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RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells.

H2B ubiquitylation has been implicated in active transcription but is not well understood in mammalian cells. Beyond earlier identification of hBRE1 as the E3 ligase for H2B ubiquitylation in human cells, we now show (1) that hRAD6 serves as the cognate E2-conjugating enzyme; (2) that hRAD6, through direct interaction with hPAF-bound hBRE1, is recruited to transcribed genes and ubiquitylates chromatinized H2B at lysine 120; (3) that hPAF-mediated transcription is required for efficient H2B ubiquitylation as a result of hPAF-dependent recruitment of hBRE1-hRAD6 to the Pol II transcription machinery; (4) that H2B ubiquitylation per se does not affect the level of hPAF-, SII-, and p300-dependent transcription and likely functions downstream; and (5) that H2B ubiquitylation directly stimulates hSET1-dependent H3K4 di- and trimethylation. These studies establish the natural H2B ubiquitylation factors in human cells and also detail the mechanistic basis for H2B ubiquitylation and function during transcription.

Pubmed ID: 19410543

Authors

  • Kim J
  • Guermah M
  • McGinty RK
  • Lee JS
  • Tang Z
  • Milne TA
  • Shilatifard A
  • Muir TW
  • Roeder RG

Journal

Cell

Publication Data

May 1, 2009

Associated Grants

  • Agency: NCI NIH HHS, Id: CA113872
  • Agency: NCI NIH HHS, Id: CA129325
  • Agency: NIDDK NIH HHS, Id: DK071900
  • Agency: NCI NIH HHS, Id: R01 CA089455
  • Agency: NCI NIH HHS, Id: R01 CA113872
  • Agency: NCI NIH HHS, Id: R01 CA113872-03
  • Agency: NCI NIH HHS, Id: R01 CA113872-04
  • Agency: NCI NIH HHS, Id: R01 CA129325
  • Agency: NCI NIH HHS, Id: R01 CA129325-01
  • Agency: NCI NIH HHS, Id: R01 CA129325-02
  • Agency: NCI NIH HHS, Id: R01 CA150265
  • Agency: NIDDK NIH HHS, Id: R01 DK071900
  • Agency: NIDDK NIH HHS, Id: R01 DK071900-03
  • Agency: NIDDK NIH HHS, Id: R01 DK071900-04
  • Agency: NIGMS NIH HHS, Id: R01 GM069905

Mesh Terms

  • Animals
  • Cell Line
  • DNA Polymerase II
  • Histone-Lysine N-Methyltransferase
  • Histones
  • Humans
  • Methylation
  • Nuclear Proteins
  • Transcriptional Activation
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligases
  • Ubiquitination