Why does the positive regulation in bacteriophage λ affect isomerization of the RNAP-DNA complex?
نویسندگان
چکیده
The initiation of transcription involves three steps: binding, opening, and escape of RNA polymerase. To model these steps in the simplest way we will treat opening and escape as a single reaction with forward reaction rate k determined by the regulatory proteins and their interaction with the DNA. Binding will be treated as a reversible reaction with an equilibrium constant KB. Using mathematical models, it is demonstrated that in the phage λ induction the binding constant KB plays a fundamentally different role from the opening and clearing constant k. In particular modifications in KB cannot be directly compensated for by modifications in k and vice versa.
منابع مشابه
Structural basis of transcription arrest by coliphage HK022 Nun in an Escherichia coli RNA polymerase elongation complex
Coliphage HK022 Nun blocks superinfection by coliphage λ by stalling RNA polymerase (RNAP) translocation specifically on λ DNA. To provide a structural framework to understand how Nun blocks RNAP translocation, we determined structures of Escherichia coli RNAP ternary elongation complexes (TECs) with and without Nun by single-particle cryo-electron microscopy. Nun fits tightly into the TEC by t...
متن کاملStructure of Escherichia coli RNA polymerase holoenzyme at last.
Much of the mechanistic foundations of our knowledge of regulation of gene expression at the transcriptional level have been provided by Escherichia coli and its phages. E. coli RNA polymerase (EcoRNAP) is a multisubunit enzyme composed of a catalytically active core (β′βα2ω); subunits that are evolutionarily related to β′, β, α, and ω are present in DNA-dependent RNAPs of all organisms. In bac...
متن کاملKinetics of the specific binding of a second RNA polymerase to the standard bacterial-transposon-Tn3 bla promoter complex.
It was shown previously, that at moderate excess of RNA polymerase (RNAP) relative to DNA, the complex of the bla promoter from bacterial transposon Tn3 with RNAP is locked in an inactive, heparin-resistant, isomeric state which is not that of the 'open' complex. This 1:1 isomer can accommodate a second RNAP, which becomes tightly and specifically bound just upstream of the first RNAP [Duval-Va...
متن کاملStructural basis of transcription inhibition by antibiotic streptolydigin.
Streptolydigin (Stl) is a potent inhibitor of bacterial RNA polymerases (RNAPs). The 2.4 A resolution structure of the Thermus thermophilus RNAP-Stl complex showed that, in full agreement with the available genetic data, the inhibitor binding site is located 20 A away from the RNAP active site and encompasses the bridge helix and the trigger loop, two elements that are considered to be crucial ...
متن کاملMolecular basis of RNA polymerase promoter specificity switch revealed through studies of Thermus bacteriophage transcription regulator
Transcription initiation is the central point of gene expression regulation. Understanding of molecular mechanism of transcription regulation requires, ultimately, the structural understanding of consequences of transcription factors binding to DNA-dependent RNA polymerase (RNAP), the enzyme of transcription. We recently determined a structure of a complex between transcription factor gp39 enco...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2008