Effects of site-directed mutagenesis of <Emphasis Type="Italic">mglA</Emphasis> on motility and swarming of <Emphasis Type="Italic">Myxococcus xanthus</Emphasis> |
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| Authors: | Sarah A Fremgen Neal S Burke Patricia L Hartzell |
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| Institution: | 1.Department of Microbiology, Molecular Biology and Biochemistry, 142 Life Science,University of Idaho,Moscow,USA;2.Department of Veterinary Medicine,Washington State University,Pullman,USA |
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| Abstract: | Background The mglA gene from the bacterium Myxococcus xanthus encodes a 22kDa protein related to the Ras superfamily of monomeric GTPases. MglA is required for the normal function of
A-motility (adventurous), S-motility (social), fruiting body morphogenesis, and sporulation. MglA and its homologs differ from all eukaryotic and other prokaryotic
GTPases because they have a threonine (Thr78) in place of the highly conserved aspartate residue of the consensus PM3 (phosphate-magnesium binding) region. To identify residues critical for MglA function or potential protein interactions, and explore the
function of Thr78, the phenotypes of 18 mglA mutants were characterized. |
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