HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 42, 39070-39073, October 18, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/42/39070    most recent C200253200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ashiuchi, M. Articles by Misono, H. Search for Related Content PubMed PubMed Citation Articles by Ashiuchi, M. Articles by Misono, H. Social Bookmarking                      What's this?

ACCELERATED PUBLICATION
Glutamate Racemase Is an Endogenous DNA Gyrase Inhibitor^*

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

From the  Department of Bioresources Science, Kochi University, Nankoku, Kochi 783-8502 and ^¶ Department of Biotechnology, Kansai University, Suita, Osaka 564-8680, Japan

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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				S. Sengupta, S. Ghosh, and V. Nagaraja Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme Microbiology, September 1, 2008; 154(9): 2796 - 2803. [Abstract] [Full Text] [PDF]

				S. Sengupta and V. Nagaraja YacG from Escherichia coli is a specific endogenous inhibitor of DNA gyrase Nucleic Acids Res., August 1, 2008; 36(13): 4310 - 4316. [Abstract] [Full Text] [PDF]

				S. Sengupta, M. Shah, and V. Nagaraja Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding Nucleic Acids Res., November 14, 2006; 34(19): 5567 - 5576. [Abstract] [Full Text] [PDF]

				B. Fournier and A. Klier Protein A gene expression is regulated by DNA supercoiling which is modified by the ArlS-ArlR two-component system of Staphylococcus aureus Microbiology, November 1, 2004; 150(11): 3807 - 3819. [Abstract] [Full Text] [PDF]