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. 1990 May;87(10):3635–3639. doi: 10.1073/pnas.87.10.3635

Purification and properties of Myxococcus xanthus C-factor, an intercellular signaling protein.

S K Kim 1, D Kaiser 1
PMCID: PMC53957  PMID: 2111012

Abstract

C-factor, a Myxococcus xanthus protein that restores the developmental defects of a class of nonautonomous mutants resulting from mutation of the csgA gene, has been purified approximately 1000-fold from starved wild-type cells. The monomeric form of C-factor is a single polypeptide with a molecular mass of 17 kDa that can be solubilized by detergent from membrane components. Characterization by gel filtration and denaturing gel electrophoresis suggests that biologically active C-factor is a dimer composed of two 17-kDa monomers. Antibodies against a form of the M. xanthus csgA gene product overexpressed in Escherichia coli react with purified C-factor.

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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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