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Journal Articles

Phylogenetic and disruption analyses of aspartate kinase of ${it Deinococcus radiodurans}$

Nishida, Hiromi*; Narumi, Issei

Bioscience Biotechnology and Biochemistry, 71(4), p.1015 - 1020, 2007/04

https://doi.org/10.1271/bbb.60671
 Times Cited Count：2 Percentile：10.84(Biochemistry & Molecular Biology)

The radioresistant bacterium ${it Deinococcus radiodurans}$ is evolutionarily closely related to the themophilic bacterium ${it Thermus thermophilus}$. These bacteria have a single gene encoding an aspartate kinase (AK). ${it T. thermophilus}$ has an aminoadipate pathway for lysine biosynthesis, which does not use AK. Phylogenetic analysis showed that ${it D. radiodurans}$ AK had different protein structure and different evolutionary history from ${it T. thermophilus}$ AK. Disruption analysis of ${it D. radiodurans}$ AK indicated that ${it D. radiodurans}$ AK was not used for lysine biosynthesis but for threonine and methionine biosyntheses. Thus these two AKs have different evolutionary origins, but their functions are not different.

Journal Articles

Disruption analysis of ${it DR1420}$ and/or ${it DR1758}$ in the extremely radioresistant bacterium ${it Deinococcus radiodurans}$

Nashida, Hiromi*; Narumi, Issei

Microbiology, 148(9), p.2911 - 2914, 2002/09

The extremely radioresistant bacterium ${it Deinococcus radiodurans}$ has the related homologous genes to bacterial lysine biosyntheses both through the aminoadipate pathway and the diaminopimelate pathway. We disrupted ${it DR1420}$ and/or ${it DR1758}$. The ${it DR1420}$ is homologous to ${it lysZ}$ that is essential for the aminoadipate pathway. The ${it DR1758}$ is homologous to ${it lysA}$ that is essential for the diaminopimelate pathway. Each disruptant of ${it DR1420}$, ${it DR1758}$, and ${it DR1420}$ and ${it DR1758}$ grew in a minimal medium, as well as wild-type. This result shows that ${it Deinococcus radiodurans}$ employs a unique way for lysine biosynthesis.

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