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Microbiology 149 (2003), 2733-2738; DOI  10.1099/mic.0.26315-0
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Microbiology 149 (2003), 2733-2738; DOI  10.1099/mic.0.26315-0
© 2003 Society for General Microbiology

Application of a bacterial two-hybrid system for the analysis of protein–protein interactions between FemABX family proteins

Susanne Rohrer and Brigitte Berger-Bächi

University of Zürich, Institute of Medical Microbiology, Gloriastr. 32, CH-8028 Zürich, Switzerland

Correspondence
Brigitte Berger-Bächi
bberger{at}immv.unizh.ch

Protein–protein interactions play an important role in all cellular processes. The development of two-hybrid systems in yeast and bacteria allows for in vivo assessment of such interactions. Using a recently developed bacterial two-hybrid system, the interactions of the Staphylococcus aureus proteins FemA, FemB and FmhB, members of the FemABX protein family, which is involved in peptidoglycan biosynthesis and {beta}-lactam resistance of numerous Gram-positive bacteria, were analysed. While FmhB is involved in the addition of glycine 1 of the pentaglycine interpeptide of S. aureus peptidoglycan, FemA and FemB are specific for glycines 2/3 and 4/5, respectively. FemA–FemA, FemA–FemB and FemB–FemB interactions were found, while FmhB exists solely as a monomer. Interactions detected by the bacterial two-hybrid system were confirmed using the glutathione S-transferase-pulldown assay and gel filtration.

Abbreviations: BTH, bacterial two-hybrid; GST, glutathione S-transferase; His6, hexahistidine; HRP, horseradish peroxidase




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Staphylococcus research
Microbiology, October 1, 2003; 149(10): 2697 - 2699.
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