rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Characterization and expression of histone deacetylase 1 (AtHD1) in Arabidopsis thaliana
  name:
    name part: Fong, Man Kim, 1974-
    role:
      role term: creator
  name:
    name part: Chen, Z. Jeffrey
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2005
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: remote
  abstract: The reversible process of histone acetylation and deacetylation is an important mechanism of epigenetic regulation in the control of gene expression and chromatin structure. In general, histone acetylation is related to gene activation, whereas histone deacetylation is associated with transcriptional gene silencing and maintenance of heterochromatin. A large number of histone deacetylases (HDACs), the enzymes that catalyze the reaction of histone deacetylation, have been identified in plants and other eukaryotes, and they were found to play crucial roles in plant growth and development. In Arabidopsis thaliana, histone deacetylase 1 (AtHD1) is a homolog of Saccharomyces cerevisiae Rpd3 that is a global transcriptional regulator. Downregulation of AtHD1 in transgenic Arabidopsis results in histone hyperacetylation and induces a variety of phenotypic and developmental defects, suggesting that AtHD1 is also a global regulator of many physiological and developmental processes. To characterize the expression pattern and distribution of AtHD1 in cells, the subcellular location of AtHD1 was determined by monitoring the expression of an AtHD1-GFP fusion protein in a transient expression assay and in transgenic Arabidopsis.The results show that AtHD1 is localized in the nucleus and appears to be excluded from the nucleolus. The histone deacetylase activity of AtHD1 was studied in an in vitro assay using radiolabeled histone peptides as a substrate. Recombinant AtHD1 produced by bacteria demonstrated a moderate but significant HDAC activity, whereas that produced by the baculovirus expression system did not have activity. This suggests that AtHD1 may require other cofactors or association with other proteins, rather than post-translational modifications, in order to have full HDAC activity. To study the possible interactions of AtHD1 with other proteins, a recombinant AtHD1 protein with two units of c-myc epitope fused to its C-terminus was expressed in transgenic Arabidopsis…
  note: by Man Kim Fong.
  note: "Major Subject: Molecular and Environmental Plant Sciences"
  note: Title from author supplied metadata (automated record created on Sep. 21, 2005.)
  note: Vita.
  note: Abstract.
  note: Electronic resource.
  note: Mode of access: World Wide Web.
  note: System requirements: World Wide Web access and Adobe Acrobat Reader.
  note: M. S. Texas A&M University 2005.
  note: Includes bibliographical references.
  note: Text (Thesis).
  subject:
    topic: Major Molecular and Enviromental Plant Sciences
  subject:
    topic: chromatin
  subject:
    topic: histone
  subject:
    topic: deacetylase
  identifier: http://hdl.handle.net/1969.1/2365
  record info:
    record content source: TXA
    record creation date: 051005
    record change date: 20151102132914.0
    record identifier: in00002073679