What question did this study set out to answer?

To identify specific charged amino acid residues in subdomain 1 of Dictyostelium actin that interact with myosin during ATP-driven sliding motion and force generation.

March 15, 1993Proceedings of the National Academy of SciencesOpen Access

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

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Population

Dictyostelium actin mutants

Design

Preclinical

Authors

MJM JoharaTokyo University of the Arts YTYoko Y. ToyoshimaThe University of Tokyo AIAkihiko IshijimaThe University of Osaka

Discussion

Member takes

Implication

Advances molecular models of actomyosin; leaves open relevance to human cardiac sarcomere function.

Key Points

To identify specific charged amino acid residues in subdomain 1 of Dictyostelium actin that interact with myosin during ATP-driven sliding motion and force generation.
Substituted acidic residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 of Dictyostelium actin with histidine using site-directed mutagenesis.
Expressed and purified mutant actin proteins to homogeneity from Dictyostelium cells.
Assessed in vitro sliding movement of actin filaments over glass-immobilized heavy meromyosin, and measured single-filament force generation for C-terminal mutants.
Charge-reversion mutations at D24/D25 and E99/E100 impaired ATP-driven sliding movement over heavy meromyosin.
Mutations at C-terminal residues E360/E361 and D363/E364 did not impair ATP-driven sliding motion.
C-terminal mutations at E360/E361 and D363/E364 retained normal single-filament force generation with myosin.

Structured PICO

Population

Dictyostelium actin mutants (amino acid residues D24/D25, E99/E100, E360/E361, and D363/E364 in subdomain 1 replaced with histidine residues)

Intervention

Charge-reversion site-directed mutagenesis

Outcome

Sliding movement of mutant actin filaments on heavy meromyosin attached to a glass surface and force generated by a single actin filament and myosinsurrogate

Specific amino acid residues (D24/D25 and E99/E100) in subdomain 1 of Dictyostelium actin are critical for ATP-driven sliding motion with myosin.

Cite This Study

Johara et al. (1993) studied this question.

synapsesocial.com/papers/6a13ca003f9a9dbf1d39e3bc https://doi.org/10.1073/pnas.90.6.2127

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Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

Charge-reversion mutagenesis of Dictyostelium actin to map the surface recognized by myosin during ATP-driven sliding motion.

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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