deletion mapping and complementation with newly isolated plasmids. One of the new alleles of the ilvB gene is a mu-1 insertion. When present in the donor strain, this allele interferes with the linkage of genes flanking the mu-1 insertion, as well as the linkage of genes to either side of the mu-1 insertion.

scholarly journals Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene.

1988 ◽  
Vol 263 (28) ◽  
pp. 14288-14295 ◽  
Author(s):  
G A Mitchell ◽  
J E Looney ◽  
L C Brody ◽  
G Steel ◽  
M Suchanek ◽  
...  
Keyword(s):  
Cdna Cloning ◽  
Structural Gene

scholarly journals POPULATION GENETICS OF DROSOPHILA AMYLASE. IV. SELECTION IN LABORATORY POPULATIONS MAINTAINED ON DIFFERENT CARBOHYDRATES

Genetics ◽  
1983 ◽  
Vol 103 (4) ◽  
pp. 675-689
Author(s):  
Jeffrey R Powell ◽  
Marko Andjelković
Keyword(s):  
Structural Gene ◽  
Amylase Activity ◽  
Enzyme System ◽  
Specific Expression ◽  
Carbohydrate Source ◽  
Laboratory Populations ◽  
Consistent Change ◽  
Regulation Changes ◽  
Starch Medium

ABSTRACT Two polymorphic systems impinging on α-amylase in Drosophila pseudoobscura have been studied in laboratory populations maintained on medium in which the only carbohydrate source was starch (the substrate of amylase) and replicas maintained on medium in which the only carbohydrate source was maltose (the product of amylase). The two polymorphic systems were alleles at the structural gene (Amy) coding for the enzyme (allozymes) and variation in the tissue-specific expression along the adult midgut controlled by several genes. In the seven populations on maltose medium little consistent change was noted in either system. In the seven populations on starch medium, both polymorphisms exhibited selective changes. A midgut pattern of very limited expression of amylase rose in frequency in all starch populations, as did the frequency of the "fast" (1.00) Amy allele. The overall specific amylase activity did not differ between starch-adapted and maltose-adapted flies.—The results, along with previous studies, indicate that when a gene-enzyme system is specifically stressed in laboratory populations, allozymes often exhibit selective differences. Such results make the selectionist hypothesis at least tenable. Furthermore, the fact that both types of polymorphisms responded to selection indicates the role of structural gene vs. gene regulation changes in adaptive evolution is not an either/or question but one of relative roles and interactions.

scholarly journals A GENETICALLY DISTINCT FORM OF CYCLIC AMP PHOSPHODIESTERASE ASSOCIATED WITH CHROMOMERE 3D4 IN DROSOPHILA MELANOGASTER

Genetics ◽  
1979 ◽  
Vol 91 (3) ◽  
pp. 521-535
Author(s):  
John A Kiger ◽  
Eric Golanty
Keyword(s):  
Drosophila Melanogaster ◽  
Cyclic Amp ◽  
Structural Gene ◽  
Regulatory Gene ◽  
Heat Stability ◽  
Normal Female ◽  
Dependent Manner ◽  
Cyclic Amp Phosphodiesterase ◽  
Heat Stable ◽  
Camp Levels

ABSTRACT Two cyclic AMP phosphodiesterase enzymes (E.C.3.1.4.17) are present in homogenates of adult Drosophila melanogaster. The two enzymes differ from one another in heat stability, affinity for Mg++, Ca++ activation and molecular weight. They do not differ markedly in their affinities for cyclic AMP, and both exhibit anomalous Michaelis-Menten kinetics. The more heatlabile enzyme is controlled in a dosage-dependent manner by chromomere 3D4 of the X chromosome and is absent in flies that are deficient for chromomere 3D4. Chromomere 3D4 is also necessary for the maintenance of normal cAMP levels, for male fertility, and for normal female fertility and oogenesis. The structural gene(s) for the more heat-stable enzyme is located outside of chromomeres 3C12-3D4. Whether 3D4 contains a structural gene, or a regulatory gene necessary for the presence of the labile enzyme, remains to be determined.

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