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Journal of Bacteriology, April 2005, p. 2920-2925, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2920-2925.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Positive Selection for Loss-of-Function tat Mutations Identifies Critical Residues Required for TatA Activity

Matthew G. Hicks,1 Philip A. Lee,1,{dagger} George Georgiou,2 Ben C. Berks,3 and Tracy Palmer1,4*

Department of Molecular Microbiology, John Innes Centre,1 School of Biological Sciences, University of East Anglia, Norwich,4 Department of Biochemistry, University of Oxford, Oxford, United Kingdom,3 Department of Chemical Engineering, University of Texas, Austin, Texas2

Received 16 November 2004/ Accepted 3 January 2005

The Tat system, found in the cytoplasmic membrane of many bacteria, is a general export pathway for folded proteins. Here we describe the development of a method, based on the transport of chloramphenicol acetyltransferase, that allows positive selection of mutants defective in Tat function. We have demonstrated the utility of this method by selecting novel loss-of-function alleles of tatA from a pool of random tatA mutations. Most of the mutations that were isolated fall in the amphipathic region of TatA, emphasizing the pivotal role that this part of the protein plays in TatA function.

* Corresponding author. Mailing address: Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, United Kingdom. Phone: 44-1603-450726. Fax: 44-1603-450778. E-mail: tracy.palmer{at}bbsrc.ac.uk.

{dagger} Present address: Department of Chemical Engineering, University of Texas, Austin, TX 78712.

Journal of Bacteriology, April 2005, p. 2920-2925, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2920-2925.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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  • Greene, N. P., Porcelli, I., Buchanan, G., Hicks, M. G., Schermann, S. M., Palmer, T., Berks, B. C. (2007). Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin Arginine Translocase. J. Biol. Chem. 282: 23937-23945 [Abstract] [Full Text]  
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