The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase.
F(1)-ATPase is a rotary motor protein, and ATP hydrolysis generates torque at the interface between the gamma subunit, a rotor shaft, and the alpha(3)beta(3) substructure, a stator ring. The region of conserved acidic "DELSEED" motif of the beta subunit has a contact with gamma subunit and has been assumed to be involved in torque generation. Using the thermophilic alpha(3)beta(3)gamma complex in which the corresponding sequence is DELSDED, we replaced each residue and all five acidic residues in this sequence with alanine. In addition, each of two conserved residues at the counterpart contact position of gamma subunit was also replaced. Surprisingly, all of these mutants rotated with as much torque as the wild-type. We conclude that side chains of the DELSEED motif of the beta subunit do not have a direct role in torque generation.
Hara
K Y
KY
Chemical Resources Laboratory, R-1, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan.
Noji
H
H
Bald
D
D
Yasuda
R
R
Kinosita
K
K
Yoshida
M
M
D000255:Adenosine Triphosphate / Q000737:chemistry; D020816:Amino Acid Motifs; D006868:Hydrolysis; D008958:Models, Molecular; D016296:Mutagenesis; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics
D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases