Article Abstract:
Fine structure of Escherichia coli RNA polymerase (RNAP)-promoter interactions is discussed with proposal of a model in which the alpha subunit contacts UP element DNA through amino acid residues in two helix-hairpin-helix motifs. Information about recognition of the core promoter by sigma(super.70) has been extended by identification of functional groups in the major grooves of the -10 and -35 hexamers in which modifications interfere with RNAP binding. Footprinting studies of RNAP on templates with the rrnB P1 core promoter fused to UP elements of one proximal subsite were carried out. The UP element is a little upstream of the -35 hexamer.
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Article Abstract:
Research has been conducted on C-terminal domain of Escherichia coli RNA polymerase alpha subunit. The authors have investigated specific substitutions in sigma region and in alpha subunit, and report that these substitutions decrease transcription initiation from promoters containing some upstream element DNA.
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Article Abstract:
A study reports an unknown interaction with Escherichia coli ribonucleic acid polymerase (RNAP) that defines an additional recognition element in bacterial promoters. Results indicate that ribosomal RNA (rRNA) promoters create the short-lived complex required for specific responses to the RNAP binding factors ppGpp and DksA by making a non-optimal sigma1.2-discriminator interaction ultimately accounting for regulation of ribosome synthesis.
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