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Why is TBP considered to be a universal transcription factor?

Short Answer

Expert verified

A TBP mutant that is deficient for TATA box-binding can nonetheless facilitate in vitro transcriptional initiation by both RNAP I and RNAP III with certain class II TATA-less promoters. Therefore, TBP is the only known universal transcription factor.

Step by step solution

01

Introduction

To initiate transcription at their respective promoters, RNAP I and RNAP III require different sets of GTFs from each other and from RNAP II. This is not surprising, given the three types of promoters' highly diverse organizational structures. TATA boxes are absent from nearly all promotersrecognized by RNAP I (class I promoters) and nearly all promoters recognized by RNAP III (class III promoters).

02

TBP as a universal transcription factor

When it was discovered that TBP is required for both RNAP I and RNAP III initiation, it came as a shock. TBP participates by forming the GTFs SLI (with class I promoters) and TFIIIB (with class III promoters) by combining with various sets of TAFs. A TBP mutant that is faulty for TATA box-binding, like certain class II TATA-less promoters, can still support in vitro transcriptional initiation by both RNAP I and RNAP III. TBP, the only known universal transcription factor, is clearly a protein with a wide range of applications.

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Most popular questions from this chapter

If an enhancer is placed on one plasmid and its corresponding promoter is placed on a second plasmid that is catenated (linked) with the first, initiation is almost as efficient as when the enhancer and promoter are on the same plasmid. However, initiation does not occur when the two plasmids are unlinked. Explain.

The RNA polymerase from bacteriophage T7differs structurally from prokaryotic and eukaryotic RNAPs and is extremely specific for its own promoter. Why do these properties make T7RNAP useful in experiments with recombinant DNA?

What is the advantage of starting RNA processing before transcription is complete?

The bacterial enzyme polynucleotide phosphorylase (PNPase) is a 3'โ†’5' exoribonuclease that degrades mRNA. (a) The enzyme catalyzes a phosphorolysis reaction, as does glycogen phosphorylase (Section 16-1), rather than hydrolysis. Write an equation for the mRNA phosphorolysis reaction. (b) In vitro, PNPase also catalyzes the reverse of the phosphorolysis reaction. What does this reaction accomplish and how does it differ from the reaction carried out by RNA polymerase? (c) PNPase includes a binding site for long ribonucleotides, which may promote the enzyme's processivity. Why would this be an advantage for the primary activity of PNPase in vivo?

Question: Certain E. coli bacteriophages encode a protein called Q, which binds to RNAP shortly after transcription initiation but before ฯƒ70 is released. Q increases the rate of transcription and renders RNAP resistant to Rho-dependent termination. (a) Explain how Q could enhance expression of bacteriophage genes. (b) Explain why the effect of Q depends on its ability to interact with specific DNA sequences, not just RNAP .

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