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Transcriptional Arrest - Escherichia Coli Rna Polymerase Translocates Backward, Leaving the 3' End of the Rna Intact and Extruded

  1. Author:
    Komissarova, N.
    Kashlev, M.

  2. Author Address

    Kashlev M NCI FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM BLDG 539 ROOM 222 FREDERICK, MD 21702 USA NCI FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM FREDERICK, MD 21702 USA PUBL HLTH RES INST NEW YORK, NY 10016 USA
    1. Year: 1997
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 94
    2. 5
    3. Pages: 1755-1760
  4. Type of Article: Article
  1. Abstract:

    RNA polymerase (RNAP) may become arrested during transcript elongation when ternary complexes remain intact but further RNA synthesis is blocked, Using a combination of DNA and RNA footprinting techniques, we demonstrate that the loss of catalytic activity upon arrest of Escherichia coli RNAP is accompanied by an isomerization of the ternary complex in which the enzyme disengages from the 3' end of the transcript and moves backward along the DNA with concomitant reverse threading of the intact RNA through the enzyme. The reversal of RNAP brings the active center to the internal RNA position and thereby it represents a step in factor-facilitated transcript cleavage. Secondary structure elements or the 5' end of the transcript can prevent the isomerization by blocking the RNA threading. The described novel property of RNAP has far-reaching implications for the understanding of the elongation mechanism and gene regulation. [References: 26]

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