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Originally published In Press as doi:10.1074/jbc.C100047200 on February 23, 2001

J. Biol. Chem., Vol. 276, Issue 15, 11473-11476, April 13, 2001
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ACCELERATED PUBLICATION
Binding of CO at the Pro2 Side Is Crucial for the Activation of CO-sensing Transcriptional Activator CooA
1H NMR SPECTROSCOPIC STUDIES*

Katsuhiko Yamamoto, Haruto IshikawaDagger , Satoshi Takahashi, Koichiro Ishimori, and Isao Morishima§

From the Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto 606-8501, Japan

Hiroshi Nakajima, and Shigetoshi Aono§

From the School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Nomi-gun, Ishikawa 923-1292, Japan

CooA is a heme-containing transcriptional activator that anaerobically binds to DNA at CO atmosphere. To obtain information on the conformational transition of CooA induced by CO binding to the heme, we assigned ring current-shifted 1H NMR signals of CooA using two mutants whose axial ligands of the heme were replaced. In the absence of CO, the NMR spectral pattern of H77Y CooA, in which the axial histidine (His77) was replaced with tyrosine, was similar to that of wild-type CooA. In contrast, the spectra of CooADelta N5, in which the NH2 termini including the other axial ligand (Pro2) were deleted, were drastically modulated. We assigned three signals of wild-type CooA at -4.5, -3.6, and -2.8 ppm to delta 1-, alpha -, and delta 2-protons of Pro2, respectively. The Pro2 signals were undetectable in the upfield region of the spectrum of the CO-bound state, which confirms that CO displaces Pro2. Interestingly, the Pro2 signals were observed for CO-bound H77Y CooA, implying that CO binds to the trans position of Pro2 in H77Y CooA. The abolished CO-dependent transcriptional activity of H77Y CooA is therefore the consequence of Pro2 ligation. These observations are consistent with the view that the movement of the NH2 terminus triggers the conformational transition to the DNA binding form.

* This work was supported by Grants-in-aid 08249102 (to I. M.) and 11116212, 12019222, and 12680631 (to S. A.) for Scientific Research on Priority Areas from Ministry of Education, Culture, Sports, Science, and Technology in Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by Research Fellowships of the Japan Society for the Promotion of Science for Young Scientists.

§ To whom correspondence may be addressed: Tel.: 81-75-753-5921; Fax: 81-75-751-7611; E-mail: morisima@mds.moleng.kyoto-u.ac.jp (for I. M.) or Tel.: 81-761-51-1681; Fax: 81-761-51-1149; E-mail:aono@jaist.ac.jp (for S. A.).

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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