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Journal of Bacteriology, December 2008, p. 8238-8243, Vol. 190, No. 24
0021-9193/08/$08.00+0     doi:10.1128/JB.00889-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Altered Oligomerization Properties of N316 Mutants of Escherichia coli TyrR{triangledown}

Takashi Koyanagi,1,2 Takane Katayama,2 Hideyuki Suzuki,1,3 and Hidehiko Kumagai2*

Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502,1 Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836,2 Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Kyoto 606-8585, Japan3

Received 30 June 2008/ Accepted 6 October 2008

The transcriptional regulator TyrR is known to undergo a dimer-to-hexamer conformational change in response to aromatic amino acids, through which it controls gene expression. In this study, we identified N316D as the second-site suppressor of Escherichia coli TyrRE274Q, a mutant protein deficient in hexamer formation. N316 variants exhibited altered in vivo regulatory properties, and the most drastic changes were observed for TyrRN316D and TyrRN316R mutants. Gel filtration analyses revealed that the ligand-mediated oligomer formation was enhanced and diminished for TyrRN316D and TyrRN316R, respectively, compared with the wild-type TyrR. ADP was substituted for ATP in the oligomer formation of TyrRN316D.

* Corresponding author. Mailing address: Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa 921-8836, Japan. Phone: 81-76-227-7522. Fax: 81-76-227-7557. E-mail: hidekuma{at}ishikawa-pu.ac.jp

{triangledown} Published ahead of print on 17 October 2008.

Journal of Bacteriology, December 2008, p. 8238-8243, Vol. 190, No. 24
0021-9193/08/$08.00+0     doi:10.1128/JB.00889-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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