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AEM Accepts, published online ahead of print on 12 October 2007
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Appl. Environ. Microbiol. doi:10.1128/AEM.01861-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Expression of Mycoplasma proteins carrying an affinity tag in M. pneumoniae allows rapid purification and circumvents problems related to the abberant genetic code

Sebastian R. Schmidl, Claudine Hames, and Jörg Stülke*

Department of General Microbiology, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany

* To whom correspondence should be addressed. Email: jstuelk{at}gwdg.de.


  Abstract

In Mycoplasma pneumoniae and several other mollicutes, the UGA opal codon specifies tryptophan rather than a translation stop. This makes it often difficult to express Mycoplasma proteins in heterologous hosts. In this work, we demonstrate that mollicute proteins can be fused to an affinity tag and be expressed directly in M. pneumoniae. The protein can than be purified by affinity chromatography and be used for biochemical or any other desired analysis.




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