Purification and properties of Myxococcus xanthus C-factor, an intercellular signaling protein.
AUTOR(ES)
Kim, S K
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=53957Documentos Relacionados
- C factor, a cell-surface-associated intercellular signaling protein, stimulates the cytoplasmic Frz signal transduction system in Myxococcus xanthus.
- Purification and in vitro phosphorylation of Myxococcus xanthus AsgA protein.
- Myxococcus xanthus protein C is a major spore surface protein.
- Myxococcus xanthus encodes an ATP-dependent protease which is required for developmental gene transcription and intercellular signaling.
- Purification and properties of Myxococcus xanthus cell surface antigen 1604.