TLS Online TPP Program

#Question id: 4350


Portions of the DNA sequences of normal and mutant b-globin genes are shown. The most plausible explanation for why the indicated mutation (changing an A to a G) results in the disease b-thalassemia is that the mutation

#Unit 3. Fundamental Processes
  1. changes the amino acid specified by the codon of which the altered base is part

  2. generates a recognition site for a restriction enzyme, so the gene is cut in two

  3. creates a new splice site, so that a portion of the intron is not removed

  4. results in an increase in the transcription of the b-globin gene

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TLS Online TPP Program

#Question id: 4481

#Unit 3. Fundamental Processes

Choose correct statements about recognition mechanism of TBP ;

A. TBP causes the minor groove to be widened to an almost flat conformation

B. It also bends the DNA by an angle of ~120o

C. The interaction between TBP and DNA involves maximum number of hydrogen bonds between the protein and the edges of the base.

D. Much of the specificity is imposed by two pairs of phenylalanine side chains that intercalate between the base pairs at either end of the recognition sequence and drive the strong bend in the DNA.

TLS Online TPP Program

#Question id: 4482

#Unit 3. Fundamental Processes

The General Transcription Factors of RNA Polymerase, with their subunits, select correct matching

A.     TBP

      1

B.     TFIA

      11

C.     TAFs

       2

D.     TFIIH

      10

TLS Online TPP Program

#Question id: 4483

#Unit 3. Fundamental Processes

TAF42 and TAF62 from Drosophila form a structure similar to that of the

TLS Online TPP Program

#Question id: 4484

#Unit 3. Fundamental Processes

Match General Transcription Factors with their functions;

    i. TAFs

 A. Appears to regulate the binding of TBP to DNA. It does this using an inhibitory flap that binds to the DNA-binding surface of TBP, another example of molecular mimicry. This flap must be displaced for TBP to bind TATA.

  ii. TFIIB

B. Insert into the RNA-exit channel and active center cleft of Pol II in a manner analogous to the sigma region 3/4 linker in the bacterial case.

  iii. TFIIH

 C.  As an ATP-driven translocator of double-stranded DNA.

   iv. TFIIF

D. This two-subunit (in humans) factor associates with Pol II and is recruited to the promoter together with that enzyme.

TLS Online TPP Program

#Question id: 4485

#Unit 3. Fundamental Processes

In multicellular organisms, regulatory sequences can spread thousands of nucleotides from the promoter—both upstream and downstream—and can be made up of tens of regulator binding sites. Often, these binding sites are grouped in units called_?

TLS Online TPP Program

#Question id: 4486

#Unit 3. Fundamental Processes

Activators can recruit factors needed for polymerase to initiate or elongate transcription. In all of these functions, the activator is merely recruiting proteins to the promoter. In bacteria, RNA polymerase is the only protein that needs to be recruited; this is not the case in eukaryotes. Indeed, in eukaryotes, a given activator might work in all three ways:

 1.    Recruitment of nucleosome modifiers and remodelers

i.     “open” the promoter

 2.    Recruitment of general transcription factors and mediators

ii.      That stimulate Pol II initiation and elongation

 3.       Recruitment of protein complexes

iii.     To recruit PTEFb/SEC