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Applied and Environmental Microbiology, December 2007, p. 7799-7801, Vol. 73, No. 23
0099-2240/07/$08.00+0     doi:10.1128/AEM.01861-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Expression of Mycoplasma Proteins Carrying an Affinity Tag in M. pneumoniae Allows Rapid Purification and Circumvents Problems Related to the Aberrant Genetic Code{triangledown}

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

Received 10 August 2007/ Accepted 2 October 2007

In Mycoplasma pneumoniae and several other mollicutes, the UGA opal codon specifies tryptophan rather than a translation stop. This often makes it 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 then be purified by affinity chromatography and be used for biochemical or any other desired analysis.

* Corresponding author. Mailing address: Department of General Microbiology, Institute of Microbiology and Genetics, Georg-August University Göttingen, Grisebachstr. 8, D-37077 Göttingen, Germany. Phone: 49-551-393781. Fax: 49-551-393808. E-mail: jstuelk{at}gwdg.de

{triangledown} Published ahead of print on 12 October 2007.

Applied and Environmental Microbiology, December 2007, p. 7799-7801, Vol. 73, No. 23
0099-2240/07/$08.00+0     doi:10.1128/AEM.01861-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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