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Size polymorphisms due to changes in the number of O-glycosylated tandem repeats in the Dictyostelium discoideum glycoprotein PsA

Article Abstract:

The role of modB dependent glycosylation on the molecular mass polymorphism of PsA glycoproteins from Dictyostelium discoideum was studied using parasequal genetic techniques. The polymorphisms resulted from incremental additions or deletions of an O-glycosylated tandem proline-threonine-valine-threonine repeat. This could be the result of an unequal crossing-over event in an ancestral gene. Molecular mass forms varied far less than initially expected. The amino acid sequence was less than that predicted from the DNA sequence, suggesting the presence of a cleavage site.

Author: Williams, Keith L., Gooley, Andrew A., Marshchalek, Rolf
Publisher: Genetics Society of America
Publication Name: Genetics
Subject: Biological sciences
ISSN: 0016-6731
Year: 1992
Nucleotide sequence, Base sequence, Genetic polymorphisms, Amino acid sequence, Amino acid sequencing

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Tandem repeats in extrachromosomal ribosomal DNA of Dictyostelium discoideum, resulting from chromosomal mutations

Article Abstract:

Duplications in a spacer region of ribosomal DNA (rDNA) resulted in a ladder of ribosomal DNA-containing bands in Dictyostelium discoideum that ranged from 110 to 300 kilobases (kb) on orthogonal field electrophoresis gels. These were found to be due to mutations at either one of two chromosome loci. The ladder was formed by the insertion of a 34-kb fragment into the central spacer region of the rDNA palindrome. Restriction enzyme analysis suggests that these ladders resulted from crossovers between two rDNA molecules.

Author: Williams, Keith L., Cole, Robert A.
Publisher: Genetics Society of America
Publication Name: Genetics
Subject: Biological sciences
ISSN: 0016-6731
Year: 1992
Ribosomes, Microbial mutation, Extrachromosomal DNA

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Glycoprotein complexes interacting with cellulose in the "cell print" zones of the Dictyostelium discoideum extracellular matrix

Article Abstract:

A group of glycoproteins called sheathins are a component of the cell print of the sheath laid down by the slime mold Dictyostelium discoideum in its slug phase. They are associated with cellulose in the sheath and are critical for slug migration. Sheathins have a molecular mass of 53-68 kDa, and are dimeric and trimeric forms of a 12-35 kDa monomer. The subunits are not identical, but are produced by three different genes.

Author: Williams, Keith L., Gooley, Andrew A., Wilkins, Marc R., Zhou-Chou, Ti, Vardy, Phil H.
Publisher: Elsevier B.V.
Publication Name: Developmental Biology
Subject: Biological sciences
ISSN: 0012-1606
Year: 1995
Glycoproteins, Extracellular matrix

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Subjects list: Research, Analysis, Genetic aspects, Dictyostelium
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