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Nucleic Acids Research, 1981, Vol. 9, No. 11 2517-2533
© 1981

MOLECULAR BIOLOGY

Characterization of the ß-lactamase promoter of pBR322

David R. Russell and George N. Bennett

Department of Biochemistry, Rice University Houston, TX 77001, USA

Received March 30, 1981. The ß-lactamase promoter of pBR322, derived from Tn3, has been characterized using several techniques. The transcription initiation site islocated 35 base pairs from the translation initiation codon of ß-lactamase. The mRNA produced in vitro has a 51 pppGpA terminus. RNA polymerase bound at this start site protects a region from about –50 to +20 from DNA ase I cleavage using the foot printing technique. RNA polymerase binds rapidly to the (ß-lactamase promoter. The half-time of association is less than one-half minute. The half-time of dissociation is approximately 6 hr. A study of the binding of RNA polymerase at different temperatures showed a large change between 11° and 15°C. Comparison of these parameters with those reported for other promoters is discussed.


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