The outer membrane protein TolC from Sinorhizobium meliloti affects protein secretion, polysaccharide biosynthesis, antimicrobial resistance, and symbiosis.

Sinorhizobium meliloti is capable of establishing a symbiotic nitrogen fixation relationship with Medicago sativa. During this process, it must cope with diverse environments and has evolved different types of transport systems that help its propagation in the plant roots. TolC protein family members are the outer-membrane components of several transport systems involved in the export of diverse molecules, playing an important role in bacterial survival.

Recent advances in studies on structure and symbiosis-related function of rhizobial K-antigens and lipopolysaccharides.

Exopolysaccharides (EPSs) and K polysaccharides (K-antigens, capsular polysaccharides, or KPSs) are important for the recognition of the symbiotic partner and the infection process, whereas lipopolysaccharides (LPSs) may function at a later stage of symbiosis. Recently, considerable progress has been made in the structural investigation of rhizobial K-antigens and LPSs. This structural data, together with the availability of more and more mutant data, allows new insights into the structure-function relationships of surface polysaccharides and the mode of their action on host cells.

Striking complexity of lipopolysaccharide defects in a collection of Sinorhizobium meliloti mutants.

Although the role that lipopolysaccharide (LPS) plays in the symbiosis between Sinorhizobium meliloti and alfalfa has been studied for over a decade, its function in this process remains controversial and poorly understood. This is largely due to a lack of mutants affected by its synthesis. In one of the definitive studies concerning this issue, Clover 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.

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.

Diversity of Sinorhizobium meliloti from the Central Asian Alfalfa Gene Center.

Sinorhizobium meliloti was isolated from nodules and soil from western Tajikistan, a center of diversity of the host plants (Medicago, Melilotus, and Trigonella species). There was evidence of recombination, but significant disequilibrium, between and within the chromosome and megaplasmids. The most frequent alleles matched those in the published genome sequence.