Details

Autor(en) / Beteiligte

• Moormann, Michael
• Zähringer, Ulrich
• Moll, Hermann
• Kaufmann, Raimund
• Schmid, Roland
• Altendorf, Karlheinz

Titel

A New Glycosylated Lipopeptide Incorporated into the Cell Wall of a Smooth Variant of Gordona hydrophobica

Ist Teil von

• The Journal of biological chemistry, 1997-04, Vol.272 (16), p.10729-10738

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1997

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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 1 H and 13 C 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 β-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 -β- d -glucopyranosyl)-threonyl-glycyl- d -leucyl- l -valyl- l -seryl- l -phenylalanyl-glycyl- l -valyl lactone. The other GPLs constitute structural variations within the nature of the β-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.