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Stability and structure of clathrin.

H Edelhoch, K Prasad, R E Lippoldt

    Biochemistry
    |May 8, 1984
    PubMed
    Summary
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    Urea dissociates clathrin (8 S) light chains, allowing coat structure reformation after urea removal. Higher urea concentrations disrupt secondary and tertiary structures, revealing two distinct transitions and suggesting independent domains within clathrin heavy chains.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Molecular Biophysics

    Background:

    • Clathrin (8 S) is a protein complex essential for cellular vesicle formation.
    • Understanding clathrin's structural dynamics is crucial for elucidating its function in endocytosis.

    Purpose of the Study:

    • To investigate the effects of urea on clathrin dissociation and structural transitions.
    • To characterize the stability and domain organization of clathrin heavy chains.

    Main Methods:

    • Light scattering
    • Ultracentrifugation
    • Column chromatography
    • Tryptophan polarization
    • Emission maxima
    • Circular dichroism
    • Difference spectroscopy

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  • Sedimentation

    • Main Results:

    • Urea at 3 M dissociates clathrin light chains, preserving coat structure upon urea removal.
    • Higher urea concentrations (above 3 M) eliminate secondary and tertiary structures.
    • Two distinct urea-induced transitions were observed, one between 3-6 M and another starting at 7 M.
    • Aggregation of clathrin chains occurred in 4-5 M urea solutions.
    • Results suggest two independent domains within clathrin heavy chains, each with a cooperative transition.

    Conclusions:

    • Clathrin's dissociation and structural integrity are modulated by urea concentration.
    • The heavy chains of clathrin likely possess two distinct, independently folding domains.