Cited by 131Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationBacteriophages and microbial interactions

Specific recognition of choline residues in the cell wall teichoic acid by the N-acetylmuramyl-L-alanine amidase of Pneumococcus.

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Höltje, J V, Tomasz, A·1975·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1016/s0021-9258(19)41160-5

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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].”

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Authors
Höltje, J. V., & Tomasz, A.
Affiliations
Rockefeller University (US)
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
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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