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The stability and transitions of tryptic-digested clathrin.

R Zarrilli, R E Lippoldt, H Edelhoch

Archives of Biochemistry and Biophysics

|August 15, 1985

Summary

Tryptic digestion of clathrin baskets did not alter their pH-dependent dissociation or molecular transitions. This indicates that the distal portions of clathrin triskelion arms are not essential for structural integrity or molecular interactions.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Clathrin mediates vesicle formation in cells.
Clathrin baskets form the protein coat of vesicles.
The structure and function of clathrin are crucial for cellular processes.

Purpose of the Study:

To investigate the impact of partial digestion on clathrin basket structure and function.
To determine if the distal portions of clathrin triskelion arms are essential for structural transitions and molecular interactions.

Main Methods:

Light scattering to determine pH-dependent dissociation of trypsin-digested and undigested clathrin baskets.
Fluorescence spectra and polarization measurements to study molecular transitions of clathrin from digested and undigested baskets.

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Main Results:

No significant difference in pH-dependent dissociation was observed between digested and undigested clathrin baskets.
Molecular transitions of clathrin from both digested and undigested baskets were found to be very similar.
Removal of approximately one-third of the mass from the distal portions of the clathrin triskelion arms did not affect its structural transitions.

Conclusions:

The distal portions of clathrin triskelion arms are not critical for the structural transitions or molecular interactions within clathrin baskets.
Interactions between clathrin molecules in the basket structure and within the molecule remain intact after tryptic digestion.
The specific function of the distal portion of the clathrin chain requires further investigation.