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Papers In Press, published online ahead of print February 23, 2001
J. Biol. Chem, 10.1074/jbc.C100047200
Submitted on January 30, 2001
Revised on February 22, 2001
Accepted on February 22, 2001

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 Ishikawa, Satoshi Takahashi, Koichiro Ishimori, Isao Morishima, Hiroshi Nakajima, and Shigetoshi Aono

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

Corresponding Author: morisima{at}mds.moleng.kyoto-u.ac.jp

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 CooA?N5, in which N-terminal 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 N-terminal triggers the conformational transition to the DNA binding form.


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