Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements

Md Shahjahan P Siddique; Takashi Miyazaki; Eisaku Katayama; Taro Q P Uyeda; Makoto Suzuki

doi:10.1016/j.bbrc.2005.04.152

Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements

Md Shahjahan P Siddique, Takashi Miyazaki, Eisaku Katayama, Taro Q P Uyeda, Makoto Suzuki

ENG - Materials Processing

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

We have engineered acto-S1chimera proteins carrying the entire actin inserted in loop 2 of the motor domain of Dictyostelium myosin II with 24 or 18 residue-linkers (CP24 and CP18, respectively). These proteins were capable of self-polymerization as well as copolymerization with skeletal actin and exhibited rigor-like structures. The MgATPase rate of CP24-skeletal actin copolymer was 1.06 s^-1, which is slightly less than the V _max of Dictyostelium S1. Homopolymer filaments of skeletal actin, CP24, and CP18 moved at 4.7 ± 0.6, 2.9 ± 0.6, and 4.1 ± 0.8 μm/s (mean ± SD), respectively, on coverslips coated with skeletal myosin at 27°C. Statistically thermodynamic considerations suggest that the S1 portion of chimera protein mostly resides on subdomain 1 (SD-1) of the actin portion even in the presence of ATP. This and the fact that filaments of CP18 with shorter linkers moved faster than CP24 filaments suggest that SD-1 might not be as essential as conventionally presumed for actomyosin sliding interactions.

Original language	English
Pages (from-to)	474-481
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	332
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2005.04.152
Publication status	Published - 2005 Jul 1

Keywords

Acto-S1 chimera
ATPase
Dictyostelium
Electron microscopy
Intermediate state
Loop 2
Motility function

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/j.bbrc.2005.04.152

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title = "Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements",

abstract = "We have engineered acto-S1chimera proteins carrying the entire actin inserted in loop 2 of the motor domain of Dictyostelium myosin II with 24 or 18 residue-linkers (CP24 and CP18, respectively). These proteins were capable of self-polymerization as well as copolymerization with skeletal actin and exhibited rigor-like structures. The MgATPase rate of CP24-skeletal actin copolymer was 1.06 s-1, which is slightly less than the V max of Dictyostelium S1. Homopolymer filaments of skeletal actin, CP24, and CP18 moved at 4.7 ± 0.6, 2.9 ± 0.6, and 4.1 ± 0.8 μm/s (mean ± SD), respectively, on coverslips coated with skeletal myosin at 27°C. Statistically thermodynamic considerations suggest that the S1 portion of chimera protein mostly resides on subdomain 1 (SD-1) of the actin portion even in the presence of ATP. This and the fact that filaments of CP18 with shorter linkers moved faster than CP24 filaments suggest that SD-1 might not be as essential as conventionally presumed for actomyosin sliding interactions.",

keywords = "Acto-S1 chimera, ATPase, Dictyostelium, Electron microscopy, Intermediate state, Loop 2, Motility function",

author = "Siddique, {Md Shahjahan P} and Takashi Miyazaki and Eisaku Katayama and Uyeda, {Taro Q P} and Makoto Suzuki",

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AU - Siddique, Md Shahjahan P

AU - Miyazaki, Takashi

AU - Katayama, Eisaku

AU - Uyeda, Taro Q P

AU - Suzuki, Makoto

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Y1 - 2005/7/1

N2 - We have engineered acto-S1chimera proteins carrying the entire actin inserted in loop 2 of the motor domain of Dictyostelium myosin II with 24 or 18 residue-linkers (CP24 and CP18, respectively). These proteins were capable of self-polymerization as well as copolymerization with skeletal actin and exhibited rigor-like structures. The MgATPase rate of CP24-skeletal actin copolymer was 1.06 s-1, which is slightly less than the V max of Dictyostelium S1. Homopolymer filaments of skeletal actin, CP24, and CP18 moved at 4.7 ± 0.6, 2.9 ± 0.6, and 4.1 ± 0.8 μm/s (mean ± SD), respectively, on coverslips coated with skeletal myosin at 27°C. Statistically thermodynamic considerations suggest that the S1 portion of chimera protein mostly resides on subdomain 1 (SD-1) of the actin portion even in the presence of ATP. This and the fact that filaments of CP18 with shorter linkers moved faster than CP24 filaments suggest that SD-1 might not be as essential as conventionally presumed for actomyosin sliding interactions.

AB - We have engineered acto-S1chimera proteins carrying the entire actin inserted in loop 2 of the motor domain of Dictyostelium myosin II with 24 or 18 residue-linkers (CP24 and CP18, respectively). These proteins were capable of self-polymerization as well as copolymerization with skeletal actin and exhibited rigor-like structures. The MgATPase rate of CP24-skeletal actin copolymer was 1.06 s-1, which is slightly less than the V max of Dictyostelium S1. Homopolymer filaments of skeletal actin, CP24, and CP18 moved at 4.7 ± 0.6, 2.9 ± 0.6, and 4.1 ± 0.8 μm/s (mean ± SD), respectively, on coverslips coated with skeletal myosin at 27°C. Statistically thermodynamic considerations suggest that the S1 portion of chimera protein mostly resides on subdomain 1 (SD-1) of the actin portion even in the presence of ATP. This and the fact that filaments of CP18 with shorter linkers moved faster than CP24 filaments suggest that SD-1 might not be as essential as conventionally presumed for actomyosin sliding interactions.

KW - Acto-S1 chimera

KW - ATPase

KW - Dictyostelium

KW - Electron microscopy

KW - Intermediate state

KW - Loop 2

KW - Motility function

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Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements

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