65
views
0
recommends
+1 Recommend
0 collections
    8
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Histone acetylation in chromatin structure and transcription.

      Nature
      Acetylation, Animals, Chromatin, chemistry, metabolism, physiology, Forecasting, Gene Expression Regulation, Heterochromatin, Histones, Humans, Protein Conformation, Transcription, Genetic

      Read this article at

      ScienceOpenPublisherPubMed
      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.

          Abstract

          'The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle. These acetylation patterns may direct histone assembly and help regulate the unfolding and activity of genes.

          Related collections

          Most cited references58

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

          The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases

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

            The CBP co-activator is a histone acetyltransferase.

            The CBP protein acts as a transcriptional adaptor for many different transcription factors by directly contacting DNA-bound activators. One mechanism by which CBP is thought to stimulate transcription is by recruiting the histone acetyltransferase (HAT) P/CAF to the promoter. Here we show that CBP has intrinsic HAT activity. The HAT domain of CBP is adjacent to the binding site for the transcriptional activator E1A. Although E1A displaces P/CAF from CBP, it does not disrupt the CBP-associated HAT activity. Thus E1A carries HAT activity when complexed with CBP. Targeting CBP-associated HAT activity to specific promoters may therefore be a mechanism by which E1A acts as a transcriptional activator.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p

              Trapoxin is a microbially derived cyclotetrapeptide that inhibits histone deacetylation in vivo and causes mammalian cells to arrest in the cell cycle. A trapoxin affinity matrix was used to isolate two nuclear proteins that copurified with histone deacetylase activity. Both proteins were identified by peptide microsequencing, and a complementary DNA encoding the histone deacetylase catalytic subunit (HD1) was cloned from a human Jurkat T cell library. As the predicted protein is very similar to the yeast transcriptional regulator Rpd3p, these results support a role for histone deacetylase as a key regulator of eukaryotic transcription.
                Bookmark

                Author and article information

                Comments

                Comment on this article