Arginine promotes Proteus mirabilis motility and fitness by contributing to conservation of the proton gradient and proton motive force
Version of Record online: 7 AUG 2014
© 2014 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 3, Issue 5, pages 630–641, October 2014
How to Cite
MicrobiologyOpen 2014; 3(5): 630–641
- Issue online: 9 OCT 2014
- Version of Record online: 7 AUG 2014
- Manuscript Accepted: 16 JUN 2014
- Manuscript Revised: 4 JUN 2014
- Manuscript Received: 14 APR 2014
- National Institute of Allergy and Infectious Diseases
- National Institutes of Health. Grant Numbers: R01AI059722, F32AI102552
|MBO3194-sup-0001-FIGS1.tif||image/tif||1087K||Figure S1. Arginine decarboxylase is required for optimal growth at pH 5 and response to arginine. Proteus mirabilis HI4320 (A) and the speA mutant (B) were diluted 1:100 in unbuffered LB (pH 7) versus LB adjusted to pH 5 with or without 10 mmol/L arginine. Cultures were incubated at 37°C with continuous shaking, and OD600 readings were taken every 15 min for 18 h. Error bars indicate mean ± SD for one representative experiment with five replicates.|
|MBO3194-sup-0001-TableS1.docx||Word document||12K||Table S1. Primers used in this study.|
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