Differential effects of chemoreceptor methylation-domain mutations on swarming and development in the social bacterium Myxococcus xanthus.
The soil bacterium Myxococcus xanthus is a model organism for the study of multicellular behaviour and development in bacteria. M. xanthus cells move on solid surfaces by gliding motility, periodically reversing their direction of movement. Motility is co-ordinated to allow cells to effectively feed on macromolecules or prey bacteria when nutrients are plentiful and to form developmental fruiting bodies when nutrients are limiting. The Frz signal transduction pathway regulates cellular movements by modulating cell reversal frequency. Input to the Frz pathway is controlled by the cytoplasmic receptor, FrzCD, a methyl-accepting chemotaxis protein (MCP). FrzCD lacks the transmembrane and periplasmic domains common to MCPs but contains a unique N-terminal domain, the predicted ligand-binding domain. As deletion of the N-terminal domain of FrzCD only results in minor defects in motility, we investigated the possibility that the methylation of the conserved C-terminal domain of FrzCD plays a central role in regulating the pathway. For this study, each of the potential methylation sites of FrzCD were systematically modified by site-directed mutagenesis, substituting glutamine/glutamate pairs for alanines. Four of the seven mutations produced dramatic phenotypes; two of the mutations had a stimulatory effect on the pathway, as evidenced by cells hyper-reversing, whereas another two had an inhibitory effect, causing these cells to rarely reverse. These four mutants displayed defects in vegetative swarming and developmental aggregation. These results suggests a model in which the methylation domain can both activate and inhibit the Frz pathway depending on which residues are methylated. The diversity of phenotypes suggests that specific modifications of FrzCD act to differentially regulate motility and developmental aggregation in M. xanthus.
Astling
David P
DP
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3204, USA.
Lee
Josephine Y
JY
Zusman
David R
DR
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002633:Chemotaxis / Q000502:physiology*; D004121:Dimethyl Sulfoxide / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008745:Methylation; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D016941:Myxococcus xanthus / Q000235:genetics / Q000502:physiology*; D000439:Pentanols / Q000378:metabolism; D010641:Phenotype; D015398:Signal Transduction / Q000502:physiology*; D012997:Solvents
D001426:Bacterial Proteins; C065626:FrzCD protein, Myxococcus xanthus; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D000439:Pentanols; D012997:Solvents; C029683:isopentyl alcohol; D004121:Dimethyl Sulfoxide