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The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins

Author

Listed:
  • George Orphanides

    (Howard Hughes Medical Institute
    University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School)

  • Wei-Hua Wu

    (University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School)

  • William S. Lane

    (Harvard Microchemistry Facility, Harvard University)

  • Michael Hampsey

    (University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School)

  • Danny Reinberg

    (Howard Hughes Medical Institute
    University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School)

Abstract

The regulation of gene expression depends critically upon chromatin structure1. Transcription of protein-coding genes can be reconstituted on naked DNA with only the general transcription factors and RNA polymerase II (ref. 2). This minimal system cannot transcribe DNA packaged into chromatin, indicating thataccessory factors may facilitate access to DNA. Two classes of accessory factor, ATP-dependent chromatin-remodelling enzymes3 and histone acetyltransferases4, facilitate transcription initiation from chromatin templates. FACT (for facilitates chromatin transcription) is a chromatin-specific elongation factor required for transcription of chromatin templates in vitro5,6. Here we show that FACT comprises a new human homologue of the Saccharomyces cerevisiae Spt16/Cdc68 protein and the high-mobility group-1-like protein structure-specific recognition protein-1. Yeast SPT16/CDC68 is an essential gene that has been implicated in transcription and cell-cycle regulation. Consistent with our biochemical analysis of FACT, we provide evidence that Spt16/Cdc68 is involved in transcript elongation in vivo. Moreover, FACT specifically interacts with nucleosomes and histone H2A/H2B dimers, indicating that it may work by promoting nucleosome disassembly upon transcription. In support of this model, we show that FACT activity is abrogated by covalently crosslinking nucleosomal histones.

Suggested Citation

  • George Orphanides & Wei-Hua Wu & William S. Lane & Michael Hampsey & Danny Reinberg, 1999. "The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins," Nature, Nature, vol. 400(6741), pages 284-288, July.
  • Handle: RePEc:nat:nature:v:400:y:1999:i:6741:d:10.1038_22350
    DOI: 10.1038/22350
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    Cited by:

    1. Anfeng Luo & Jingwei Kong & Jun Chen & Xue Xiao & Jie Lan & Xiaorong Li & Cuifang Liu & Peng-Ye Wang & Guohong Li & Wei Li & Ping Chen, 2023. "H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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