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Biophys J, October 1999, p. 2175-2183, Vol. 77, No. 4

Functional Conformation Changes in the TF1-ATPase beta  Subunit Probed by 12 Tyrosine Residues

Hiromasa Yagi,* Kaeko Tozawa,* Nobuaki Sekino,* Tomoyuki Iwabuchi,* Masasuke Yoshida,# and Hideo Akutsu*

 *Department of Chemistry and Biotechnology, Faculty of Engineering, Yokohama National University, Yokohama 240-8501, and  #Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama 226-0026, Japan

The effect of nucleotide binding on the structure of the F1-ATPase beta  subunit from thermophilic bacillus PS-3 (TF1beta ) was investigated by monitoring the NMR signals of the 12 tyrosine residues. The 3,5-proton resonances of 12 tyrosine residues could be observed for the specifically deuterated beta  subunit. The assignment of 3,5-proton resonances of all of the tyrosine residues was accomplished using 14 mutant proteins, in each of which one or two tyrosine residues were replaced by phenylalanine. Binding of Mg·ATP induced an upfield shift of Tyr341 resonance, suggesting that their aromatic rings are stacked to each other. Besides Tyr341, the signal shift observed on Mg·ATP binding was restricted to the resonances of Tyr148, Tyr199, Tyr238, and Tyr307, suggesting that Mg·ATP induces a conformational change in the hinge region. This can be correlated to the change from the open to closed conformations as implicated in the crystal structure. Mg·ADP induced a similar but distinctly different conformational change. Therefore, the intrinsic conformational change in the beta  subunit induced by the nucleotide binding is proposed to be one of the essential driving forces for the F1 rotation. Reconstitution experiments showed that Tyr277, one of the four conserved tyrosines, is essential to the formation of the alpha 3beta 3gamma complex.

Biophys J, October 1999, p. 2175-2183, Vol. 77, No. 4
© 1999 by the Biophysical Society   0006-3495/99/10/2175/09  $2.00


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