Die Beeinflussung der Aminosäuresequenz des serinhaltigen Mureins von Staphylococcus epidermidis Stamm 24 durch die Nährbodenzusammensetzung

Translated title of the contribution: The effect of nutrition on the amino acid sequence of the serine containing murein of Staphylococcus epidermis strain 24

K. H. Schleifer, L. Huss, O. Kandler

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

The murein (peptidoglycan) of S. epidermidis strain 24 contains Mur GlcNH2, Ala, Glu, Lys, Gly, Ser at a molar ratio of about 1:1:2.4:1:1:4.2:0.6 when grown in a yeast extract dextrose medium. Glutamic acid occurs as an amide. The amino acid sequence was determined by analysing the oligopeptides from partial acid hydrolysate. The tetrapeptide bound to the muramic acid (l-Ala-d-Glu-NH2-l-Lys-d-Ala) is identical with those found in S. aureus and S. epidermidis strain 66. About 1/3 of the muropeptides is still present as pentapeptides, since the second d-alanine of the muramyl pentapeptide precursor is not split off. This fact is indicated by the ratio of l-Ala/d-Ala of 1:1.3, the isolation of muropentapeptides from the lysozyme lysates and by the result of the hydrazinolysis. About 50% of the pentaglycine interpeptide chains contain one mole of l-serine. The exact position of l-serine could not be determined. However, it could be shown, that serine is never bound to the e{open}-amino group of lysine. In very rare cases, the e{open}-amino group of lysine is substituted by l-alanine which remains N-terminal and can not be used for crosslinkages. As shown by dinitrophenylation, about 3.5% of the e{open}-amino groups of lysine is free and about 50% of the interpeptide chains are not cross-linked. If the organism is grown in a glycine deficient minimal medium, the glycine content of the murein drops by 40%, while l-alanine increases. Here, about 15% of the e{open}-amino groups of lysine is substituted by l-alanine, which again is not used for cross-linkages. Another 35% of the e{open}-amino groups of lysine remain free. From the existing interpeptide chains 30% are not cross-linked. The addition of glycine to the minimal medium causes an increase of the glycine content in the murein, however, the extra alanine protion nearly disappears. The addition of serine leads to an increase of not only the serine portion but also the glycine portion in the murein. However, when alanine is added the alanine portion of murein is slightly increased and the glycine portion further decreased. The results of these experiments were compared to corresponding preliminary experiments with S. epidermidis (strain 66) and S. aureus (strain Copenhagen). In spite of modificative changes in the murein composition, clear genetical differences between the 3 strains were obvious.

Translated title of the contributionThe effect of nutrition on the amino acid sequence of the serine containing murein of Staphylococcus epidermis strain 24
Original languageGerman
Pages (from-to)387-404
Number of pages18
JournalArchiv für Mikrobiologie
Volume68
Issue number4
DOIs
StatePublished - Dec 1969
Externally publishedYes

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