Literature DB >> 17248656

Dominance Relationships between Two Allelic Genes Controlling Glycosyltransferases with Different Substrate Specificity in Melandrium.

J van Brederode1, G van Nigtevecht.   

Abstract

Genetical analysis showed that the genes g(G) and g(X), which control, respectively, the glucosylation and xylosylation of the 7-hydroxyl group of isovitexin in the petals of Melandrium, are alleles. In petal extracts of plants possessing the gene g(X) an enzyme was present which catalyzed the transfer of the xylose moiety of UDP-xylose to the 7-hydroxyl group of isovitexin. The xylosyl-transferase controlled by the gene g(X) had a "true K(m) value" of 0.77 mM for UDP-xylose. The "true K(m) value" for isovitexin was << 0.04 mM. The transfer of glucose from UDP-glucose to the 7-hydroxyl group of isovitexin is catalyzed by the enzyme controlled by gene g(G). In plants possessing both the alleles g(G) and g(X), only the gene product of g(G), i.e., isovitexin 7-O-glucoside, was found. In this respect g(G) is dominant over allele g(X). In petal extracts of these g(G)g(X) plants, however, besides UDP-glucose: isovitexin 7-O-glucosyltransferase, also UDP-xylose: isovitexin 7-O-xylosyltransferase could be detected. This means that the dominance is not a consequence of transcriptional and/or translational control. Enzyme kinetic experiments showed that inhibition of the xylosyltransferase by the endproduct of the glucosyltransferase did not occur. Comparison of the enzyme kinetic parameters revealed that the dominance is probably caused by differences in V(max) between the two enzymes, both working at saturating isovitexin concentrations. A competition model is suggested which explains why the amount of isovitexin 7-O-glucoside in g(G)g(G) plants and the amount of isovitexin 7-O-xyloside in g(X)g(X) plants are about the same, whereas in g(G)g(X) plants isovitexin 7-O-xyloside escapes detection. The differences in distribution of the isovitexin glycosylation genes in the two species M. album and M. dioicum are discussed.

Entities:  

Year:  1974        PMID: 17248656      PMCID: PMC1213143     

Source DB:  PubMed          Journal:  Genetics        ISSN: 0016-6731            Impact factor:   4.562


  2 in total

1.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

Review 2.  Enzymatic basis for blood groups in man.

Authors:  V Ginsburg
Journal:  Adv Enzymol Relat Areas Mol Biol       Date:  1972
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  5 in total

1.  Are allozymes differing in substrate specificity involved in the evolution of Silene species?

Authors:  J van Brederode; O Mastenbroek
Journal:  Theor Appl Genet       Date:  1983-01       Impact factor: 5.699

2.  Variation in the substrate specificity of allozymes catalyzing flavone-O-glucoside biosynthesis in Silene plants.

Authors:  J M Steyns; J van Brederode
Journal:  Biochem Genet       Date:  1986-06       Impact factor: 1.890

3.  Unravelling the biochemical basis of blood group ABO and Lewis antigenic specificity.

Authors:  W T Morgan; W M Watkins
Journal:  Glycoconj J       Date:  2000 Jul-Sep       Impact factor: 2.916

4.  Dominance relationships between allelic glycosyltransferase genes in Melandrium: An enzyme-kinetic approach.

Authors:  J van Brederode; G van Nigtevecht
Journal:  Theor Appl Genet       Date:  1975-01       Impact factor: 5.699

5.  Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica).

Authors:  J Kamsteeg; J van Brederode; G van Nigtevecht
Journal:  Biochem Genet       Date:  1978-12       Impact factor: 1.890

  5 in total

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