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Journal of Bacteriology, January 2007, p. 169-178, Vol. 189, No. 1
0021-9193/07/$08.00+0     doi:10.1128/JB.00792-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

ß-D-Allose Inhibits Fruiting Body Formation and Sporulation in Myxococcus xanthus{triangledown}

Marielena Chavira,1 Nga Cao,1 Karen Le,1 Tanveer Riar,1 Navid Moradshahi,1 Melinda McBride,1 Renate Lux,2 and Wenyuan Shi1,2*

Department of Microbiology, Immunology and Molecular Genetics,1 School of Dentistry, University of California, Los Angeles, California2

Received 1 June 2006/ Accepted 3 October 2006

Myxococcus xanthus, a gram-negative soil bacterium, responds to amino acid starvation by entering a process of multicellular development which culminates in the assembly of spore-filled fruiting bodies. Previous studies utilizing developmental inhibitors (such as methionine, lysine, or threonine) have revealed important clues about the mechanisms involved in fruiting body formation. We used Biolog phenotype microarrays to screen 384 chemicals for complete inhibition of fruiting body development in M. xanthus. Here, we report the identification of a novel inhibitor of fruiting body formation and sporulation, ß-D-allose. ß-D-Allose, a rare sugar, is a member of the aldohexose family and a C3 epimer of glucose. Our studies show that ß-D-allose does not affect cell growth, viability, agglutination, or motility. However, ß-galactosidase reporters demonstrate that genes activated between 4 and 14 h of development show significantly lower expression levels in the presence of ß-D-allose. Furthermore, inhibition of fruiting body formation occurs only when ß-D-allose is added to submerged cultures before 12 h of development. In competition studies, high concentrations of galactose and xylose antagonize the nonfruiting response to ß-D-allose, while glucose is capable of partial antagonism. Finally, a magellan-4 transposon mutagenesis screen identified glcK, a putative glucokinase gene, required for ß-D-allose-mediated inhibition of fruiting body formation. Subsequent glucokinase activity assays of the glcK mutant further supported the role of this protein in glucose phosphorylation.


* Corresponding author. Mailing address: UCLA School of Dentistry, CHS 20-114, 650 Charles E. Young Dr. South, Box 951668, Los Angeles, CA 90095-1668. Phone: (310) 825-8356. Fax: (310) 794-7109. E-mail: wenyuan{at}ucla.edu.

{triangledown} Published ahead of print on 20 October 2006.


Journal of Bacteriology, January 2007, p. 169-178, Vol. 189, No. 1
0021-9193/07/$08.00+0     doi:10.1128/JB.00792-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.







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