11 Mar 2012

THE Bioengineering Project to produce Industrially Helpful Microbes to produce Biofuels




Engineering Microbial Surfaces for Biofuel Production

Dwindling world supplies connected with petroleum possess become more intense the particular search for choice causes of transportation energy. Alternative along with sustainable biofuels made out of lignocellulosic biomass are especially guaranteeing alternatives. In order to cost-efficiently develop these kinds of biofuels brand-new approaches are expected to help alter lignocellulosic biomass in fermentable sugars. One encouraging method is by using microbial multi-enzyme cellulosome complexes in order to decay biomass. Cellulosomes could often provide as purified complexes or while different parts of microorganisms that will straight ferment biomass straight into biofuels. To facilitate his or her optimization in addition to application, i am creating methods to show off cellulosome chimeras at first glance involving M. Subtilis, any model organism that's highly amenable to be able to genetic tricks and well-suited pertaining to commercial apps.

REFERENCES

1. Chambers, H.F. & Deleo, F.R. Waves of resistance: Staphylococcus aureus in the antibiotic era. Nat Rev Microbiol 7, 629-41 (2009).

2. Klevens, R.M. Et al. Invasive methicillin-resistant Staphylococcus aureus infections in the United States. Jama 298, 1763-71 (2007).

3. Lowry, F.D. Staphylococcus aureus infections. New England Journal of Medicine 339, 520-532 (1998).

4. Comfort, D. & Clubb, R.T. A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria. Infect Immun 72, 2710-22 (2004).

5. Connolly, K.M. & Clubb, R.T. Sortase Pathways in Gram-Positive Bacteria. In Structural Biology of Bacterial Pathogenesis (eds. Waksman, G. & Caparon, M.) (Wiley, New York, 2004).

6. Connolly, K.M. Et al. Sortase from Staphylococcus aureus does not contain a thiolate-imidazolium ion pair in its active site. J Biol Chem 278, 34061-5 (2003).

7. Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O. & Clubb, R.T. Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc Natl Acad Sci U S A 98, 6056-61 (2001).

8. Jung, M.E. Et al. Synthesis of (2R,3S) 3-amino-4-mercapto-2-butanol, a threonine analogue for covalent inhibition of sortases. Bioorg Med Chem Lett 15, 5076-9 (2005).

9. Liew, C.K. Et al. Localization and mutagenesis of the sorting signal binding site on sortase A from Staphylococcus aureus. FEBS Lett 571, 221-6 (2004).

10. Naik, M.T. Et al. Staphylococcus aureus Sortase A transpeptidase. Calcium promotes sorting signal binding by altering the mobility and structure of an active site loop. J Biol Chem 281, 1817-26 (2006).

11. Suree, N., Jung, M.E. & Clubb, R.T. Recent advances towards new anti-infective agents that inhibit cell surface protein anchoring in Staphylococcus aureus and other gram-positive pathogens. Mini Rev Med Chem 7, 991-1000 (2007).

12. Suree, N. Et al. The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized. J Biol Chem 284, 24465-77 (2009).

13. Suree, N. Et al. Discovery and structure-activity relationship analysis of Staphylococcus aureus sortase A inhibitors. Bioorg Med Chem 17, 7174-85 (2009).

14. Weiner, E.M., Robson, S.A., Marohn, M. & Clubb, R.T. The sortase A enzyme that attaches proteins to the cell wall of B. Anthracis contains an unusual active site architecture. J Biol Chem.

15. Yeates, T.O. & Clubb, R.T. Biochemistry. How some pili pull. Science 318, 1558-9 (2007).

16. Pilpa, R.M. Et al. Solution structure of the NEAT (NEAr Transporter) domain from IsdH/HarA: The human hemoglobin receptor in Staphylococcus aureus. J Mol Biol 360, 435-47 (2006).

17. Pilpa, R.M. Et al. Functionally distinct NEAT (NEAr Transporter) domains within the Staphylococcus aureus IsdH/HarA protein extract heme from methemoglobin. J Biol Chem 284, 1166-76 (2009).

18. Robson, S.A., Peterson, R., Bouchard, L.S., Villareal, V.A. & Clubb, R.T. A Heteronuclear Zero Quantum Coherence N(z)-Exchange Experiment That Resolves Resonance Overlap and Its Application To Measure the Rates of Heme Binding to the IsdC Protein. J Am Chem Soc (2010).

19. Villareal, V.A., Pilpa, R.M., Robson, S.A., Fadeev, E.A. & Clubb, R.T. The IsdC protein from Staphylococcus aureus uses a flexible binding pocket to capture heme. J Biol Chem 283, 31591-600 (2008).

20. Clancy, K.W., Melvin, J.A. & McCafferty, D.G. Sortase transpeptidases: Insights into mechanism, substrate specificity, and inhibition. Biopolymers 94, 385-96.

21. Maresso, A.W. & Schneewind, O. Sortase as a target of anti-infective therapy. Pharmacol Rev 60, 128-41 (2008).

22. Maresso, A.W. & Schneewind, O. Iron acquisition and transport in Staphylococcus aureus. Biometals 19, 193-203 (2006).

23. Mazmanian, S.K. Et al. Passage of heme-iron across the envelope of Staphylococcus aureus. Science 299, 906-9 (2003).

24. Skaar, E.P. & Schneewind, O. Iron-regulated surface determinants (Isd) of Staphylococcus aureus: Stealing iron from heme. Microbes Infect 6, 390-7 (2004).

25. Liu, M. Et al. Direct hemin transfer from IsdA to IsdC in the iron-regulated surface determinant (Isd) heme acquisition system of Staphylococcus aureus. J Biol Chem 283, 6668-76 (2008).

26. Zhu, H. Et al. Pathway for heme uptake from human methemoglobin by the iron-regulated surface determinants system of Staphylococcus aureus. J Biol Chem 283, 18450-60 (2008).


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