The function of the σ-factor of Escherichia coli RNA polymerase in template site selection View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1971-09

AUTHORS

Karl Mueller

ABSTRACT

Binding of Escherichia coli RNA polymerase to T4 DNA in the absence or presence of σ-factor was studied, using a “competing template” method determining the amounts of RNA polymerase attached to T4 DNA.RNA polymerase lacking the σ-factor (core enzyme) was found to bind to T4 DNA at a maximum ratio of 22 μg polymerase/μg DNA, suggesting that the amount of core enzyme bound is limited only by space on the template. In the presence of σ-factor, however, polymerase attachment was found to be restricted to a small number of specific template sites. That the σ-factor prevents nonspecific polymerase attachment is also demonstrated by the finding that addition of σ to nonspecifically bound core enzyme stimulates release of the enzyme from the DNA.The results further indicate that σ is also required for a step in the process of chain initiation, subsequent to polymerase attachment. This σ-dependent reaction may be responsible for the fact that RNA polymerase-DNA complexes formed in presence of σ are more stable (dissociation rate constant ≦0.0005 min-1) than those formed in the absence of σ-factor (dissociation rate constant 0.04 min-1).RNA polymerase saturated with σ-factor is heterogeneous with respect to the maximum number of enzyme molecules binding to T4 DNA. A comparison of these numbers with the numbers of template sites utilized for chain initiation (determined by Bremer, 1970) suggeststhat the polymerase binding measured occurs at the template sites at which RNA polymerase having a long functional lifetime initiates transcription; “early quitter” RNA polymerase, characterized by a very short functional lifetime (Müller and Bremer, 1969), seems to form unstable complexes with the DNA which are apparently detected by other binding assays;that the stable polymerase-DNA complexes contain at least two classes of polymerase molecules which seem to bind to the same promoter sites (17/T4 genome) at different multiplicities (1 o4 7 molecules/promoter, respectively). More... »

PAGES

273-296

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00433112

DOI

http://dx.doi.org/10.1007/bf00433112

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031052319

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4935355


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