Document Type
Article
Publication Date
1-29-2008
Abstract
In some bacteria Lys-tRNALys is used both in translation and for the specific addition of Lys to phosphatidylglycerol in the cytoplasmic membrane. This reaction is catalyzed by the membrane protein MprF, and the lysyl-phosphatidylglycerol formed contributes to the resistance of these bacteria to various cationic antibacterial molecules. Obtaining proteins and reconstituting an in vitro system mimicking membrane conditions is a major challenge to studying the function of membrane proteins, especially when labile substrates such as Lys-tRNALys are required. Here we report methods to obtain a stable enriched membrane fraction containing MprF, and the techniques necessary to quantitatively monitor its activity in vitro and in vivo.
Recommended Citation
Roy, H. and Ibba, M. (2008) Monitoring Lys-tRNALys phosphatidylglycerol transferase activity. Methods 44, 164-169. https://doi.org10.1016/j.ymeth.2007.09.002
Copyright
Elsevier
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
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Comments
NOTICE: this is the author’s version of a work that was accepted for publication in Methods. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Methods, volume 44, in 2008. https://doi.org/10.1016/j.ymeth.2007.09.002
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