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YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids


Sulfoquinovose is produced by photosynthetic organisms at a rate of 1010 tons per annum and is degraded by bacteria as a source of carbon and sulfur. We have identified Escherichia coli YihQ as the first dedicated sulfoquinovosidase and the gateway enzyme to sulfoglycolytic pathways. Structural and mutagenesis studies unveiled the sequence signatures for binding the distinguishing sulfonate residue and revealed that sulfoquinovoside degradation is widespread across the tree of life.

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Figure 1: E. coli YihQ is a sulfoquinovosidase that hydrolyzes SQDG to SQ.
Figure 2: Structural identification of SQ-binding residues.

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  1. Harwood, J.L. & Nicholls, R.G. Biochem. Soc. Trans. 7, 440–447 (1979).

    CAS  Article  Google Scholar 

  2. Benning, C. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49, 53–75 (1998).

    CAS  Article  Google Scholar 

  3. Denger, K. et al. Nature 507, 114–117 (2014).

    CAS  Article  Google Scholar 

  4. Felux, A.K., Spiteller, D., Klebensberger, J. & Schleheck, D. Proc. Natl. Acad. Sci. USA 112, E4298–E4305 (2015).

    CAS  Article  Google Scholar 

  5. Shimojima, M. Prog. Lipid Res. 50, 234–239 (2011).

    CAS  Article  Google Scholar 

  6. Martelli, H.L. & Benson, A.A. Biochim. Biophys. Acta 93, 169–171 (1964).

    CAS  Article  Google Scholar 

  7. Roy, A.B., Hewlins, M.J., Ellis, A.J., Harwood, J.L. & White, G.F. Appl. Environ. Microbiol. 69, 6434–6441 (2003).

    CAS  Article  Google Scholar 

  8. Denger, K., Huhn, T., Hollemeyer, K., Schleheck, D. & Cook, A.M. FEMS Microbiol. Lett. 328, 39–45 (2012).

    CAS  Article  Google Scholar 

  9. Sugimoto, K., Sato, N. & Tsuzuki, M. FEBS Lett. 581, 4519–4522 (2007).

    CAS  Article  Google Scholar 

  10. Durham, B.P. et al. Proc. Natl. Acad. Sci. USA 112, 453–457 (2015).

    CAS  Article  Google Scholar 

  11. Shibuya, I. & Benson, A.A. Nature 192, 1186–1187 (1961).

    CAS  Article  Google Scholar 

  12. Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P.M. & Henrissat, B. Nucleic Acids Res. 42, D490–D495 (2014).

    CAS  Article  Google Scholar 

  13. Okuyama, M., Mori, H., Chiba, S. & Kimura, A. Protein Expr. Purif. 37, 170–179 (2004).

    CAS  Article  Google Scholar 

  14. Andersson, L., Carriére, F., Lowe, M.E., Nilsson, A. & Verger, R. Biochim. Biophys. Acta 1302, 236–240 (1996).

    Article  Google Scholar 

  15. Lee, S.S., Yu, S. & Withers, S.G. J. Am. Chem. Soc. 124, 4948–4949 (2002).

    CAS  Article  Google Scholar 

  16. McCarter, J.D. & Withers, S.G. J. Am. Chem. Soc. 118, 241–242 (1996).

    CAS  Article  Google Scholar 

  17. Quaroni, A. & Semenza, G. J. Biol. Chem. 251, 3250–3253 (1976).

    CAS  PubMed  Google Scholar 

  18. Okuyama, M. et al. Eur. J. Biochem. 268, 2270–2280 (2001).

    CAS  Article  Google Scholar 

  19. Davies, G.J., Planas, A. & Rovira, C. Acc. Chem. Res. 45, 308–316 (2012).

    CAS  Article  Google Scholar 

  20. Speciale, G., Thompson, A.J., Davies, G.J. & Williams, S.J. Curr. Opin. Struct. Biol. 28, 1–13 (2014).

    CAS  Article  Google Scholar 

  21. Tagami, T. et al. J. Biol. Chem. 288, 19296–19303 (2013).

    CAS  Article  Google Scholar 

  22. Studier, F.W. Protein Expr. Purif. 41, 207–234 (2005).

    CAS  Article  Google Scholar 

  23. Winter, G. J. Appl. Cryst. 43, 186–190 (2010).

    CAS  Article  Google Scholar 

  24. Collaborative Computational Project, Number 4. Acta Crystallogr. D Biol. Crystallogr. 50, 760–763 (1994).

  25. Celniker, G. et al. Isr. J. Chem. 53, 199–206 (2013).

    CAS  Article  Google Scholar 

  26. Ashkenazy, H., Erez, E., Martz, E., Pupko, T. & Ben-Tal, N. Nucleic Acids Res. 38, W529–W533 (2010).

    CAS  Article  Google Scholar 

  27. The PyMOL Molecular Graphics System version 1.7.4 (Schrödinger, LLC).

  28. McNicholas, S., Potterton, E., Wilson, K.S. & Noble, M.E.M. Acta Crystallogr. D Biol. Crystallogr. 67, 386–394 (2011).

    CAS  Article  Google Scholar 

  29. Dereeper, A. et al. Nucleic Acids Res. 36, W465–W469 (2008).

    CAS  Article  Google Scholar 

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We thank S.G. Withers for the gift of 5-fluoro-β-L-idopyranosyl fluoride and N.A. Williamson for technical assistance. This work was supported by grants from the UK Biotechnology and Biological Sciences Research Council and the European Research Council (AdG-322942 to G.J.D.), the Australian Research Council (to S.J.W.), the Ramaciotti Foundation and the Victorian Endowment for Science Knowledge and Innovation, with additional support from the Australian Cancer Research Foundation and Victorian State Government Operational Infrastructure Support, NHMRC IRIISS grant 9000220 (to E.D.G.-B.). We thank the Diamond Light Source (Didcot, UK) for access to beamlines IO4, IO4-1 and IO2 (proposal number mx-9948).

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Authors and Affiliations



G.S. synthesized substrate and performed LC/MS analysis. G.S. and E.D.G.-B. cloned, expressed, mutagenized and purified enzymes and performed kinetic analyses. Y.J. performed crystallographic studies and prepared the accompanying figures. Experiments were designed by G.J.D., S.J.W. and E.D.G.-B., who collectively wrote the paper.

Corresponding author

Correspondence to Ethan D Goddard-Borger.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Text and Figures

Supplementary Results, Supplementary Tables 1–3 and Supplementary Figures 1–7. (PDF 2820 kb)

Supplementary Note

Synthetic Procedures (PDF 529 kb)

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Speciale, G., Jin, Y., Davies, G. et al. YihQ is a sulfoquinovosidase that cleaves sulfoquinovosyl diacylglyceride sulfolipids. Nat Chem Biol 12, 215–217 (2016).

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