TY - JOUR
T1 - Strength and lifetime of the bond between actin and skeletal muscle α-actinin studied with an optical trapping technique
AU - Miyata, Hidetake
AU - Yasuda, Ryohei
AU - Kinosita, Kazuhiko
N1 - Funding Information:
We thank Dr. A. Ikegami (Medical School, Keio University) and Dr. Y. Inoue (RIKEN) for their continuous support. This work was also supported by Grants-in-Aid from Ministry of Education, Science and Culture of Japan, by Special Coordination Funds for Promoting Science and Technology from the Agency of Science and Technology and a grant from Keio Universtiy.
PY - 1996/5/21
Y1 - 1996/5/21
N2 - The force required to break the bond between skeletal muscle actin and α-actinin (unbinding force) was measured at the level of individual molecules with an optical trapping technique. An actin filament, to the barbed-end of which was attached a gelsolin-coated polystyrene bead, was bound to α-actinin molecules adsorbed to a nitrocellulose-coated glass surface (~ 1 α-actinin molecule per 1 μm actin filament). The filament-bound bead was held by the optical trap and the force was applied to break the bond by pulling the bead. The unbinding force ranged from 1.4 to 44 pN. The average magnitude of the force was ~ 18 pN. As the probability of the bond breakage has been suggested to be governed by the magnitude of the external force, the relationship was studied between the magnitude of the unbinding force and the time required to break the bond (unbinding time). The unbinding time ranged from ~ 0.1 to ~ 20 seconds, and tended to become shorter as the unbinding force became larger. The unbinding time seemed to be classifiable into two major groups: one group having a time value of 1 sec or less and the other having a time value ranging from several to 20 seconds. This suggests the existence of at least two classes of the actin-actinin bonds.
AB - The force required to break the bond between skeletal muscle actin and α-actinin (unbinding force) was measured at the level of individual molecules with an optical trapping technique. An actin filament, to the barbed-end of which was attached a gelsolin-coated polystyrene bead, was bound to α-actinin molecules adsorbed to a nitrocellulose-coated glass surface (~ 1 α-actinin molecule per 1 μm actin filament). The filament-bound bead was held by the optical trap and the force was applied to break the bond by pulling the bead. The unbinding force ranged from 1.4 to 44 pN. The average magnitude of the force was ~ 18 pN. As the probability of the bond breakage has been suggested to be governed by the magnitude of the external force, the relationship was studied between the magnitude of the unbinding force and the time required to break the bond (unbinding time). The unbinding time ranged from ~ 0.1 to ~ 20 seconds, and tended to become shorter as the unbinding force became larger. The unbinding time seemed to be classifiable into two major groups: one group having a time value of 1 sec or less and the other having a time value ranging from several to 20 seconds. This suggests the existence of at least two classes of the actin-actinin bonds.
KW - Actin-actinin bond
KW - Bond lifetime
KW - Intermolecular force
KW - Surface denaturation
KW - Unbinding force
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U2 - 10.1016/0304-4165(96)00003-7
DO - 10.1016/0304-4165(96)00003-7
M3 - Article
C2 - 8645711
AN - SCOPUS:0029984843
SN - 0006-3002
VL - 1290
SP - 83
EP - 88
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 1
ER -