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J. Bacteriol., Jan 1998, 395-399, Vol 180, No. 2
Copyright © 1998, American Society for Microbiology

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 [In Process Citation]

A Becker and A Puhler
Lehrsthul fur Genetik, Fakultat fur Biologie, Universitat Bielefeld, Germany. hippo@genetik.uni-bielefeld.de

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.


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