Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4

Andrew Bowman, Tom Owen-Hughes

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

    3 Citations (Scopus)

    Abstract

    The structural characterisation of protein-protein interactions is often challenging. Where interactions are not amenable to high-resolution approaches, alternatives providing lower resolution information are often of value. One such approach is site-directed cross-linking. Here, through the introduction of cysteine residues at strategic locations in histone proteins, we use site-directed cross-linking to monitor the association of chromatin subunits. This approach is informative for the study of both recombinant and native chromatin complexes consisting either of histone subunits alone or in association with accessory proteins, in this case histone chaperones. The approaches described may be generally applicable for monitoring the interactions of a diverse range of multi-protein complexes.
    Original languageEnglish
    Title of host publicationChromatin remodeling
    Subtitle of host publicationmethods and protocols
    EditorsRandall H. Morse
    PublisherHumana Press
    Pages373-387
    Number of pages15
    ISBN (Electronic)9781617794773
    ISBN (Print)9781617794766
    DOIs
    Publication statusPublished - 2012

    Publication series

    NameMethods in Molecular Biology
    PublisherHumana Press
    Volume833
    ISSN (Print)1064-3745

    Fingerprint

    Histones
    Catalytic Domain
    Proteins
    Chromatin
    Histone Chaperones
    Cysteine

    Cite this

    Bowman, A., & Owen-Hughes, T. (2012). Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. In R. H. Morse (Ed.), Chromatin remodeling: methods and protocols (pp. 373-387). (Methods in Molecular Biology; Vol. 833). Humana Press. https://doi.org/10.1007/978-1-61779-477-3_22
    Bowman, Andrew ; Owen-Hughes, Tom. / Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. Chromatin remodeling: methods and protocols. editor / Randall H. Morse. Humana Press, 2012. pp. 373-387 (Methods in Molecular Biology).
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    abstract = "The structural characterisation of protein-protein interactions is often challenging. Where interactions are not amenable to high-resolution approaches, alternatives providing lower resolution information are often of value. One such approach is site-directed cross-linking. Here, through the introduction of cysteine residues at strategic locations in histone proteins, we use site-directed cross-linking to monitor the association of chromatin subunits. This approach is informative for the study of both recombinant and native chromatin complexes consisting either of histone subunits alone or in association with accessory proteins, in this case histone chaperones. The approaches described may be generally applicable for monitoring the interactions of a diverse range of multi-protein complexes.",
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    Bowman, A & Owen-Hughes, T 2012, Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. in RH Morse (ed.), Chromatin remodeling: methods and protocols. Methods in Molecular Biology, vol. 833, Humana Press, pp. 373-387. https://doi.org/10.1007/978-1-61779-477-3_22

    Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. / Bowman, Andrew; Owen-Hughes, Tom.

    Chromatin remodeling: methods and protocols. ed. / Randall H. Morse. Humana Press, 2012. p. 373-387 (Methods in Molecular Biology; Vol. 833).

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

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    Bowman A, Owen-Hughes T. Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. In Morse RH, editor, Chromatin remodeling: methods and protocols. Humana Press. 2012. p. 373-387. (Methods in Molecular Biology). https://doi.org/10.1007/978-1-61779-477-3_22