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Edited by Christopher T. Walsh, Harvard Medical School, Boston, MA, and approved December 22, 2011 (received for review October 24, 2011)
Abstract
Resistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-mediated inhibition by an unknown mechanism. Here we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains a four-cysteine zinc finger with a unique structural fold. This domain mediates a high-affinity interaction with the C-terminal domains of EF-G. By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosome·EF-G·GDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation. Ribosome clearance by these proteins represents a highly unusual antibiotic resistance mechanism, which appears to be fine-tuned by the relative abundance of FusB-type protein, ribosomes, and EF-G.
Footnotes
- ↵1To whom correspondence should be addressed. E-mail: a.j.oneill{at}leeds.ac.uk.
Author contributions: M.V.R., W.W., S.W.H., T.A.E., and A.J.O. designed research; G.C., G.S.T., F.P., A.S., and A.J.O. performed research; G.C., G.S.T., H.T.J., F.P., A.S., M.V.R., W.W., T.A.E., and A.J.O. analyzed data; and G.C. and A.J.O. wrote the paper.
The authors declare no conflict of interest.
Data deposition: The coordinates of FusC reported in this paper have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2yb5) and the FusB chemical shift data reported in this paper have been deposited in the BioMagResBank, www.bmrb.wisc.edu (accession no. 17503).
This article is a PNAS Direct Submission.
This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1117275109/-/DCSupplemental.
Freely available online through the PNAS open access option.
Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid
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