A new glycosylated lipopeptide incorporated into the cell wall of a smooth variant of Gordona hydrophobica
Autor(en): | Moormann, M Zahringer, U Moll, H Kaufmann, R Schmid, R Altendorf, K |
Stichwörter: | Biochemistry & Molecular Biology; BIOFILTERS; CHROMATOGRAPHY; MYCOBACTERIA; PERFORMANCE; ROUGH | Erscheinungsdatum: | 1997 | Herausgeber: | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Journal: | JOURNAL OF BIOLOGICAL CHEMISTRY | Volumen: | 272 | Ausgabe: | 16 | Startseite: | 10729 | Seitenende: | 10738 | Zusammenfassung: | A cell wall component of a smooth variant of Gordona hydrophobica 1775/15 was isolated and purified, and its structure was determined by various chemical methods, including chemical synthesis of part structures, Edman degradation, gas chromatography/mass spectrometry analysis, matrix-assisted laser desorption ionization-post-source decay (MALDI-PSD) tandem mass spectrometry, and H-1 and C-13 NMR using one- and two-dimensional, homo- and heteronuclear correlated spectroscopy. The cell wall component was found to be a (mono-) glycosylated peptidolipid (GPL) consisting of a tridecapeptide interlinked by a beta-hydroxylated fatty acid (3-hydroxyeicosanoic acid, 20:0 (3-OH) to form a cyclic lactone ring structure. The main fraction of GPL, for which we propose the name gordonin, was identified as 3-hydroxyeicosanoyl-L-seryl-L-phenylalanyl-L-seryl-L-seryl-D-alanyl-L-(O -beta-D-glucopyranosyl)-threyonyl-glycyl-D-leucyl-L-valyl-L-seryl-L-phen ylalanyl-glycyl-L-valyl lactone. The other GPLs constitute structural variations within the nature of the beta-hydroxylated fatty acid (20:0(3-OH) versus 22:1(3-OH)) in a ratio of about 1:0.9 as well as within one amino acid (D-Leu versus L-Phe) in about 30%. Sequence information was obtained in part by Edman degradation as well as gas chromatography/mass spectrometry analysis of di- and tripeptide fragments. However, the complete amino acid sequence could only be established by MALDI-PSD from the linear molecule, i.e. after ring opening of the lactone. In contrast, rough variants of G. hydrophobica 1775/15 lack these peptidolipids or synthesize them to a much lesser extent indicating that gordonin contributes significantly to the physicochemical character of the cell surface. |
ISSN: | 00219258 |
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