What question did this study set out to answer?

Determine the high-resolution architecture of myosin thick filaments and their non-myosin components in the flight muscle of Drosophila melanogaster.

June 5, 2020Open Access

CryoEM Structure of Drosophila Flight Muscle Thick Filaments at 7Å Resolution

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Key result

Cryo-electron microscopy of Drosophila flight muscle thick filaments at 7Å resolution revealed highly conserved myosin tail packing into curved molecular crystalline layers, despite disordered myosin heads.

Why the study?

Myosin thick filaments are key striated muscle structures but remain poorly understood, leaving it unclear how the myosin alpha-helical coiled-coil tail is arranged in the backbone.

Population

Thick filaments of flight muscle from the fruit fly Drosophila melanogaster

Design

CryoEM structural study at 7 Å resolution

Authors

NDNadia DaneshparvarFlorida State University DTDianne W. TaylorFlorida State University TOThomas S. O’LearyUniversity of Vermont

Discussion

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Implication

No immediate clinical relevance; leaves open extension to human cardiac myosin organization.

Key Points

Determine the high-resolution architecture of myosin thick filaments and their non-myosin components in the flight muscle of Drosophila melanogaster.
Reconstructed the three-dimensional structure of isolated Drosophila flight muscle thick filaments at 7 Å resolution using cryo-electron microscopy.
Compared filament backbone packing and non-myosin densities with the homologous structure from the giant waterbug Lethocerus indicus.
Myosin tails assemble into curved molecular crystalline layers that are structurally identical to those in Lethocerus indicus, despite over 245 million years of evolutionary divergence.
Identified four non-myosin protein densities along the filament, including three shared with Lethocerus and one novel density on the outer backbone tentatively attributed to stretchin-Mlck.
Revealed that myosin motor heads are disordered along the filament backbone rather than arranged in regular crystalline patterns.

Cite This Study

Daneshparvar et al. (2020) studied this question. Cryo-electron microscopy of Drosophila flight muscle thick filaments at 7Å resolution revealed highly conserved myosin tail packing into curved molecular crystalline layers, despite disordered myosin heads.

synapsesocial.com/papers/6a86daa9a6ddb97d43d3be88 https://doi.org/10.1101/2020.06.05.136580

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CryoEM Structure of Drosophila Flight Muscle Thick Filaments at 7Å Resolution

Discussion

Member takes

Implication

Key Points

Cite This Study

CryoEM Structure of Drosophila Flight Muscle Thick Filaments at 7Å Resolution

Discussion

Member takes

Implication

Key Points

Cite This Study

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