Spatial arrangement of δ-factor and core enzyme of Escherichia coli RNA polymerase. A neutron solution scattering study

H. Lederer, K. Mortensen, R.P. May, G. Baer, H.L. Crespi, D. Dersch, H. Heumann

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    Abstract

    By means of neutron solution scattering we determined the position and orientation of core enzyme and σ-factor within the Escherichia coli RNA polymerase holoenzyme with the aim of improving existing models. The individual components, core enzyme (E) and σ-factor (σ), were highlighted by deuterium labeling and their center-to-center distances determined in the monomeric and the dimeric holoenzyme. The following distance parameters were obtained: dE1 − σ1 = 8.6(± 1) nm, dE1 − E2 = 11.5(± 1) nm, dσ1 − σ2 = 12.0(±0.7) nm, dE1 − σ2 = 9(± 3) nm. Using a triangulation procedure the position of the σ-factors, σ1 and σ2, were determined with respect to the mass center of the core enzyme molecules, E1 and E2 assuming a symmetrical arrangement of the holoenzyme molecules in the dimer (C2 symmetry). In addition, the orientation of the σ-factor with respect to core enzyme was estimated by means of model calculations. The obtained model of holoenzyme depicts the σ-factor as buried in a groove of core enzyme, probably between the large subunits β′ and β.
    Original languageEnglish
    JournalJournal of Molecular Biology
    Volume219
    Issue number4
    Pages (from-to)747-755
    ISSN0022-2836
    DOIs
    Publication statusPublished - 1991

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