A specific DIF binding protein in Dictyostelium.
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Journal: 1990/November - EMBO Journal
ISSN: 0261-4189
PUBMED: 2170113
Abstract:
Differentiation Inducing Factor (DIF-1), a small chlorinated organic molecule which is produced during Dictyostelium development, is believed to be the morphogen that controls the stalk-specific pathway of differentiation. We describe the identification and characterization of a protease-sensitive activity from cell lysates which binds tritiated DIF-1 with the properties expected of a DIF receptor. Scatchard and linear subtraction plots show a single class of binding sites, of high affinity (Kd = 1.8 nM) and low abundance (1100 sites/cell). The activity elutes from heparin-agarose as a single peak. Various DIF-1 analogues compete for binding in proportion to their activities in a stalk cell differentiation bioassay. The amount of binding activity is developmentally regulated, peaking shortly before the appearance of the prestalk-prespore pattern and before the developmental rise in DIF concentration; the rise occurs at the same time that prestalk-specific genes become DIF inducible. Addition of cyclic AMP to aggregated cells, which induces post-aggregative gene expression in general, also induces the binding activity.
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EMBO J 9(10): 3323-3328
PMID: 2170113

A specific DIF binding protein in Dictyostelium.

Abstract

Differentiation Inducing Factor (DIF-1), a small chlorinated organic molecule which is produced during Dictyostelium development, is believed to be the morphogen that controls the stalk-specific pathway of differentiation. We describe the identification and characterization of a protease-sensitive activity from cell lysates which binds tritiated DIF-1 with the properties expected of a DIF receptor. Scatchard and linear subtraction plots show a single class of binding sites, of high affinity (Kd = 1.8 nM) and low abundance (1100 sites/cell). The activity elutes from heparin-agarose as a single peak. Various DIF-1 analogues compete for binding in proportion to their activities in a stalk cell differentiation bioassay. The amount of binding activity is developmentally regulated, peaking shortly before the appearance of the prestalk-prespore pattern and before the developmental rise in DIF concentration; the rise occurs at the same time that prestalk-specific genes become DIF inducible. Addition of cyclic AMP to aggregated cells, which induces post-aggregative gene expression in general, also induces the binding activity.

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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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MRC Laboratory of Molecular Biology, Cambridge, UK.
MRC Laboratory of Molecular Biology, Cambridge, UK.
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Abstract
Differentiation Inducing Factor (DIF-1), a small chlorinated organic molecule which is produced during Dictyostelium development, is believed to be the morphogen that controls the stalk-specific pathway of differentiation. We describe the identification and characterization of a protease-sensitive activity from cell lysates which binds tritiated DIF-1 with the properties expected of a DIF receptor. Scatchard and linear subtraction plots show a single class of binding sites, of high affinity (Kd = 1.8 nM) and low abundance (1100 sites/cell). The activity elutes from heparin-agarose as a single peak. Various DIF-1 analogues compete for binding in proportion to their activities in a stalk cell differentiation bioassay. The amount of binding activity is developmentally regulated, peaking shortly before the appearance of the prestalk-prespore pattern and before the developmental rise in DIF concentration; the rise occurs at the same time that prestalk-specific genes become DIF inducible. Addition of cyclic AMP to aggregated cells, which induces post-aggregative gene expression in general, also induces the binding activity.
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