This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ward, M. J.
Right arrow Articles by Zusman, D. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ward, M. J.
Right arrow Articles by Zusman, D. R.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2000, p. 546-550, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Disruption of aldA Influences the Developmental Process in Myxococcus xanthus

Mandy J. Ward, Helen Lew, and David R. Zusman*

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720

Received 5 August 1999/Accepted 26 October 1999

Previously, we identified a gene (aldA) from Myxococcus xanthus, which we suggested encoded the enzyme alanine dehydrogenase on the basis of similarity to known Ald protein sequences (M. J. Ward, H. Lew, A. Treuner-Lange, and D. R. Zusman, J. Bacteriol. 180:5668-5675, 1998). In this study, we have confirmed that aldA does encode a functional alanine dehydrogenase, since it catalyzes the reversible conversion of alanine to pyruvate and ammonia. Whereas an aldA gene disruption mutation did not significantly influence the rate of growth or spreading on a rich medium, AldA was required for growth on a minimal medium containing L-alanine as the major source of carbon. Under developmental conditions, the aldA mutation caused delayed aggregation in both wild-type (DZ2) and FB (DZF1) strains. Poorly formed aggregates and reduced levels of spores were apparent in the DZ2 aldA mutant, even after prolonged development.

* Corresponding author. Mailing address: Department of Molecular and Cell Biology, 401 Barker Hall, University of California at Berkeley, Berkeley, CA 94720-3204. Phone: (510) 642-2293. Fax: (510) 643-6334. E-mail: zusman{at}uclink4.berkeley.edu.

Journal of Bacteriology, January 2000, p. 546-550, Vol. 182, No. 2
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Chen, J. M., Alexander, D. C., Behr, M. A., Liu, J. (2003). Mycobacterium bovis BCG Vaccines Exhibit Defects in Alanine and Serine Catabolism. Infect. Immun. 71: 708-716 [Abstract] [Full Text]  
  • Feng, Z., Caceres, N. E., Sarath, G., Barletta, R. G. (2002). Mycobacterium smegmatisL-Alanine Dehydrogenase (Ald) Is Required for Proficient Utilization of Alanine as a Sole Nitrogen Source and Sustained Anaerobic Growth. J. Bacteriol. 184: 5001-5010 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»