Journal ArticleDOI
Condensation of DNA by the C-terminal domain of histone H1. A circular dichroism study.
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TLDR
It is concluded that the condensation of DNA mediated by histone H1 is mainly due to its C-terminal domain, which is characterized by a nonconservative circular dichroism spectrum which is currently attributed to ordered aggregation of the DNA molecules.About:
This article is published in Biophysical Chemistry.The article was published on 1985-06-01. It has received 33 citations till now. The article focuses on the topics: Circular dichroism & DNA condensation.read more
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Nucleocytoplasmic transport of DNA: enhancing non-viral gene transfer
Kylie M. Wagstaff,David A. Jans +1 more
TL;DR: This review focuses on the nucleocytoplasmic delivery of DNA and mechanisms to enhance to non-viral-mediated gene transfer.
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Histonefection: Novel and potent non-viral gene delivery.
TL;DR: This work has found that histones efficiently mediate gene transfer (histonefection) and appears to have particular promise in cancer gene transfer and therapy.
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Induction of secondary structure in a COOH-terminal peptide of histone H1 by interaction with the DNA: an infrared spectroscopy study.
TL;DR: The results support the presence of inducible helical and turn elements, both sharing the character of DNA-binding motifs.
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Repeat peptide motifs which contain beta-turns and modulate DNA condensation in chromatin.
TL;DR: The H1 repeat adopts a more rigid beta-turn-containing structure which probably binds to the DNA minor groove as assessed by competition with the drug Hoechst 33258 and is enhanced by the nucleolin repeat which by itself does not promote any alteration in DNA conformation.
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Definition of a C-reactive protein binding determinant on histones.
TL;DR: CRP binding was not diminished by cleavage of the C-terminal fragment but was greatly decreased when the central globular region of H2A was tested, which is the first reported CRP binding determinant on a protein.
References
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Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.
TL;DR: It is concluded that H1 stabilizes the nucleosome and is located in the region of the exit and entry points of the DNA in H1-depleted chromatin, which has the form of an unravelled filament.
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Studies on histones. 7. Preparative methods for histone fractions from calf thymus.
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The structure of histone H1 and its location in chromatin.
TL;DR: On the basis of their primary structure, the lysine-rich histones are a unified family of proteins that are protected from trypsin digestion in chromatin and corresponds to the segment of highest sequence conservation.
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Action of micrococcal nuclease on chromatin and the location of histone H1
Markus Noll,Roger D. Kornberg +1 more
TL;DR: Digestion of rat liver chromatin with micrococcal nuclease at 2°C yields fragments containing multiples of 198±6 base-pairs, which represents the DNA content of a unit of the structure, which suggests an association of H1 with the region of DNA that links adjacent units of theructure.