| Title | Improvement in the Stability of Glycinecin A through Protein Fusion of the Two Structural Components |
|---|---|
| Author | Youngmee Kim, Somi K. Cho, and Moonjae Cho * |
| Address | Department of Biochemistry, Cheju National University Medical School, Jeju 690-756, Korea |
| Bibliography | Journal of Microbiology, 39(3),177-180, 2001, |
| DOI | |
| Key Words | glycinecin, chimeric protein stability, Xanthomonas, bacteriocin |
| Abstract | Glycinecin A, a bacteriocin produced by Xanthomonas campestris pv. glycines, inhibits the growth of X. c. pv. vesicatoria. We have reported that purified glycinecin A is composed of two polypeptides, is active over a wide range of pH (6 to 9), and is stable at temperatures up to 60 C. Glycinecin A is a heterodimer consisting of 39- and 14-kDa subunits; the two encoding genes, glyA and glyB, respectively, have been cloned (Heu et al. 2001. Appl. Environ. Microbiol. 67, 4105-4110). Co-expression of glyA and glyB in the same cell is essential for bacteriocin activity. We constructed and produced a chimeric glycinecin A connecting glyA and glyB in one open reading frame. The chimeric glycinecin A has the same bactericidal activity as the wild-type glycinecin A. However, the chimeric glycinecin A is more stable in a wider range of pH and temperature. |
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