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Related Experiment Video

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Methods to Quantify Pharmacologically Induced Alterations in Motor Function in Human Incomplete SCI

Methods to Quantify Pharmacologically Induced Alterations in Motor Function in Human Incomplete SCI

Published on: April 18, 2011

Converter domain mutations in myosin alter structural kinetics and motor function.

Laura K Gunther¹, John A Rohde², Wanjian Tang¹

¹Department of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, Hershey, Pennsylvania 17033.

The Journal of Biological Chemistry

|December 7, 2018

Summary

Investigating myosin V mutations (R712G and F750L) reveals how altering structural transitions impacts motor function. These myosin mutations, linked to human cardiomyopathies, affect force generation without changing overall pre- and post-power-stroke states.

Keywords:

ATPase actin cardiomyopathy fluorescence resonance energy transfer (FRET)mechanochemistry motor protein muscle myosin structural kinetics

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Myosins are essential molecular motors utilizing an ATPase cycle for force generation.
Specific mutations in the myosin V converter domain (R712G, F750L) are investigated for their impact on mechanochemistry.
These mutations correspond to those found in human β-cardiac myosin, linked to cardiomyopathies.

Purpose of the Study:

To examine how specific structural transitions in the myosin V ATPase cycle are affected by R712G and F750L mutations.
To understand the relationship between these myosin mutations and impaired motor function.
To explore potential therapeutic strategies targeting structural state transitions.

Main Methods:

Utilized *in vitro* motility assays under varying loads to assess myosin V mechanochemistry.
Employed transient kinetic analysis and stopped-flow Förster Resonance Energy Transfer (FRET) to study ATPase cycle kinetics.
Investigated conformational states using time-resolved FRET to analyze pre- and post-power-stroke populations.

Main Results:

Both R712G and F750L mutations reduced the ability to overcome frictional loads, despite similar unloaded velocities.
R712G slowed ATP hydrolysis and recovery-stroke rates, while F750L enhanced these steps.
Mutations altered the population of post-power-stroke conformations in specific actin-binding states without changing overall pre- and post-power-stroke structures.

Conclusions:

Alterations in key allosteric pathways can modify equilibrium and activation energies of structural transitions in myosin.
Disease-associated myosin mutations can impair motor function by affecting these transitions, not necessarily overall conformation.
Targeting transitions between structural states offers a potential therapeutic avenue for myosin-related diseases.