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. 1986 Aug;6(8):2820–2827. doi: 10.1128/mcb.6.8.2820

Sulfate suicide selection of Dictyostelium discoideum mutants defective in protein glycosylation.

J A Boose, E J Henderson
PMCID: PMC367849  PMID: 3785215

Abstract

The assembly and processing of glycoprotein-linked oligosaccharides in Dictyostelium discoideum has been shown to generate a wide array of glycan structures which undergo dramatic developmental regulation. As late steps in processing of these oligosaccharides involve sulfation, a sulfate suicide selection procedure was developed to select for temperature-sensitive glycoprotein-processing mutants. Of 673 clones derived from the survivors of suicide selection, 99 were classified by replica-plating fluorography as temperature sensitive for sulfate transport or incorporation. Of these, 74 were unable to complete the developmental program to the fruiting body stage at the restrictive temperature, 29 being blocked in some aspect of aggregation and 45 being blocked at some postaggregation stage. Quantitative metabolic labeling experiments with representative clones showed that they incorporated wild-type levels of [35S]methionine but reduced levels of sulfate at the restrictive temperature. The specific incorporation patterns in the mutants suggest that distinct oligosaccharide-processing steps are involved in different developmental events.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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