Altered Oligomerization Properties of N316 Mutants of Escherichia coli TyrR-Reference-Cited by-同舟云学术

Altered Oligomerization Properties of N316 Mutants of Escherichia coli TyrR

Published:2008-12-15 Issue:24 Volume:190 Page:8238-8243
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Koyanagi Takashi¹²,Katayama Takane²,Suzuki Hideyuki¹³,Kumagai Hidehiko²

Affiliation:

1. Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502

2. Research Institute for Bioresources and Biotechnology, Ishikawa Prefectural University, Nonoichi, Ishikawa, 921-8836

3. Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Sakyo-ku, Kyoto 606-8585, Japan

Abstract

ABSTRACT 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 TyrR E274Q , a mutant protein deficient in hexamer formation. N316 variants exhibited altered in vivo regulatory properties, and the most drastic changes were observed for TyrR N316D and TyrR N316R mutants. Gel filtration analyses revealed that the ligand-mediated oligomer formation was enhanced and diminished for TyrR N316D and TyrR N316R , respectively, compared with the wild-type TyrR. ADP was substituted for ATP in the oligomer formation of TyrR N316D .

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.00889-08

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