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Light meromyosin paracrystal formation.

P K Chowrashi, F A Pepe

The Journal of Cell Biology

|July 1, 1977

Summary

This summary is machine-generated.

Light meromyosin (LMM) paracrystal formation reveals distinct stagger relationships influenced by fragment length and enzyme preparation. Nucleic acid is crucial for specific axial repeat patterns in LMM paracrystals.

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Area of Science:

Muscle protein structure and assembly
Biochemistry of myosin and its fragments
Crystallography and self-assembly

Background:

Myosin rod structure and its role in muscle filament organization are not fully understood.
Light meromyosin (LMM) fragments are key components in studying myosin assembly.
Understanding LMM self-assembly provides insights into the larger myosin structure.

Purpose of the Study:

To investigate the factors influencing light meromyosin (LMM) paracrystal formation.
To elucidate the role of different LMM preparation methods and associated molecules in paracrystal structure.
To determine the specific stagger relationships and axial repeat periodicities in LMM paracrystals.

Main Methods:

Preparation of column-purified light meromyosin (LMM) using various enzymatic digestions (trypsin, papain).

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Analysis of LMM paracrystal formation under different conditions, including varying fragment lengths and enzyme treatments.

Electron microscopy to observe and measure axial repeat periodicities and intra-sheet structures of paracrystals.

Main Results:

Different LMM fragment lengths and enzymatic preparations yield paracrystals with distinct axial repeat periodicities, suggesting varied stagger relationships.
Paracrystals with a 14-nm axial repeat periodicity are formed by staggered aggregation of sheets exhibiting a 44-nm axial repeat.
C-protein binding appears specific to certain LMM molecular arrangements, leading to consistent axial repeat patterns.
Nucleic acid is identified as the cause of the 43-nm axial repeat in ethanol-resistant LMM fractions; its absence results in a 14-nm repeat.
The 43-nm axial repeat pattern differs between LMM preparations obtained via trypsin and papain digestion.

Conclusions:

The myosin rod's different segments likely dictate distinct stagger relationships in paracrystal formation.
LMM self-assembly into paracrystals is a complex process influenced by fragment characteristics, associated proteins (C-protein), and nucleic acids.
The observed axial repeat patterns provide a framework for understanding the higher-order structure of myosin filaments.