Histone acetylation and chromatin remodeling are required for UV-B-dependent transcriptional activation of regulated genes in maize.

Academic Article


  • The nuclear proteomes of maize (Zea mays) lines that differ in UV-B tolerance were compared by two-dimensional gel electrophoresis after UV light treatment. Differential accumulation of chromatin proteins, particularly histones, constituted the largest class identified by mass spectrometry. UV-B-tolerant landraces and the B73 inbred line show twice as many protein changes as the UV-B-sensitive b, pl W23 inbred line and transgenic maize expressing RNA interference constructs directed against chromatin factors. Mass spectrometic analysis of posttranslational modifications on histone proteins demonstrates that UV-B-tolerant lines exhibit greater acetylation on N-terminal tails of histones H3 and H4 after irradiation. These acetylated histones are enriched in the promoter and transcribed regions of the two UV-B-upregulated genes examined; radiation-sensitive lines lack this enrichment. DNase I and micrococcal nuclease hypersensitivity assays indicate that chromatin adopts looser structures around the selected genes in the UV-B-tolerant samples. Chromatin immunoprecipitation experiments identified additional chromatin factor changes associated with the nfc102 test gene after UV-B treatment in radiation-tolerant lines. Chromatin remodeling is thus shown to be a key process in acclimation to UV-B, and lines deficient in this process are more sensitive to UV-B.
  • Authors

  • Casati, Paula
  • Campi, Mabel
  • Chu, Feixia
  • Suzuki, Nagi
  • Maltby, David
  • Guan, Shenheng
  • Burlingame, Alma L
  • Walbot, Virginia
  • Status

    Publication Date

  • April 2008
  • Published In

  • The Plant Cell  Journal
  • Keywords

  • Acetylation
  • Base Sequence
  • Chromatin
  • DNA Primers
  • Gene Expression Regulation, Plant
  • Histones
  • Mass Spectrometry
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Promoter Regions, Genetic
  • Transcriptional Activation
  • Ultraviolet Rays
  • Zea mays
  • Digital Object Identifier (doi)

    Start Page

  • 827
  • End Page

  • 842
  • Volume

  • 20
  • Issue

  • 4