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J Biol Chem, Vol. 275, Issue 19, 14260-14263, May 12, 2000
From the Chemical Resources Laboratory, R-1, Tokyo Institute of
Technology, Nagatsuta 4259, Yokohama 226-8503, Japan,
§ CREST (Core Research for Evolutional Science and
Technology) Genetic Programming Team 13, Teikyo University,
Biotechnology Research Center 3F, Nogawa 907, Miyamae-ku, Kawasaki
216-000, Japan, and the ¶ Department of Physics, Faculty of
Science and Technology, Keio University, Yokohama 223-8522, Japan
F1-ATPase is a rotary motor
protein, and ATP hydrolysis generates torque at the interface between
the
The Role of the DELSEED Motif of the
Subunit in Rotation
of F1-ATPase*
,
subunit, a rotor shaft, and the
3
3 substructure, a stator ring. The
region of conserved acidic "DELSEED" motif of the subunit has a
contact with subunit and has been assumed to be involved in torque
generation. Using the thermophilic 33
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 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 subunit do not have a
direct role in torque generation.
*
This work was supported in part by grants from CREST (Core
Research for Evolutional Science and Technology, 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.
Supported by Fellowships of the Japan Society for the Promotion of
Science for Young Scientists.
To whom correspondence should be addressed. Fax:
81-45-924-5277; E-mail: myoshida@res.titech.ac.jp.
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