Equilibrium dissociation constant for specific binding of RNAP to phage T7 promoter

Value 3 nM
Organism Bacteria Escherichia coli
Reference Bintu L, Buchler NE, Garcia HG, Gerland U, Hwa T, Kondev J, Phillips R. Transcriptional regulation by the numbers: models. Curr Opin Genet Dev. 2005 Apr15(2):116-24. p.118 caption of fig.1cPubMed ID15797194
Primary Source [39] Dayton CJ, Prosen DE, Parker KL, Cech CL. Kinetic measurements of Escherichia coli RNA polymerase association with bacteriophage T7 early promoters. J Biol Chem. 1984 Feb 10 259(3):1616-21.PubMed ID6363413
Method Primary source abstract: "The binding constant for the initial association of polymerase with promoters and the forward rate of isomerization to an "open" complex capable of initiation have been measured for the A1, A3, C, and D promoters using the abortive initiation reaction."
Comments P.118 caption to fig.1c: "In particular, making the simplest assumption that the genomic background for RNAP is given only by the non-specific binding of RNAP with DNA, we take K[NS]pd=10 000 nM [ref 37], for the lac promoter K[S]pd=550 nM [BNID 103590] and for the T7 promoter, K[S]pd=3nM [primary source]. For the lac promoter, this results in Δɛpd=-2.9kBT and for the T7 promoter, Δɛpd=-8.1kBT."
Entered by Uri M
ID 103592