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mam. Hehe. Nga pala mam, di ko nasagot number 5 tsaka 33. Ndi ko mahanap. May
module mam akong nadownload. Tingin ko dun binase ung questions, eto ung link mam.
http://trishul.sci.gu.edu.au/courses/bbs2710/Module_Notes.doc

1. The relationship between the genotype and phenotype is a simple one

The genotype codes for the phenotype. The "internally coded, inheritable
information", or Genotype, carried by all living organisms, holds the critical instructions
that are used and interpreted by the cellular machinary of the cells to produce the
"outward, physical manifestation", or Phenotype of the organism.
2.

3. Feedback inhibition is accomplished in two ways: via allosteric

regulation(noncompetitive inhibition), whereby an inhibitor binds to a site distant from
the active site and causes a conformational change in the enzyme thereby decreasing
its ability to bind with the substrate and hence catalyze the reaction, or via competitive
inhibition where the inhibitor binds to the active site, directly preventing the formation of
an enzyme-substrate complex. Allosteric enzymes are generally intricate molecules,
composed of at least two protein subunits; conformational changes occur when allosteric
sites are filled, thereby changing the shape of the active site itself.

4.
5.
6. Catabolite repression is a type ofpositive control of transcription, since a regulatory protein
affects anincrease (upregulation) in the rate of transcription of an operon. The process was
discovered in E. coli and was originally referred to as the glucose effectbecause it was found
that glucose repressed the synthesis of certain inducible enzymes, even though the inducer
of the pathway was present in the environment.
7. Quorum sensing is a system of stimuli and response correlated to population density. Many
species of bacteria use quorum sensing to coordinate gene expression according to the
density of their local population. In similar fashion, some social insects use quorum sensing
to determine where to nest. In addition to its function in biological systems, quorum sensing
has several useful applications for computing and robotics.
8.
Two dimeric chemoreceptors methyl-accepting chemotaxis proteins (MCPs) are shown, one of
which is interacting with a periplasmic binding protein (PBP). In addition, two chemotaxis protein
(Che)W monomers and a CheA dimer are shown interacting with the highly conserved signalling
domain of the MCPs in the cytoplasm. It should be noted that, given the packing within MCP clusters
and the calculations of the number of chemosensory proteins, the actual arrangement will be
different. One CheA monomer will probably not interact with one MCP dimer, and instead a CheA
dimer might span several receptors. A decrease in attractant concentration induces trans-
autophosphorylation of the CheA dimer, which phosphorylates the response regulator CheY.
Phosphorylated CheY then binds to the flagellar motor to bring about a change in direction.
Phosphorylated CheA also phosphorylates another response regulator the methylesterase CheB.
Phosphorylated CheB competes with a constitutive methyltransferase, CheR, to control the degree
of methylation of specific glutamates in the MCPs. This resets the signalling state of the receptors
and allows them to adapt to the present concentration of attractant and to sense subsequent
changes. The dephosphorylation of phosphorylated CheY is accelerated by the phosphatase CheZ. P,
phosphoryl group.
9. In bacterial cells, enzymatic reactions may be regulated by two unrelated modes: (1) control
or regulation of enzyme activity (feedback inhibition orend product inhibition), which
mainly operates to regulate biosynthetic pathways; and (2) control or regulation of enzyme
synthesis, including end-product repression, which functions in the regulation of biosynthetic
pathways, and enzyme induction and catabolite repression, which regulate mainly degradative
pathways. The process of feedback inhibition regulates the activity of preexisting enzymes in the
cells. The processes of end-product repression, enzyme induction and catabolite repression are
involved in the control of synthesis of enzymes. The processes which regulate the synthesis of
enzymes may be either a form of positive control or negative control. End-product repression and
 enzyme induction are mechanisms of negative control because they lead to a decrease in the
rate of transcription of proteins. Catabolite repression is considered a form of positive
control because it affects anincrease in rates of transcription of proteins.
10. Enzymes are biological molecules (proteins) that act as catalysts and help complex
reactions occur everywhere in life. Let's say you ate a piece of meat. Proteases would
go to work and help break down the peptide bonds between the amino acids.
active site is the region of an enzyme where substrate molecules bind and undergo a
chemical reaction.
Allosteric enzymes are enzymes that change their conformational ensemble upon
binding of an effector, which results in an apparent change in binding affinity at a
different ligand binding site.
A ligand is a substance that forms a complex with a biomolecule to serve a biological
purpose.
An enzyme modulator is a type of drug which modulates enzymes. They include enzyme
inhibitors and enzyme inducers. In an homogenous assay, "an enzyme modulator ...
iscovalently linked to the ligand which competes with free ligand from the test sample for the
available antibodies.
Allosteric enzymes are enzymes that change their conformational ensemble upon
binding of an effector, which results in an apparent change in binding affinity at a
different ligand binding site.
Competitive inhibition is a form of enzymeinhibition where binding of the inhibitor to
the active site on the enzyme prevents binding of the substrate and vice versa. Most
competitive inhibitors function by binding reversibly to the active site of the enzyme.

11.

Figure Error! No text of specified style in document.:1 Enzyme catalysis

The figure above illustrates the process of catalysis carried out by a generic enzyme. A
substrate binds to the active site of the enzyme and the products are released leaving the
enzyme ready to repeat the process. The small, unexplained site in the lower left-hand corner
may be a second binding site. This second site does not bind the substrate that is catalysed by
the enzyme; rather it binds a molecule that modulates the activity of the enzyme.

12. Allosteric control is an extremely important mechanism for cellular

regulation. Allosteric enzymes play a pivotal role in cells because they
have two functions they not only catalyze reactions in metabolic
pathways, but also control the rates of these pathways. Regulation by
allosteric enzymes involves the binding of signaling molecules to specific
regulatory sites, and this binding induces conformational changes which
result in alterations in catalytic activity.
13. TRUE. Allosteric enzymes have two binding sites. One is the active site where the
catalysis of the product occurs (i.e. this is the basic function of the enzyme). The second
site is where the allosteric effector binds and the kinetics of this site are independent of
the active site. When the effector binding site is open, the conformation of the enzyme is
such that substrate can bind to the active site and catalysis can occur. The binding of
the effector molecule to the specific effector binding site results in a conformational
change in the enzyme effectively closing the active site and reducing (or eliminating) the
enzymes ability to catalyse the substrate.

14. There are two types of allosteric effectors: positive allosteric effectors and negative allosteric
effectors. The positive ones activate something, whereas the negative ones inactivate
 something.
A negative allosteric regulator can be both good or bad. An example of a good one would be like
feedback inhibition. If a certain pathway in the body is making too much of something, then the
product of the pathway will come back and inhibit one of the earlier enzymes thereby saving
energy. An example of a bad one would be if some kind of drug were administered in the body
where it inhibits something it's not supposed to.

A positive allosteric effector could also be good or bad.

An example of a good one would be if an enzyme is being activated to make something that's
deficient in the cell. An example of a bad one would be when the allosteric effector is working
when it's not supposed to.
In general, when the allosteric effect is a result of some natural physiological response, then it's
usually a good thing whether it's an activator or an inhibitor.

15. The regulation of branched pathways is more complicated because the concentration of
two products must be accounted for. In fact, several intricate feedback mechanisms have
been found in branched biosynthetic pathways.

Feedback Inhibition and Activation

Consider, for example, the biosynthesis of the amino acids valine, leucine, and
isoleucine. A common intermediate, hydroxyethyl thiamine pyrophosphate (hydroxyethyl-
TPP; Section 17.1.1), initiates the pathways leading to all three of these amino acids.
Hydroxyethyl-TPP can react with -ketobutyrate in the initial step for the synthesis of isoleucine.
Alternatively, hydroxyethyl-TPP can react with pyruvate in the committed step for the pathways
leading to valine and leucine. Thus, the relative concentrations of -ketobutyrate and pyruvate
determine how much isoleucine is produced compared with valine and leucine. Threonine
deaminase, the PLP enzyme that catalyzes the formation of -ketobutyrate, is allosterically
inhibited by isoleucine (Figure 24.22). This enzyme is also allosterically activated by valine.
Thus, this enzyme is inhibited by the product of the pathway that it initiates and is activated by
the end product of a competitive pathway. This mechanism balances the amounts of different
amino acids that are synthesized.

16. central dogma of molecular biology definition

Describes a key assumption of molecular
biology, namely, that each gene inthe DNA molecule carries the information nee
ded to construct one protein,which, acting as an enzyme, controls one chemical
reaction in the cell.
17. Gene expression is the process by which the genetic code - the nucleotide sequence - of a gene is
used to direct protein synthesis and produce the structures of the cell. Genes that code for amino acid
sequences are known as 'structural genes'.
Gene regulation is a label for the cellular processes that control the rate and manner of gene
expression. A complex set of interactions between genes, RNA molecules, proteins (including
transcription factors) and other components of the expression system determine when and where
specific genes are activated and the amount of protein or RNA product produced.

Some genes are expressed continuously, as they produce proteins involved in basic metabolic functions; some

genes are expressed as part of the process of cell differentiation; and some genes are expressed as a result of

cell differentiation.

Mechanisms of gene regulation include:

Regulating the rate of transcription. This is the most economical method of regulation.

Regulating the processing of RNA molecules, including alternative splicing to produce more than one protein
product from a single gene.

Regulating the stability of mRNA molecules.

 Regulating the rate of translation.

Transcription factors are proteins that play a role in regulating the transcription of genes by binding to specific

regulatory nucleotide sequences.

18. If we consider the central dogma of molecular biology, we can see that there are two

main steps at which protein production can be regulated - at the levels of transcription
and translation. This topic will look at means of regulating protein production at each of
these levels.
 Figure Error! No text of specified style in document.:2 Central Dogma of Molecular Biology
(Figure 11-3, Snustad et al, 1997. Principles of Genetics)

Control of Transcription Initiation

It seems fairly clear that one of the most obvious places to control protein production would be
at the level of transcription initiation. The processes of transcription and translation were
detailed in Module 1 and should be revised before reading this section.

Remember: Transcription initiation involves (1) the binding of RNA polymerase to the promoter
elements of the gene, (2) the localised unwinding of the double-stranded DNA template and (3)
the addition of the first few ribonucleotides to the nascent RNA chain.

A central theme driving the survival of bacteria is the efficiency and economy of bacterial growth
(see experiment 1 above). The regulation of gene expression at the level of transcription
initiation is very much in keeping with this theme as it not only spares the cell the burden of
translating the protein but also save making the messenger.

Control regions can be adjacent or overlap these elements and it is proteins (or regulators) that
bind to these regions that control transcription initiation. A regulator that binds to a control
region and increases the rate of transcription is called an activator (or positive regulator)
whereas one that decreases transcription is called a repressor (or negative regulator).
Activators may work by relaxing the region of the DNA double helix in the region of the promoter
elements allowing greater access for the RNA polymerase. Conversely, the binding of
repressors may result in a blocking of the promoter elements that interferes with the actions of
the polymerase.
Examples of repression and induction are seen in the operon model (the structure of a operon
is shown below) and will be discussed later in this module (see lac operon).
 Figure Error! No text of specified style in document.:3 Structural features of an operon
(Figure 21-3(a), Snustad et al, 1997. Principles of Genetics)

A common pattern in the control of transcription initiation is on that parallels feedback inhibition
of enzyme activity. That is, the regulation of genes that encode repressors is often brought
about by the repressor proteins they produce. This is called autogenous regulation and
probably exists to prevent overproduction of repressor proteins.

Control of Transcription Termination

Generally, once transcription has been initiated it will continue until (a) a DNA sequence is
transcribed that, in the mRNA, forms a stable hairpin loop structure (called a terminator) or (b)
the paused RNA polymerase is exposed to a Rho factor (generally).

Although transcription termination must occur at the end of a gene (or operon), it can
occur early in transcription and this, when controlled, can play a regulatory role. The
events involved in regulatory termination mechanisms begin with a pausing of the RNA
polymerase. The stem-and-loop structure forms in the newly synthesized mRNA which
either directly interferes with the actions of the RNA polymerase or disrupts the RNA-DNA
hybrid in the transcription bubble. Whatever the case, it is most likely that the polymerase
will be ejected from the transcription bubble, effectively terminating transcription.

Mechanisms also exist that can override termination signals when conditions become
appropriate for the expression of these genes. This regulated transcription termination is called
attenuation.

Control of Translation
In some cases, the expression of bacterial genes is controlled after the mRNA has been made
by posttranscriptional regulation. This generally occurs by preventing the initiation of
translation and, as a result, stops the synthesis of the protein.

19. A. In genetics, an operon is a functioning unit of genomic DNA containing a cluster of

genes under the control of a single promoter.

B. In genetics, a promoter is a region of DNA that initiates transcription of a particular
gene.Promoters are located near the transcription start sites of genes, on the same
strand and upstream on the DNA (towards the 5' region of the sense strand).
C. A regulator gene, regulator, or regulatory gene is a gene involved in controlling the
expression of one or more other genes. A regulator gene may encode a protein, or it
 may work at the level of RNA, as in the case of genes encoding microRNAs. In
prokaryotes, regulator genesoften code for repressor proteins.
D. In molecular biology, an inducer is a molecule that regulates gene expression.
An inducer can bind to repressors or activators. Inducersfunction by disabling
repressors. The gene is expressed because aninducer binds to the repressor.
E. In molecular genetics, a repressor is a DNA- or RNA-binding protein that inhibits the
expression of one or more genes by binding to the operator or associated silencers. A
DNA-binding repressor blocks the attachment of RNA polymerase to the promoter, thus
preventing transcription of the genes into messenger RNA.
F. Terminators are genetic parts that usually occur at the end of a gene or operon and
cause transcription to stop.
G. In genetics, an operator is a segment of DNA to which a transcription factor binds to
regulate gene expression. The transcription factor is a repressor, which can bind to
the operator to prevent transcription.
20. A common pattern in the control of transcription initiation is on that parallels feedback
inhibition of enzyme activity. That is, the regulation of genes that encode repressors is often
brought about by the repressor proteins they produce. This is called autogenous regulation
and probably exists to prevent overproduction of repressor proteins.

21. Several mechanisms of regulating transcription termination have been discovered in bacteria
and eukaryotes. RNA polymerase itself plays a role in the two principal mechanisms of transcription
termination that occur in E. coli. An additional protein, a transcription-termination factor called Rho, is
required in one mechanism but not the other. These mechanisms are commonly referred to as Rho-
independent and Rho-dependent termination. In eukaryotes, the mechanisms for terminating
transcription appear to differ for each of the three RNA polymerases. In this section, we first focus on
termination mechanisms in bacteria, which are better understood than eukaryotic mechanisms, and
then describe two well-studied examples of transcription termination in eukaryotes.

22. Control of Translation

In some cases, the expression of bacterial genes is controlled after the mRNA has been made
by posttranscriptional regulation. This generally occurs by preventing the initiation of
translation and, as a result, stops the synthesis of the protein.

23. This mechanism of regulation comes about through allosteric interactions. If we consider
experiment 2 above, histidine supplied to the medium resulted in the bacteria shutting down the
pathway responsible for histidine synthesis. This would have been observed for virtually any
basic building block and would have occurred at any point during the growth cycle once the
media was supplemented with the appropriate metabolite. In this experiment, the immediate
response that was observed is merely an exaggeration of a process that is occurring
continuously within the cell, not only monitoring histidine synthesis, but all other metabolites as
well.

The regulatory mechanism at work in this system involves the disruption of enzyme activity
through allosteric inhibition (or the loss of enzyme activity as a result in the change of the
enzymes conformational shape). This type of inhibition arises when a specific ligand (or
allosteric effector) binds to a specific site on an allosteric enzyme and alters the
conformational state of the enzyme. In the case of histidine synthesis, histidine (the allosteric
effector) acts on the first enzyme in the histidine biosynthesis pathway, effectively shutting it
down.
24. Biosynthesis of the Aspartate family of Amino Acids
L-lysine, L-threonine, L-methionine and L-isoleucine are the four amino acids in the aspartate
family of amino acids as they are all synthesized from L-aspartic acid. It is interested to note
that humans, like many other eukaryotes, are unable to synthesize lysine and must obtain this
essential amino acid from the diet.

E. coli synthesizes L-lysine through the diaminopimeilc pathway. The production of the other
three amino acids branches from this pathway following the second enzymatic modification and
utilises the L-aspartate semialdehyde produced from this step.

Figure Error! No text of specified style in document.:4 Diaminopimelic Pathway in E. coli

The above diagram shows the steps from L-aspartate to each of the amino acids produced
through this pathway in E. coli. The dashed lines show feedback inhibition mechanisms (i.e.
where the product acts on the enzyme) whilst the solid lines show repression (or the effect on
gene expression by a particular product). The figures E1 to E9 represent the enzymes that
catalyze the reactions. The only ones we will consider in this discussion are E1: aspartakinase
and E7: homoserine dehydrogenase. The three arrows in the conversion of L-aspartate to L-
aspartyl phosphate indicate that there are three aspartakinase isoenzymes (two of these also
happen to possess homoserine dehydrogenase activity). Also note that the conversion of
piperideine-2,6-dicarboylate to meso-2,6-diaminopimelate is a multistep process. From the
above diagram, it can be seen that the regulation of aspartate family amino acid synthesis is a
fairly complex process with lysine involved in feedback inhibition on two reactions and
repression of six. Threonine, not only regulates its own synthesis via feedback inhibition at E8,
but also the synthesis of isoleucine and methionine by controlling the branch point away from
the diaminopimelic pathway and all amino acids at the aspartakinase reaction.
Now consider the biosynthesis of the same amino acids in Corynebacterium glutamicum, a
Gram-positive bacteria used in the commercial production of lysine.

Figure Error! No text of specified style in document.:5 Synthesis of Aspartic acid family amino acids in
Corynebacterium

As before, E7 is homoserine dehydrogenase and E1 is aspartakinase. In terms of the pathway

itself, there are two significant differences. Firstly, the of piperideine-2,6-dicarboylate to meso-
2,6-diaminopimelate occurs in a single step in the corynebacteria as compared to the four steps
in the E. coli pathway. Secondly, and most significant for this discussion, is that there is only a
single aspartakinase isoform.

Only three steps in this entire pathway are regulated, however the positions where they occur
result in simple, but effective regulation, of all the end products. For the purposes of this
comparison we will only consider the production of lysine versus the production of the other
three. Threonine (through feedback inhibition), methionine (via repression) and, to a lesser
extent, isoleucine regulate the flow of L-aspartate semialdehyde between the two major
branches of the pathway. Under conditions where threonine, isoleucine and methionine are
produced in excess, they act on the homoserine dehydrogenase (or the gene that encodes it in
the case of methionine) to inhibit the conversion of aspartate semialdehyde to L-homoserine.
Under these conditions, the aspartate semialdehyde will continue along the lysine-producing
branch, resulting in the accumulation of lysine.

Which brings us to a major regulatory mechanism occurring in this pathway. The accumulation
of lysine, together with threonine, results in the feedback inhibition of aspartakinase, effectively
ending the production of all the aspartate family of amino acids.
At some stage, the levels of lysine or threonine may drop and again require the production of
these amino acids. Under the conditions of low threonine, the concerted actions of threonine
and lysine required for the feedback inhibition of aspartakinase would no longer be met and the
enzyme would start converting L-aspartate to L-aspartyl phosphate. When the branch point
between the two pathways is reached, the levels of homoserine dehydrogenase would exceed
those of E3 (dihydrodipicolinate synthetase) resulting in the conversion of aspartate
semialdehyde to homoserine and, ultimately, the production of threonine whilst having little
effect on the levels of lysine.

In the case of depleted lysine, the order of events starts the same. The low lysine results in a
disruption to the feedback inhibition mechanism working on the aspartakinase. When the
branch point is reached, the high levels of threonine keep inhibiting the activity of homoserine
dehydrogenase and the majority of aspartate semialdehyde is utilised by the lysine-producing
branch.

For depletion of both lysine and threonine, there will be no feedback inhibition acting on
the aspartakinase, so the pathway will progress. At the branch point, active homoserine
dehydrogenase will result in the production of threonine, methionine and isoleucine.
Comparable levels of dihydrodipicolinate synthetase will also process some of the
aspartate semialdehyde into the lysine-producing branch ultimately producing lysine.

These organisms are used in the industrial production of lysine as mutations in the homoserine
dehydrogenase or aspartakinase feedback mechanism result in strains that overproduce lysine.
24.

TRUE. Note that the conversion of piperideine-2,6-dicarboylate to meso-2,6-diaminopimelate is

a multistep process. From the above diagram, it can be seen that the regulation of aspartate
family amino acid synthesis is a fairly complex process with lysine involved in feedback
inhibition on two reactions and repression of six. Threonine, not only regulates its own
synthesis via feedback inhibition at E8, but also the synthesis of isoleucine and methionine by
controlling the branch point away from the diaminopimelic pathway and all amino acids at the
aspartakinase reaction.
27. The accumulation of lysine, together with threonine, results in the feedback inhibition of
aspartakinase, effectively ending the production of all the aspartate family of amino acids.

At some stage, the levels of lysine or threonine may drop and again require the production of
these amino acids. Under the conditions of low threonine, the concerted actions of threonine
and lysine required for the feedback inhibition of aspartakinase would no longer be met and the
enzyme would start converting L-aspartate to L-aspartyl phosphate. When the branch point
between the two pathways is reached, the levels of homoserine dehydrogenase would exceed
those of E3 (dihydrodipicolinate synthetase) resulting in the conversion of aspartate
semialdehyde to homoserine and, ultimately, the production of threonine whilst having little
effect on the levels of lysine.
28. L-lysine, L-threonine, L-methionine and L-isoleucine are the four amino acids in the aspartate
family of amino acids as they are all synthesized from L-aspartic acid. It is interested to note
that humans, like many other eukaryotes, are unable to synthesize lysine and must obtain this
essential amino acid from the diet.
29.
a. The accumulation of lysine, together with threonine, results in the feedback inhibition of
aspartakinase, effectively ending the production of all the aspartate family of amino acids.
b. In the case of depleted lysine, the order of events starts the same. The low lysine results in a
disruption to the feedback inhibition mechanism working on the aspartakinase.
c. the concerted actions of threonine and lysine required for the feedback inhibition of
aspartakinase would no longer be met and the enzyme would start converting L-aspartate to L-
aspartyl phosphate.
d. For depletion of both lysine and threonine, there will be no feedback inhibition acting on the
aspartakinase, so the pathway will progress.

30. The lac operon contains several genetic elements. The lacZ (-galactosidase), lacY
(permease) and lacA (transacetylase) genes represent the structural genes of the operon. The
permease is responsible for lactose uptake into the cell whilst the -galactosidase converts
lactose into glucose and galactose. These genes are all expressed from the promoter (P) and
are under the control of the operator (O). Upstream of the promoter for lacZYA, is the lacI
gene, which encodes the lac repressor. The lacI gene has its own promoter, PI.
31. The lac operon is an inducible operon (i.e. the lacZYA genes are only expressed in the
presence of lactose [see induction] and in the absence of glucose.
32. Induction of the lac operon
The structural genes of the lac operon are only expressed in the presence of lactose. The
regulatory gene, lacI, encodes a repressor protein. In the absence of the inducer (in this case
allolactose), the repressor protein binds to the lac operator which, in turn, prevents transcription
by blocking the binding of RNA polymerase to the promoter. There is a small level of
transcription in the uninduced state and this provides a low level background activity of all the
enzymes encoded by the structural genes.

When lactose becomes available, the background level of -galactosidase activity converts
some of the lactose into allolactose (which is the inducer). The inducer binds to the repressor
and this complex is unable to interact with the operator. With the operator cleared of any
repressor molecules, the RNA polymerase is free to bind and transcription of lacZYA can occur.
33.

34. FALSE. The tryptophan operon encodes the genes involved in tryptophan biosynthesis.
Unlike the lac operon (which is an inducible operon), the trp operon is probably the best known
repressible operon. Again in contrast to the lac operon, the gene for the repressor (trpR) is not
located near the structural genes (trpLEDCBA).

35. The repression of the trp operon works as follows. In the absence of tryptophan (the co-
repressor) the RNA polymerase binds to the promoter (P1) and transcribes the structural genes
within the operon. When tryptophan becomes available, the complex formed between it and the
repressor protein (from trpR) bind to the operator (O) and prevent transcription.
36. TRUE. Because it occurs during termination. But there is another regulatory mechanism at
work within this operon attenuation. This mechanism acts at the level of transcription
termination. The main molecule involved in the attenuation of the trp operon is the charged
tRNATrp and works on the attenuator region in the trpL gene.
37. The attenuation mechanism relies of the coupling of transcription and translation and works
as follows. Immediately upstream of region 1 are two tryptophan (UGG) codons and
immediately downstream of region 1 is a stop codon (UGA). In the presence of tryptophan, the
levels of charged tRNATrp are high and the ribosome progresses past the two trp codons at its
usual rate until it reaches the stop codon where it is terminated. This effectively ties up region 1
and 2 so they cannot take part in base pairing. With region 2 unavailable for base pairing,
region 3 pairs with region 4 to form the transcription terminator and transcription stops
preventing expression of the trp operon genes.
38. FALSE. The only combination that forms a transcription terminator is regions 3 and 4.