Specific amino acid substitutions in the proline-rich motif of the Rhizobium meliloti exoP protein result in enhanced production of low- molecular-weight succinoglycan at the expense of high-molecular-weight succinoglycan

Abstract

The production of the acidic exopolysaccharide succinoglycan (EPS I) by Rhizobium meliloti exoP* mutants expressing an ExoP protein lacking its C- terminal cytoplasmic domain and by mutants characterized by specific amino acid substitutions in the proline-rich motif (RX4PX2PX4SPKX9IXGXMXGXG) located from positions 443 to 476 of the ExoP protein was analyzed. The absence of the C-terminal cytoplasmic ExoP domain (positions 484 to 786) and the substitution of both arginine443 by isoleucine443 and proline457 by serine457 within the proline-rich motif resulted in enhanced production of low-molecular-weight (LMW) EPS I at the expense of high-molecular-weight (HMW) EPS I. The ratios of HMW to LMW EPS I of the wild type and mutant strains increased with osmolarity.