TLS Online TPP Program

#Id: 6472


RNA polymerase I requires two ancillary transcription factors to recognize the promoter sequence. The factor that binds to the core promoter is SL1 which consists of four protein subunits. SL1 has primary responsibility for RNA polymerase recruitment









#Unit 3. Fundamental Processes #Eukaryotic Transcription #Part B Pointers
More Pointers
TLS Online TPP Program

#Id: 2446

#Unit 3. Fundamental Processes

One consequence of the rotation of DNA is illustrated In the two-domain model for transcription, as RNA polymerase moves with respect to the double helix, it generates positive supercoils (more tightly wound DNA) ahead of it and leaves negative supercoils (partially unwound DNA) behind it. For each helical turn traversed by RNA polymerase, + 1 turn is generated ahead and -1 turn behind.




TLS Online TPP Program

#Id: 2447

#Unit 3. Fundamental Processes

The enzymes DNA gyrase, which introduces negative supercoils into DNA, and DNA topoisomerase I, which removes negative supercoils in DNA, are required to prevent topological stresses from building up in the course of transcription and replication. 


TLS Online TPP Program

#Id: 2448

#Unit 3. Fundamental Processes

Blocking the activities of gyrase and topoisomerase therefore result in major changes in DNA supercoiling, which in turn affects transcription and replication.


TLS Online TPP Program

#Id: 2449

#Unit 3. Fundamental Processes

In the absence of both activator and repressor, RNA polymerase occasionally binds the promoter spontaneously and initiates a low level (basal level) of transcription. 




TLS Online TPP Program

#Id: 2450

#Unit 3. Fundamental Processes

The lac operator overlaps the promoter, and so the repressor bound to the operator physically prevents RNA polymerase from binding to the promoter and thus initiating RNA synthesis.

TLS Online TPP Program

#Id: 2451

#Unit 3. Fundamental Processes

Allolactose binds to the Lac repressor and triggers a change in the shape (conformation) of that protein.