This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Atrih, A.
Right arrow Articles by Foster, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Atrih, A.
Right arrow Articles by Foster, S. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 1998, p. 4603-4612, Vol. 180, No. 17
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Peptidoglycan Structural Dynamics during Germination of Bacillus subtilis 168 Endospores

Abdelmadjid Atrih,1 Peter Zöllner,2 Günter Allmaier,2 Michael P. Williamson,1 and Simon J. Foster1,*

Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom,1 and Institute for Analytical Chemistry, University of Vienna, A-1090 Vienna, Austria2

Received 5 May 1998/Accepted 17 June 1998

Peptidoglycan structural dynamics during endospore germination of Bacillus subtilis 168 have been examined by muropeptide analysis. The first germination-associated peptidoglycan structural changes are detected within 3 min after the addition of the specific germinant L-alanine. We detected in the spore-associated material new muropeptides which, although they have slightly longer retention times by reversed-phase (RP)-high-pressure liquid chromatography (HPLC) than related ones in dormant spores, show the same amino acid composition and molecular mass. Two-dimensional nuclear magnetic resonance (NMR) analysis shows that the chemical changes to the muropeptides on germination are minor and are probably limited to stereochemical inversion. These new muropeptides account for almost 26% of the total muropeptides in spore-associated material after 2 h of germination. The exudate of germinated spores of B. subtilis 168 contains novel muropeptides in addition to those present in spore-associated material. Exudate-specific muropeptides have longer retention times, have no reducing termini, and exhibit a molecular mass 20 Da lower than those of related reduced muropeptides. These new products are anhydro-muropeptides which are generated by a lytic transglycosylase, the first to be identified in a gram-positive bacterium. There is also evidence for the activity of a glucosaminidase during the germination process. Quantification of muropeptides in spore-associated material indicates that there is a heterogeneous distribution of muropeptides in spore peptidoglycan. The spore-specific residue, muramic delta -lactam, is proposed to be a major substrate specificity determinant of germination-specific lytic enzymes, allowing cortex hydrolysis without any effect on the primordial cell wall.

* Corresponding author. Mailing address: Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, United Kingdom. Phone: 44 114 282 4411. Fax: 44 114 272 8697. E-mail: s.foster{at}sheffield.ac.uk.

Journal of Bacteriology, September 1998, p. 4603-4612, Vol. 180, No. 17
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Boniface, A., Parquet, C., Arthur, M., Mengin-Lecreulx, D., Blanot, D. (2009). The Elucidation of the Structure of Thermotoga maritima Peptidoglycan Reveals Two Novel Types of Cross-link. J. Biol. Chem. 284: 21856-21862 [Abstract] [Full Text]  
  • Heffron, J. D., Orsburn, B., Popham, D. L. (2009). Roles of Germination-Specific Lytic Enzymes CwlJ and SleB in Bacillus anthracis. J. Bacteriol. 191: 2237-2247 [Abstract] [Full Text]  
  • Lambert, E. A., Popham, D. L. (2008). The Bacillus anthracis SleL (YaaH) Protein Is an N-Acetylglucosaminidase Involved in Spore Cortex Depolymerization. J. Bacteriol. 190: 7601-7607 [Abstract] [Full Text]  
  • Dowd, M. M., Orsburn, B., Popham, D. L. (2008). Cortex Peptidoglycan Lytic Activity in Germinating Bacillus anthracis Spores. J. Bacteriol. 190: 4541-4548 [Abstract] [Full Text]  
  • Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
  • Stenbak, C. R., Ryu, J.-H., Leulier, F., Pili-Floury, S., Parquet, C., Herve, M., Chaput, C., Boneca, I. G., Lee, W.-J., Lemaitre, B., Mengin-Lecreulx, D. (2004). Peptidoglycan Molecular Requirements Allowing Detection by the Drosophila Immune Deficiency Pathway. J. Immunol. 173: 7339-7348 [Abstract] [Full Text]  
  • Gilmore, M. E., Bandyopadhyay, D., Dean, A. M., Linnstaedt, S. D., Popham, D. L. (2004). Production of Muramic {delta}-Lactam in Bacillus subtilis Spore Peptidoglycan. J. Bacteriol. 186: 80-89 [Abstract] [Full Text]  
  • Wei, Y., McPherson, D. C., Popham, D. L. (2004). A Mother Cell-Specific Class B Penicillin-Binding Protein, PBP4b, in Bacillus subtilis. J. Bacteriol. 186: 258-261 [Abstract] [Full Text]  
  • Horsburgh, G. J., Atrih, A., Foster, S. J. (2003). Characterization of LytH, a Differentiation-Associated Peptidoglycan Hydrolase of Bacillus subtilis Involved in Endospore Cortex Maturation. J. Bacteriol. 185: 3813-3820 [Abstract] [Full Text]  
  • Fukushima, T., Yamamoto, H., Atrih, A., Foster, S. J., Sekiguchi, J. (2002). A Polysaccharide Deacetylase Gene (pdaA) Is Required for Germination and for Production of Muramic {delta}-Lactam Residues in the Spore Cortex of Bacillus subtilis. J. Bacteriol. 184: 6007-6015 [Abstract] [Full Text]  
  • Chirakkal, H., O'Rourke, M., Atrih, A., Foster, S. J., Moir, A. (2002). Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination. Microbiology 148: 2383-2392 [Abstract] [Full Text]  
  • Atrih, A., Foster, S. J. (2001). In vivo roles of the germination-specific lytic enzymes of Bacillus subtilis 168. Microbiology 147: 2925-2932 [Abstract] [Full Text]  
  • McPherson, D. C., Driks, A., Popham, D. L. (2001). Two Class A High-Molecular-Weight Penicillin-Binding Proteins of Bacillus subtilis Play Redundant Roles in Sporulation. J. Bacteriol. 183: 6046-6053 [Abstract] [Full Text]  
  • Catalano, F. A., Meador-Parton, J., Popham, D. L., Driks, A. (2001). Amino Acids in the Bacillus subtilis Morphogenetic Protein SpoIVA with Roles in Spore Coat and Cortex Formation. J. Bacteriol. 183: 1645-1654 [Abstract] [Full Text]  
  • Chen, Y., Fukuoka, S., Makino, S. (2000). A Novel Spore Peptidoglycan Hydrolase of Bacillus cereus: Biochemical Characterization and Nucleotide Sequence of the Corresponding Gene, sleL. J. Bacteriol. 182: 1499-1506 [Abstract] [Full Text]  
  • Smith, T. J., Blackman, S. A., Foster, S. J. (2000). Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146: 249-262 [Full Text]  
  • Boland, F. M., Atrih, A., Chirakkal, H., Foster, S. J., Moir, A. (2000). Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB. Microbiology 146: 57-64 [Abstract] [Full Text]  
  • Popham, D. L., Meador-Parton, J., Costello, C. E., Setlow, P. (1999). Spore Peptidoglycan Structure in a cwlD dacB Double Mutant of Bacillus subtilis. J. Bacteriol. 181: 6205-6209 [Abstract] [Full Text]  
  • Atrih, A., Bacher, G., Allmaier, G., Williamson, M. P., Foster, S. J. (1999). Analysis of Peptidoglycan Structure from Vegetative Cells of Bacillus subtilis 168 and Role of PBP 5 in Peptidoglycan Maturation. J. Bacteriol. 181: 3956-3966 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»