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ELL facilitates RNA polymerase II pause site entry and release

Author

Listed:
  • Jung S. Byun

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Temesgen D. Fufa

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Clay Wakano

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Alfonso Fernandez

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Cynthia M. Haggerty

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Myong-Hee Sung

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

  • Kevin Gardner

    (Laboratory of Receptor Biology and Gene Expression, National Cancer Institute)

Abstract

Transcription is a multi-stage process that coordinates several steps within the transcription cycle including chromatin reorganization, RNA polymerase II recruitment, initiation, promoter clearance and elongation. Recent advances have identified the super elongation complex, containing the eleven-nineteen lysine-rich leukaemia (ELL) protein, as a key regulator of transcriptional elongation. Here we show that ELL has a diverse and kinetically distinct role before its assembly into the super elongation complex by stabilizing Pol II recruitment/initiation and entry into the pause site. Loss of ELL destabilizes the pre-initiation complexes and results in disruption of early elongation and promoter proximal chromatin structure before recruitment of AFF4 and other super elongation complex components. These changes result in significantly reduced transcriptional activation of rapidly induced genes. Thus, ELL has an early and essential role during rapid high-amplitude gene expression that is required for both Pol II pause site entry and release.

Suggested Citation

  • Jung S. Byun & Temesgen D. Fufa & Clay Wakano & Alfonso Fernandez & Cynthia M. Haggerty & Myong-Hee Sung & Kevin Gardner, 2012. "ELL facilitates RNA polymerase II pause site entry and release," Nature Communications, Nature, vol. 3(1), pages 1-11, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms1652
    DOI: 10.1038/ncomms1652
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