PMID: 9440529Jan 24, 1998Paper

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

Journal of Bacteriology
A Becker, A Pühler

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.

References

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Citations

Oct 6, 2000·Annual Review of Microbiology·H P Spaink
May 25, 2002·Molecular Plant-microbe Interactions : MPMI·Andrzej MazurAnna Skorupska
Nov 18, 2004·The Journal of Biological Chemistry·Stefan BergPatrick J Brennan
Nov 13, 1998·Proceedings of the National Academy of Sciences of the United States of America·J E GonzálezG C Walker
Apr 24, 2007·Applied and Environmental Microbiology·Hanna Dams-Kozlowska, David L Kaplan
Feb 7, 2001·Applied and Environmental Microbiology·H A Louch, K J Miller
Jan 22, 2003·Environmental Microbiology·Craig DanielsJoseph S Lam
Dec 11, 2003·Microbiology and Molecular Biology Reviews : MMBR·Hiroshi Nikaido
Oct 14, 2014·Protein Science : a Publication of the Protein Society·Sergei KalynychMiroslaw Cygler
Oct 19, 2001·The Journal of Biological Chemistry·M H Bender, J Yother
Oct 27, 2004·Research in Microbiology·Víctor Parro, Mercedes Moreno-Paz
Jan 27, 2007·Journal of Molecular Biology·Brice ObadiaChristophe Grangeasse

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