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
Becker A, Pühler A (1998)
JOURNAL OF BACTERIOLOGY 180(2): 395-399.
Zeitschriftenaufsatz
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Autor*in
Becker, Anke;
Pühler, AlfredUniBi 
Einrichtung
Abstract / Bemerkung
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 (RX(4)PX(2)PX(4)SPKX(9)IXGXMXGXG) located from positions 443 to 476 of the ExoP protein was analyzed. The absence of the (I-terminal cytoplasmic ExoP domain (positions 484 to 786) and the substitution of both arginine(443) by isoleucine(443) and proline(457) by serine(457) 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.
Erscheinungsjahr
1998
Zeitschriftentitel
JOURNAL OF BACTERIOLOGY
Band
180
Ausgabe
2
Seite(n)
395-399
ISSN
0021-9193
Page URI
https://pub.uni-bielefeld.de/record/1626543
Zitieren
Becker A, Pühler A. 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. 1998;180(2):395-399.
Becker, A., & Pühler, A. (1998). 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, 180(2), 395-399. https://doi.org/10.1128/JB.180.2.395-399.1998
Becker, Anke, and Pühler, Alfred. 1998. “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 180 (2): 395-399.
Becker, A., and Pühler, A. (1998). 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 180, 395-399.
Becker, A., & Pühler, A., 1998. 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, 180(2), p 395-399.
A. Becker and A. Pühler, “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, vol. 180, 1998, pp. 395-399.
Becker, A., Pühler, A.: 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. 180, 395-399 (1998).
Becker, Anke, and Pühler, Alfred. “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 180.2 (1998): 395-399.
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