title: Footprint of the sigma protein: a re-examination.
abstract: Escherichia coli RNA Polymerase is a multi-subunit enzyme that catalyzes RNA synthesis, using DNA as a template. The sigma subunit of this enzyme plays an important role in the recognition of promoter sites on DNA. Using DNase I footprinting, Utpala Ramesh and Claude F. Meares [(1989) Biochem. Biophys. Res. Comm. 160, 121-125] reported that in the absence of the other subunits, sigma binds specifically to the bacteriophage lambda PR promoter DNA sequence. We are unable to reproduce that result.
authors.affiliation: Chemistry Department, University of California, Davis 95616.
authors.forename: A
authors.initials: A
authors.lastname: Wellman
authors.forename: C F
authors.initials: CF
authors.lastname: Meares
mesh_terms: D010582:Bacteriophage lambda / Q000235:genetics; D012321:DNA-Directed RNA Polymerases / Q000302:isolation & purification / Q000378:metabolism*; D003850:Deoxyribonuclease I; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D009710:Nucleotide Mapping; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D012808:Sigma Factor / Q000302:isolation & purification / Q000378:metabolism*; D013698:Templates, Genetic
chemical_list: D046911:Macromolecular Substances; D012808:Sigma Factor; D012321:DNA-Directed RNA Polymerases; D003850:Deoxyribonuclease I