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M010105200v1
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Papers In Press, published online ahead of print March 1, 2001
J. Biol. Chem, 10.1074/jbc.M010105200
Submitted on November 6, 2000
Revised on February 9, 2001
Accepted on March 1, 2001

The Escherichia coli RNA polymerase-anti s70 AsiA complex utilizes a-CTD upstream promoter contacts to transcribe from a zeta -10-35 » promoter

Gilbert Orsini, Annie Kolb, and Henri Buc

Biologie Moleculaire, Institut Pasteur, 75724, Paris

Corresponding Author: orsini{at}pasteur.fr

During infection of Escherichia coli, phage T4 early protein AsiA inhibits open complex formation by the RNA polymerase holoenzyme Es70 at « -10 -35 » bacterial promoters through binding to region 4.2 of the s70 subunit. We used the -10 -35 lacUV5 promoter to study the properties of the Es70-AsiA complex in the presence of the glutamate anion. Under these experimental conditions, inhibition by AsiA was significantly decreased. KMnO4 probing showed that the observed residual transcription activity was due to the slow transformation of a ternary complex Es70/AsiA/lacUV5 into an open complex. In agreement with this observation, affinity of the enzyme for the promoter was 10-fold lower in the ternary complex than in the binary complex Es70/lacUV5. A t plot analysis of abortive transcription reactions showed that AsiA binding to Es70 resulted in a 120-fold decrease of the second order « on » rate constant of the reaction of Es70 with lacUV5 and a 55- fold decrease in the rate constant of the isomerization step leading to the open complex. This ternary complex still responded to activation by cAMP-CAP. We show that compensatory Es70-promoter upstream contacts involving the C-terminal domains of a subunits in Es70 become essential for the binding of Es70/AsiA to the lacUV5 promoter.


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