Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide

Sharypova LA, Niehaus K, Scheidle H, Holst O, Becker A (2003)
JOURNAL OF BIOLOGICAL CHEMISTRY 278(15): 12946-12954.

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Abstract
Lipid A is the hydrophobic anchor of lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria. Lipid A of all Rhizobiaceae is acylated with a long fatty acid chain, 27-hydroxyoctacosanoic acid. Biosynthesis of this long acyl substitution requires a special acyl carrier protein, AcpXL, which serves as a donor of C28 (omega-1)-hydroxylated fatty acid for acylation of rhizobial lipid A (Brozek, K.A., Carlson, R.W., and Raetz, C. R. (1996) J. BioL Chem 271,32126-32136). To determine the biological function of the C28 acylation of lipid A, we constructed an acpXL mutant of Sinorhizobium meliloti strain 1021. Gas-liquid chromatography and mass spectrometry analysis of the fatty acid composition showed that the acpXL mutation indeed blocked C28 acylation of lipid A. SDS-PAGE analysis of acpXL mutant LPS revealed only a fast migrating band, rough LPS, whereas the parental strain 1021 manifested both rough and smooth LPS. Regardless of this, the LPS of parental and mutant strains had a similar sugar composition and exposed the same antigenic epitopes, implying that different electrophoretic profiles might account for different aggregation properties of LPS molecules with and without a long acyl chain. The acpXL mutant of strain 1021 displayed sensitivity to deoxycholate, delayed nodulation of Medicago sativa, and a reduced competitive ability. However, nodules elicited by this mutant on roots of M. sativa and Medicago truncatula had a normal morphology and fixed nitrogen. Thus, the C28 fatty acid moiety of lipid A is not crucial, but it is beneficial for establishing an effective symbiosis with host plants. acpXL lies upstream from a cluster of five genes, including msbB (lpxXL), which might be also involved in biosynthesis and transfer of the C28 fatty acid to the lipid A precursor.
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Sharypova LA, Niehaus K, Scheidle H, Holst O, Becker A. Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide. JOURNAL OF BIOLOGICAL CHEMISTRY. 2003;278(15):12946-12954.
Sharypova, L. A., Niehaus, K., Scheidle, H., Holst, O., & Becker, A. (2003). Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(15), 12946-12954. doi:10.1074/jbc.M209389200
Sharypova, L. A., Niehaus, K., Scheidle, H., Holst, O., and Becker, A. (2003). Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide. JOURNAL OF BIOLOGICAL CHEMISTRY 278, 12946-12954.
Sharypova, L.A., et al., 2003. Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide. JOURNAL OF BIOLOGICAL CHEMISTRY, 278(15), p 12946-12954.
L.A. Sharypova, et al., “Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 278, 2003, pp. 12946-12954.
Sharypova, L.A., Niehaus, K., Scheidle, H., Holst, O., Becker, A.: Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide. JOURNAL OF BIOLOGICAL CHEMISTRY. 278, 12946-12954 (2003).
Sharypova, L. A., Niehaus, Karsten, Scheidle, H., Holst, O., and Becker, A. “Sinorhizobium meliloti acpXL mutant lacks the C28 hydroxylated fatty acid moiety of lipid A and does not express a slow migrating form of lipopolysaccharide”. JOURNAL OF BIOLOGICAL CHEMISTRY 278.15 (2003): 12946-12954.
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