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Journal of Bacteriology, September 2001, p. 5067-5073, Vol. 183, No. 17
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.17.5067-5073.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Functional and Evolutionary Relationship between Arginine Biosynthesis and Prokaryotic Lysine Biosynthesis through alpha -Aminoadipate

Junichi Miyazaki, Nobuyuki Kobashi, Makoto Nishiyama,* and Hisakazu Yamane

Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan

Received 30 March 2001/Accepted 6 June 2001

Our previous studies revealed that lysine is synthesized through alpha -aminoadipate in an extremely thermophilic bacterium, Thermus thermophilus HB27. Sequence analysis of a gene cluster involved in the lysine biosynthesis of this microorganism suggested that the conversion from alpha -aminoadipate to lysine proceeds in a way similar to that of arginine biosynthesis. In the present study, we cloned an argD homolog of T. thermophilus HB27 which was not included in the previously cloned lysine biosynthetic gene cluster and determined the nucleotide sequence. A knockout of the argD-like gene, now termed lysJ, in T. thermophilus HB27 showed that this gene is essential for lysine biosynthesis in this bacterium. The lysJ gene was cloned into a plasmid and overexpressed in Escherichia coli, and the LysJ protein was purified to homogeneity. When the catalytic activity of LysJ was analyzed in a reverse reaction in the putative pathway, LysJ was found to transfer the varepsilon -amino group of N2-acetyllysine, a putative intermediate in lysine biosynthesis, to 2-oxoglutarate. When N2-acetylornithine, a substrate for arginine biosynthesis, was used as the substrate for the reaction, LysJ transferred the delta -amino group of N2-acetylornithine to 2-oxoglutarate 16 times more efficiently than when N2-acetyllysine was the amino donor. All these results suggest that lysine biosynthesis in T. thermophilus HB27 is functionally and evolutionarily related to arginine biosynthesis.

* Corresponding author. Mailing address: Biotechnology Research Center, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81-3-5841-3072. Fax: 81-3-5841-8030. E-mail: umanis{at}mail.ecc.u-tokyo.ac.jp.

Journal of Bacteriology, September 2001, p. 5067-5073, Vol. 183, No. 17
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.17.5067-5073.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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