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Self-Association of the Yeast Nucleosome Assembly Protein 1

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    Self-Association of the Yeast Nucleosome Assembly Protein 1
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    Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870
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    Biochemistry

    Cite this: Biochemistry 2004, 43, 32, 10592–10599
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    https://doi.org/10.1021/bi035881b
    Published July 23, 2004
    Copyright © 2004 American Chemical Society
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    Abstract

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    The self-association properties of the yeast nucleosome assembly protein 1 (yNAP1) have been investigated using biochemical and biophysical methods. Protein cross-linking and calibrated gel filtration chromatography of yNAP1 indicate the protein exists as a complex mixture of species at physiologic ionic strength (75−150 mM). Sedimentation velocity reveals a distribution of species of 4.5−12 Svedbergs (S) over a 50-fold range of concentrations. The solution-state complexity is reduced at higher ionic strength, allowing for examination of the fundamental oligomer. Sedimentation equilibrium of a homogeneous 4.5 S population at 500 mM sodium chloride reveals these species to be yNAP1 dimers. These dimers self-associate to form higher order oligomers at more moderate ionic strength. Titration of guanidine hydrochloride converts the higher order oligomers to the homogeneous 4.5 S dimer and then converts the 4.5 S dimers to 2.5 S monomers. Circular dichroism shows that guanidine-mediated dissociation of higher order oligomers into yNAP1 dimers is accompanied by only slight changes in secondary structure. Dissociation of the dimer requires a nearly complete denaturation event.

    Copyright © 2004 American Chemical Society

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    This article is cited by 30 publications.

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    Biochemistry

    Cite this: Biochemistry 2004, 43, 32, 10592–10599
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi035881b
    Published July 23, 2004
    Copyright © 2004 American Chemical Society
    Request reuse permissions

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