Blog
About

6
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      Electrostatics of DNA compaction in viruses, bacteria and eukaryotes: functional insights and evolutionary perspective

      Read this article at

      ScienceOpenPublisher
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Related collections

          Most cited references 238

          • Record: found
          • Abstract: found
          • Article: not found

          Chromatin modifications and their function.

          The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each class. Operationally, modifications function either by disrupting chromatin contacts or by affecting the recruitment of nonhistone proteins to chromatin. Their presence on histones can dictate the higher-order chromatin structure in which DNA is packaged and can orchestrate the ordered recruitment of enzyme complexes to manipulate DNA. In this way, histone modifications have the potential to influence many fundamental biological processes, some of which may be epigenetically inherited.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Crystal structure of the nucleosome core particle at 2.8 A resolution.

            The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Histone H4-K16 acetylation controls chromatin structure and protein interactions.

              Acetylation of histone H4 on lysine 16 (H4-K16Ac) is a prevalent and reversible posttranslational chromatin modification in eukaryotes. To characterize the structural and functional role of this mark, we used a native chemical ligation strategy to generate histone H4 that was homogeneously acetylated at K16. The incorporation of this modified histone into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions. H4-K16Ac also inhibits the ability of the adenosine triphosphate-utilizing chromatin assembly and remodeling enzyme ACF to mobilize a mononucleosome, indicating that this single histone modification modulates both higher order chromatin structure and functional interactions between a nonhistone protein and the chromatin fiber.
                Bookmark

                Author and article information

                Journal
                SMOABF
                Soft Matter
                Soft Matter
                Royal Society of Chemistry (RSC)
                1744-683X
                1744-6848
                2012
                2012
                : 8
                : 36
                : 9285
                Article
                10.1039/c2sm25789k
                © 2012
                Product
                Self URI (article page): http://xlink.rsc.org/?DOI=c2sm25789k

                Comments

                Comment on this article