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Structural and functional studies of the fusidic acid resistance protein fusB

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Structural and functional studies of the fusidic acid resistance protein fusB

Xiaohu Guo

Fusidic acid, first derived from the fungus Fusidium coccineum, is an antibiotic used against Staphylococcus aureus. It functions by blocking the release of elongation factor G (EF-G) from the ribosome, thus preventing the binding of a new aminoacyl tRNA to the ribosome and blocking the translation process. One resistance mechanism for S. aureus to fusidic acid involves a single gene fusB, carried by plasmid pUB101. The FusB

protein has been shown to interact with S. aureus EF-G but not with E. coli EF-G. Further, FusB confers fusidic-acid resistance to an S. aureus in vitro translation system, but fails from protecting an E. coli in vitro translation system from fusidic-acid inhibition. With

the aim of structure determination and biochemical studies of FusB and

the FusB-EF-G complex, we have cloned, expressed and purified FusB and S. aureus EF-G. FusB has been crystallized. The crystals diffract to 3.9

Å resolution and belong to space group P2

1

2

1

2. The crystals are being further optimized. We also study the in vitro interaction of S. aureus EF-G and FusB. Our results show that the FusB can not bind to S. aureus EF-G domainⅠtogether with domain Ⅱ, and probably functions by its interacting with domainⅤ.

Master degree project in applied biotechnology (45 hp), Master of Science (2 years), 2010

Biology Education Centre, Uppsala University, Department of Cell and Molecular Biology, Biomedical centre

Supervisor: Maria Selmer

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