Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-Autonomously

Nature Microbiology

Volumn 1, Issue , 2016, Pages

  Cho, Hongbaek ^a,c   Wivagg, Carl N ^a,c   Kapoor, Mrinal ^b,c   Barry, Zachary ^b   Rohs, Patricia D A ^a   Suh, Hyunsuk ^a   Marto, Jarrod A ^a,c   Garner, Ethan C ^a   Bernhardt, Thomas G ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b HARVARD UNIVERSITY   (United States)

^c DANA FARBER CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84988358297     PISSN: None     EISSN: 20585276     Source Type: Journal    
DOI: 10.1038/nmicrobiol.2016.172     Document Type: Article

References (40)

1. Typas, A., Banzhaf, M., Gross, C. A. & Vollmer, W. From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat. Rev. Microbiol. 10, 123-136 (2012).
2. McKenna, M. Antibiotic resistance: The last resort. Nature 499, 394-396 (2013).
3. Jones, L. J., Carballido-López, R. & Errington, J. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104, 913-922 (2001).
4. Garner, E. C. et al. Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333, 222-225 (2011).
5. Domínguez-Escobar, J. et al. Processive movement of MreB-Associated cell wall biosynthetic complexes in bacteria. Science 333, 225-228 (2011).
6. van Teeffelen, S. et al. The bacterial actin MreB rotates, and rotation depends on cell-wall assembly. Proc. Natl Acad. Sci. USA 108, 15822-15827 (2011).
7. Ursell, T. S. et al. Rod-like bacterial shape is maintained by feedback between cell curvature and cytoskeletal localization. Proc. Natl Acad. Sci. USA 111, E1025-E1034 (2014).
8. Bi, E. F. & Lutkenhaus, J. FtsZ ring structure associated with division in Escherichia coli. Nature 354, 161-164 (1991).
9. Yousif, S. Y., Broome-Smith, J. K. & Spratt, B. G. Lysis of Escherichia coli by betalactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B. J. Gen. Microbiol. 131, 2839-2845 (1985).
10. Hoskins, J. et al. Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae. J. Bacteriol. 181, 6552-6555 (1999).
11. Paik, J., Kern, I., Lurz, R. & Hakenbeck, R. Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. J. Bacteriol. 181, 3852-3856 (1999).
12. Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A. & Charlier, P. The penicillinbinding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol. Rev. 32, 234-258 (2008).
13. McPherson, D. C. & Popham, D. L. Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis. J. Bacteriol. 185, 1423-1431 (2003).
14. Rice, L. B. et al. Role of class A penicillin-binding proteins in the expression of beta-lactam resistance in Enterococcus faecium. J. Bacteriol. 191, 3649-3656 (2009).
15. Cho, H., Uehara, T. & Bernhardt, T. G. Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery. Cell 159, 1300-1311 (2014).
16. Uehara, T. & Park, J. T. Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation. J. Bacteriol. 190, 3914-3922 (2008).
17. Sham, L.-T. et al. Bacterial cell wall. MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345, 220-222 (2014).
18. Meeske, A. J. et al. SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature http://dx.doi.org/10.1038/nature19331 (2016).
19. Fay, A., Meyer, P. & Dworkin, J. Interactions between late-Acting proteins required for peptidoglycan synthesis during sporulation. J. Mol. Biol. 399, 547-561 (2010).
20. Fraipont, C. et al. The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli. Microbiology 157, 251-259 (2011).
21. Lee, T. K. et al. A dynamically assembled cell wall synthesis machinery buffers cell growth. Proc. Natl Acad. Sci. USA 111, 4554-4559 (2014).
22. Varma, A., de Pedro, M. A. & Young, K. D. FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 189, 5692-5704 (2007).
23. Tan, Q., Awano, N. & Inouye, M. YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB. Mol. Microbiol. 79, 109-118 (2011).
24. Curtis, N. A., Orr, D., Ross, G. W. & Boulton, M. G. Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity. Antimicrob. Agents Chemother. 16, 533-539 (1979).
25. Grimm, J. B. et al. A general method to improve fluorophores for live-cell and single-molecule microscopy. Nat. Methods 12, 244-250 (2015).
26. Vrljic, M., Nishimura, S. Y., Brasselet, S., Moerner, W. E. & McConnell, H. M. Translational diffusion of individual class II MHC membrane proteins in cells. Biophys. J. 83, 2681-2692 (2002).
27. Schötz, G. J., Schindler, H. & Schmidt, T. Single-molecule microscopy on model membranes reveals anomalous diffusion. Biophys. J. 73, 1073-1080 (1997).
28. Baba, T. et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection. Mol. Syst. Biol. 2, 2006.0008 (2006).
29. Sung, M.-T. et al. Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Proc. Natl Acad. Sci. USA 106, 8824-8829 (2009).
30. Cho, H., McManus, H. R., Dove, S. L. & Bernhardt, T. G. Nucleoid occlusion factor SlmA is a DNA-Activated FtsZ polymerization antagonist. Proc. Natl Acad. Sci. USA 108, 3773-3778 (2011).
31. Warming, S., Costantino, N., Court, D. L., Jenkins, N. A. & Copeland, N. G. Simple and highly efficient BAC recombineering using galK selection. Nucleic Acids Res. 33, e36-e36 (2005).
32. Datsenko, K. A. &Wanner, B. L. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl Acad. Sci. USA 97, 6640-6645 (2000).
33. Yu, D. et al. An efficient recombination system for chromosome engineering in Escherichia coli. Proc. Natl Acad. Sci. USA 97, 5978-5983 (2000).
34. Ficarro, S. B. et al. Improved electrospray ionization efficiency compensates for diminished chromatographic resolution and enables proteomics analysis of tyrosine signaling in embryonic stem cells. Anal. Chem. 81, 3440-3447 (2009).
35. Askenazi, M., Parikh, J. R. & Marto, J. A. mzAPI a new strategy for efficiently sharing mass spectrometry data. Nat. Methods 6, 240-241 (2009).
36. Ursell, T. S. et al. Rod-like bacterial shape is maintained by feedback between cell curvature and cytoskeletal localization. Proc. Natl Acad. Sci. USA 111, E1025-1034 (2014).
37. Schindelin, J. et al. Fiji: An open-source platform for biological-image analysis. Nat. Methods 9, 676-682 (2012).
38. Schneider, C. A., Rasband, W. S. & Eliceiri, K.W. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675 (2012).
39. Gibson, D. G. et al. Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat. Methods 6, 343-345 (2009).
40. Jaqaman, K. et al. Robust single-particle tracking in live-cell time-lapse sequences. Nat. Methods 5, 695-702 (2008).