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A more recent version of this article appeared on October 11, 2002
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C200253200v1
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Papers In Press, published online ahead of print September 3, 2002
J. Biol. Chem, 10.1074/jbc.C200253200
Submitted on April 29, 2002
Revised on September 3, 2002
Accepted on September 3, 2002

Glutamate racemase is an endogenous DNA gyrase inhibitor

Makoto Ashiuchi, Eriko Kuwana, Takashi Yamamoto, Kazuya Komatsu, Kenji Soda, and Haruo Misono

Bioresources Science, Kochi University, Nankoku, Kochi 783-8502

Corresponding Author: ashiuchi{at}cc.kochi-u.ac.jp

Almost all bacteria possess glutamate racemase to synthesize D-glutamate as an essential component of peptidoglycans in the cell walls. The enforced production of glutamate racemase, however, resulted in suppression of cell proliferation. In the Escherichia coli JM109/pGR3 clone, the overproducer of glutamate racemase, the copy number (i.e., replication efficiency) of plasmid DNA declined dramatically, whereas the E. coli WM335 mutant that is defective in the gene of glutamate racemase showed little genetic competency. The comparatively low and high activities for DNA supercoiling were contained in the E. coli JM109/pGR3 and WM335 cells, respectively. Furthermore, we found that the DNA gyrase of E. coli was modulated by the glutamate racemase of E. coli in the presence of UDP-N-acetylmuramyl-L-alanine, which is a peptidoglycan precursor and functions as an absolute activator for the racemase. This is the first finding of the enzyme protein participating in both D-amino acid metabolism and DNA processing.


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