Specific recognition of choline residues in the cell wall teichoic acid by the N-acetylmuramyl-L-alanine amidase of Pneumococcus.
Open accessAbstract
Pneumococci growing on choline-containing medium are known to incorporate this amino alcohol into the wall teichoic acid and produce autolysin-sensitive cell walls. In contrast, bacteria grown on the choline analogue, ethanolamine, incorporate ethanolamine into the teichoic acid and synthesize cell walls that are resistant to the homologous autolysin. In this communication, we report experiments aimed at understanding the biochemical mechanism of this phenomenon. Ethanolamine-containing (autolysin-resistant) cell walls were methylated in vitro with methyl iodide. Under appropriate conditions, virtually all of the ethanolamine residues could be converted to choline. After methylation, the formerly autolysin-resistant walls could be quantitatively hydrolyzed by the pneumococcal autolysin. Methylated walls also recovered another property typical of cell walls isolated from choline-grown bacteria: they could induce the in vitro "conversion" of an inactive form of autolysin to the catalytically active form (Tomasz, A., and Westphal, M. (1971) Proc. Natl. Acad. Sci. U.S.A. 68, 2627-2630). The results suggest that the autolysin-catalyzed hydrolysis of amide bonds in the peptidoglycan requires an additional interaction between the enzyme protein and choline residues in the teichoric acid portion of the cell wall.
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Binding of surface proteins to choline containing teichoic acids occurs in Streptococcus pneumoniae.
“(ii) Binding of surface proteins to choline containing teichoic acids (in Streptococcus pneumoniae) [9].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [9]
Cites
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Self-citationPneumococcal C-substance, a ribitol teichoic acid containing choline phosphate
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Self-citationThe N,O-Diacetylmuramidase of Chalaropsis Species
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Teichoic Acid Phosphorylcholine Esterase
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Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391 · see citing works
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Self-citationProtein sorting to the cell wall envelope of Gram-positive bacteria
Ton-That, H., Marraffini, L. A., & Schneewind, O. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.04.014 · Cited by 266 · see citing works
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Hussain, M., Becker, K., von Eiff, C., Schrenzel, J., Peters, G., & Herrmann, M. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.23.6778-6786.2001 · Cited by 149 · see citing works
- Authors
- Höltje, J. V., & Tomasz, A.
- Affiliations
- Rockefeller University (US)
- ORCID
- Tomasz, A
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1975-08
- Volume
- 250
- Issue
- 15
- Pages
- 6072-6076
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1601451310
- Cited by
- 131
- References
- 15
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 2 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 3 · 2016: 1 · 2014: 5 · 2013: 1 · 2012: 2
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Keywords
- choline incorporation, N-acetylmuramyl-L-alanine amidase, monoethanolamine, methyl iodide, peptidoglycan hydrolysis, enzyme activation, Streptococcus pneumoniae
- MeSH terms
- Alanine, Amidohydrolases, Amino Acids, Cell Wall, Choline, Chromatography, Gel, Chromatography, Ion Exchange, Chromatography, Thin Layer, Ethanolamines, Galactosamine, Glucosamine, Hydrolysis, Kinetics, Muramic Acids, Phosphorylcholine, Streptococcus pneumoniae, Teichoic Acids, Time Factors
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