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Journal of Bacteriology, September 2008, p. 6148-6152, Vol. 190, No. 18
0021-9193/08/$08.00+0 doi:10.1128/JB.00789-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom
Received 5 June 2008/ Accepted 11 July 2008
The GerT protein of Bacillus cereus shares 74% amino acid identity with its homolog GerN. The latter is a Na+/H+-K+ antiporter that is required for normal spore germination in inosine. The germination properties of single and double mutants of B. cereus ATCC 10876 reveal that unlike GerN, which is required for all germination responses that involve the GerI germinant receptor, the GerT protein does not have a significant role in germination, although it is required for the residual GerI-mediated inosine germination response of a gerN mutant. In contrast, GerT has a significant role in outgrowth; gerT mutant spores do not outgrow efficiently under alkaline conditions and outgrow more slowly than the wild type in the presence of high NaCl concentrations. The GerT protein in B. cereus therefore contributes to the success of spore outgrowth from the germinated state during alkaline or Na+ stress.
Published ahead of print on 18 July 2008.
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