Neutron and x-ray scatter studies of the histone octamer and amino and carboxyl domain trimmed octamers.

Wood, Marion; Yau, Peter; Imai, Brian S.; Goldberg, Martin W.; Lambert, Stanley J.; Fowler, Allan; Baldwin, John; Godfrey, Jamie E.; Moudrianakis, Evangelos N.; Koch, M. H. J.

doi:10.1016/s0021-9258(19)67651-9

Cited by 14 publications

(1 citation statement)

References 33 publications

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“…87 At low protein concentrations the refolding and formation of large aggregates occur on time scales that differ by many orders of magnitude, with folding being fast and aggregation being slow. [81][82][83][84][85][86][87] Interestingly, H2A-H2B heterodimers and (H3-H4) 2 heterotetramer are easily formed in the presence of salt, are characterized by stable ordered structures, and possess high resistance toward the urea-and temperature-induced unfolding, 69,[88][89][90][91][92][93] with the conformational stability of these oligomers being dramatically modulated by salt. 89,90,92 The capability of purified histones to assemble into large well-defined periodic superstructures with the shape of bent rods and fibers has been described.…”

Section: Introductionmentioning

confidence: 99%

More than just tails: intrinsic disorder in histone proteins

et al. 2012

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Many biologically active proteins are disordered as a whole, or contain long disordered regions. These intrinsically disordered proteins/regions are very common in nature, abundantly found in all organisms, where they carry out important biological functions. The functions of these proteins complement the functional repertoire of "normal" ordered proteins, and many protein functional classes are heavily dependent on intrinsic disorder. Among these disorder-centric functions are interactions with nucleic acids and protein complex assembly. In this study, we present the results of comprehensive bioinformatics analyses of the abundance and roles of intrinsic disorder in 2007 histones from 746 species. We show that all the members of the histone family are intrinsically disordered proteins. Furthermore, intrinsic disorder is not only abundant in histones, but is absolutely necessary for various histone functions, starting from heterodimerization to formation of higher order oligomers, to interactions with DNA and other proteins, and to posttranslational modifications.

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Section: Introductionmentioning

confidence: 99%

More than just tails: intrinsic disorder in histone proteins

et al. 2012

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Treatment of murine lupus using nucleosomal T cell epitopes identified by bone marrow–derived dendritic cells

Suen¹,

Chuang²,

Tsai³

et al. 2004

Arthritis & Rheumatism

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Objective. Systemic lupus erythematosus (SLE) is characterized by the existence of a heterogeneous group of autoantibodies directed against intact nuclear structures, such as nucleosomes. The most prominent of these autoantibodies are those directed against doublestranded DNA (dsDNA) and histones. The majority are of the IgG isotype and show affinity maturation, both of which are known hallmarks of T cell help. Much evidence suggests that the nucleosome is a major candidate autoantigen in SLE. In this study, a novel strategy was used to identify the critical CD4؉ T cell autoepitopes in nucleosomes. In addition, peptide-based therapy was then performed in a lupus animal model.

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