Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice

Ayako Kohori, Ryohei Chiwata, Mohammad Delawar Hossain, Shou Furuike, Katsuyuki Shiroguchi, Kengo Adachi, Masasuke Yoshida, Kazuhiko Kinosita

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

F 1-ATPase is an ATP-driven rotary molecular motor in which the central γ-subunit rotates inside a cylinder made of α 3β 3 subunits. The amino and carboxyl termini of the γ rotor form a coiled coil of α-helices that penetrates the stator cylinder to serve as an axle. Crystal structures indicate that the axle is supported by the stator at two positions, at the orifice and by the hydrophobic sleeve surrounding the axle tip. The sleeve contacts are almost exclusively to the longer carboxyl-terminal helix, whereas nearly half the orifice contacts are to the amino-terminal helix. Here, we truncated the amino-terminal helix stepwise up to 50 residues, removing one half of the axle all the way up and far beyond the orifice. The half-sliced axle still rotated with an unloaded speed a quarter of the wild-type speed, with torque nearly half the wild-type torque. The truncations were made in a construct where the rotor tip was connected to a β-subunit via a short peptide linker. Linking alone did not change the rotational characteristics significantly. These and previous results show that nearly half the normal torque is generated if rotor-stator interactions either at the orifice or at the sleeve are preserved, suggesting that the make of the motor is quite robust.

Original languageEnglish
Pages (from-to)188-195
Number of pages8
JournalBiophysical Journal
Volume101
Issue number1
DOIs
Publication statusPublished - 2011 Jul 6

Fingerprint

Proton-Translocating ATPases
Torque
Adenosine Triphosphate
Peptides

ASJC Scopus subject areas

  • Biophysics

Cite this

Kohori, A., Chiwata, R., Hossain, M. D., Furuike, S., Shiroguchi, K., Adachi, K., ... Kinosita, K. (2011). Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice. Biophysical Journal, 101(1), 188-195. https://doi.org/10.1016/j.bpj.2011.05.008

Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice. / Kohori, Ayako; Chiwata, Ryohei; Hossain, Mohammad Delawar; Furuike, Shou; Shiroguchi, Katsuyuki; Adachi, Kengo; Yoshida, Masasuke; Kinosita, Kazuhiko.

In: Biophysical Journal, Vol. 101, No. 1, 06.07.2011, p. 188-195.

Research output: Contribution to journalArticle

Kohori, A, Chiwata, R, Hossain, MD, Furuike, S, Shiroguchi, K, Adachi, K, Yoshida, M & Kinosita, K 2011, 'Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice', Biophysical Journal, vol. 101, no. 1, pp. 188-195. https://doi.org/10.1016/j.bpj.2011.05.008
Kohori, Ayako ; Chiwata, Ryohei ; Hossain, Mohammad Delawar ; Furuike, Shou ; Shiroguchi, Katsuyuki ; Adachi, Kengo ; Yoshida, Masasuke ; Kinosita, Kazuhiko. / Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice. In: Biophysical Journal. 2011 ; Vol. 101, No. 1. pp. 188-195.
@article{da06ab249e7b4e91bdbba2c24dd07336,
title = "Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice",
abstract = "F 1-ATPase is an ATP-driven rotary molecular motor in which the central γ-subunit rotates inside a cylinder made of α 3β 3 subunits. The amino and carboxyl termini of the γ rotor form a coiled coil of α-helices that penetrates the stator cylinder to serve as an axle. Crystal structures indicate that the axle is supported by the stator at two positions, at the orifice and by the hydrophobic sleeve surrounding the axle tip. The sleeve contacts are almost exclusively to the longer carboxyl-terminal helix, whereas nearly half the orifice contacts are to the amino-terminal helix. Here, we truncated the amino-terminal helix stepwise up to 50 residues, removing one half of the axle all the way up and far beyond the orifice. The half-sliced axle still rotated with an unloaded speed a quarter of the wild-type speed, with torque nearly half the wild-type torque. The truncations were made in a construct where the rotor tip was connected to a β-subunit via a short peptide linker. Linking alone did not change the rotational characteristics significantly. These and previous results show that nearly half the normal torque is generated if rotor-stator interactions either at the orifice or at the sleeve are preserved, suggesting that the make of the motor is quite robust.",
author = "Ayako Kohori and Ryohei Chiwata and Hossain, {Mohammad Delawar} and Shou Furuike and Katsuyuki Shiroguchi and Kengo Adachi and Masasuke Yoshida and Kazuhiko Kinosita",
year = "2011",
month = "7",
day = "6",
doi = "10.1016/j.bpj.2011.05.008",
language = "English",
volume = "101",
pages = "188--195",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "1",

}

TY - JOUR

T1 - Torque generation in F 1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice

AU - Kohori, Ayako

AU - Chiwata, Ryohei

AU - Hossain, Mohammad Delawar

AU - Furuike, Shou

AU - Shiroguchi, Katsuyuki

AU - Adachi, Kengo

AU - Yoshida, Masasuke

AU - Kinosita, Kazuhiko

PY - 2011/7/6

Y1 - 2011/7/6

N2 - F 1-ATPase is an ATP-driven rotary molecular motor in which the central γ-subunit rotates inside a cylinder made of α 3β 3 subunits. The amino and carboxyl termini of the γ rotor form a coiled coil of α-helices that penetrates the stator cylinder to serve as an axle. Crystal structures indicate that the axle is supported by the stator at two positions, at the orifice and by the hydrophobic sleeve surrounding the axle tip. The sleeve contacts are almost exclusively to the longer carboxyl-terminal helix, whereas nearly half the orifice contacts are to the amino-terminal helix. Here, we truncated the amino-terminal helix stepwise up to 50 residues, removing one half of the axle all the way up and far beyond the orifice. The half-sliced axle still rotated with an unloaded speed a quarter of the wild-type speed, with torque nearly half the wild-type torque. The truncations were made in a construct where the rotor tip was connected to a β-subunit via a short peptide linker. Linking alone did not change the rotational characteristics significantly. These and previous results show that nearly half the normal torque is generated if rotor-stator interactions either at the orifice or at the sleeve are preserved, suggesting that the make of the motor is quite robust.

AB - F 1-ATPase is an ATP-driven rotary molecular motor in which the central γ-subunit rotates inside a cylinder made of α 3β 3 subunits. The amino and carboxyl termini of the γ rotor form a coiled coil of α-helices that penetrates the stator cylinder to serve as an axle. Crystal structures indicate that the axle is supported by the stator at two positions, at the orifice and by the hydrophobic sleeve surrounding the axle tip. The sleeve contacts are almost exclusively to the longer carboxyl-terminal helix, whereas nearly half the orifice contacts are to the amino-terminal helix. Here, we truncated the amino-terminal helix stepwise up to 50 residues, removing one half of the axle all the way up and far beyond the orifice. The half-sliced axle still rotated with an unloaded speed a quarter of the wild-type speed, with torque nearly half the wild-type torque. The truncations were made in a construct where the rotor tip was connected to a β-subunit via a short peptide linker. Linking alone did not change the rotational characteristics significantly. These and previous results show that nearly half the normal torque is generated if rotor-stator interactions either at the orifice or at the sleeve are preserved, suggesting that the make of the motor is quite robust.

UR - http://www.scopus.com/inward/record.url?scp=80052458591&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=80052458591&partnerID=8YFLogxK

U2 - 10.1016/j.bpj.2011.05.008

DO - 10.1016/j.bpj.2011.05.008

M3 - Article

VL - 101

SP - 188

EP - 195

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 1

ER -