Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Bacteriol. 1990 Dec;172(12):6661-8.

Purification and characterization of the Myxococcus xanthus FrzE protein shows that it has autophosphorylation activity.

Author information

  • 1Department of Molecular and Cell Biology, University of California, Berkeley 94720.

Abstract

Myxococcus xanthus exhibits multicellular interactions during vegetative growth and fruiting body formation. Gliding motility is needed for these interactions. The frizzy (frz) genes are required to control directed motility. FrzE is homologous to both CheA and CheY from Salmonella typhimurium. We used polyclonal antiserum raised against a fusion protein to detect FrzE in M. xanthus extracts by Western immunoblot analysis. FrzE was clearly present during vegetative growth and at much lower levels during development. A recombinant FrzE protein was overproduced in Escherichia coli, purified from inclusion bodies, and renatured. FrzE was autophosphorylated when it was incubated in the presence of [gamma-32P]ATP and MnCl2. Chemical analyses of the phosphorylated FrzE protein indicated that it contained an acylphosphate; probably phosphoaspartate. FrzE was phosphorylated in an intramolecular reaction. Based on these observations, we propose a model of the mechanism of FrzE phosphorylation in which autophosphorylation initially occurs at a conserved histidine residue within the "CheA" domain and then, via an intramolecular transphosphorylation, is transferred to a conserved aspartate residue within the "CheY" domain.

PMID:
2123853
[PubMed - indexed for MEDLINE]
PMCID:
PMC210777
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk