P

PROTEIN SYNTHESIS
S
S AND MUT
TATIONS
S
STRUCTUR
RED QUEST
TIONS
Q
Question 1 AQA/JUN07/MAK
A
KEUB/Q1
The table sho
ows some mRNA
m
base sequences and the am
mino acid seq
quences tha
at would be produced
frrom them

(a
a)

Comp
plete the tab
ble above to show the sequence of amino acids produced from the fin
nal mRNA
base sequence.
s
[1
1] Thr-His-Thr-His-Thr

(b
b)

Use th
he informatio
on in the tab
ble to give
(i) one
e sequence of DNA bases that code
es for the am
mino acid ser, [1] TCA
(ii) on
ne anticodon for the amin
no acid ser. [1] UCA

(cc)

The genetic code is described

d as non-ove
erlapping an
nd degenerate.
Explain the eviden
nce from the
e table that this code is
(i)

non-overlap
n
ping [2]
no base of a given codon
c
contrib
butes to partt of the code
e of the nextt codon / aftter one
codon ha
as been read, the immediate 3 base
es will be rea
ad as the ne
ext codon / A base
from one
e codon cannot be used for adjacen t codon

(ii)

For a specific
s
poly
ypeptide co
ontaining 1 type of a
a.a, overlapping will produce a
polypepttide made up
u of more than
t
1 a.a e.g. CAA C
CAA CAA prroduces gln--gln-gln, if
genetic code
c
is overrlapping, mR
RNA base s equence willl be CAA A
ACA AAC pro
oducing a
polypepttide with diffe
erent a.a/ an
ny valid exam
mples
degeneratte [2]

One amiino acid can be encoded

d by more th
han one codo
on

ACC and
d ACA both code for thre
eonine (Thr))

An
nderson Junior College Biology Department 2013

Tu
utorial: PROTEIN
N SYNTHESIS AND
A
GENE MUT
TATIONS

Question 2 AQA/JUN03/PD/Q1
Fig. 2.1 shows a stage in protein synthesis.
(a) (i) Name this stage.
Translation
(ii) What is molecule Q?
Proline

[1]
[1]

(b) Give the base sequence on the anticodon of

molecule Z. [1]
CAU

(c)

Describe what will happen next to

(i)

molecule Y; [2]

(ii)

Anticodon GGG binds to CCC codon at the A-site of ribosomes

through complementary base-pairing via hydrogen bonds

molecule Q. [3]

Joins to (carboxyl-end of) growing polypeptide

Via peptide bond formation between P and Q
cataysed by peptidyltransferase

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

Question 3 Modified N06 P2Q06

Fig. 3.1 is an electron micrograph of a secretory cell from the hypothalamus of the brain. The cell
synthesizes and releases ADH (vasopressin).
ADH is a peptide made up of nine amino acids.

Fig. 3.1
(a)

Label the structures A, B and C. [3]

A: cell membrane
B: mitochondrion (reject mitochondria)
C: rough endoplasmic reticulum

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

(b)

Explain the role of the following structures in the synthesis of ADH. [4]
Mitochondria [max 2m]

Involved in aerobic respiration to release energy (reject produce energy) via production
of ATP

ATP used to activate amino acids required for translation/ form polypeptide of ADH

Accept: form peptide bonds between amino acids to form polypeptide of ADH
Accept: ATP are monomers in the synthesis of mRNA of ADH/ tRNA / rRNA required for
the translation of ADH
Nuclear envelope [max 1m]

Regulation/control of movement of ribonucleoside triphosphates/ gene regulatory

proteins, RNA polymerase/ any valid examples required for transcription of ADH into
nucleus via nuclear pores

OR

Regulation/ control of movement of ADH mRNA/ ribosomal subunits / any valid examples
out of nucleus via nuclear pores

Examiners comments: Marks were lost because there was poor reference to nuclear pore
Nucleolus [max 2m]

Site of transcription of rRNA genes to form rRNA.

rRNA then assembles with ribosomal proteins imported from the cytoplasm to form
ribosomal subunits required for translation of ADH mRNA

Examiners comments: Many incorrectly thought that the nucleolus made the mRNA for ADH.
ESSAY QUESTIONS
1. Outline the main events of transcription. [7] J97

gene that codes for enzyme/protein is on one of the DNA strands template strand
RNA polymerase binds to promoter region
Unzips DNA by breaking hydrogen bonds between bases to expose the DNA template strand
for synthesis of mRNA
RNA polymerase adds free ribonucleoside triphosphate (ATP, UTP, CTP and GTP)
Order of bases added is through complementary base pairing (A to U and T to A and C to G) to
via hydrogen bond formation with template strand
ribonucleotides are joined together by phosphodiester bonds
elongates in a 5 to 3 direction with respect to the growing mRNA chain
transcription stops after RNA polymerase reads the termination signal (in prokaryotes) /
polyadenlyation signal (in eukaryotes)

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

ADDITIONAL PRACTICE
Question 1 Nov96
The figure below is a section through the rough endoplasmic reticulum representing the synthesis of
proteins.

A
B

C
(a) Name structures A to C. [3]
A:
mRNA;
B:
Large subunit of ribosome;
C:
polypeptide;
(b) Describe and explain the role in protein synthesis of
(i) structure A
[3]
messenger molecule, carrying genetic code/ information copied from DNA
each codon / triplet of bases on mRNA encodes an amino acid
serves as template: sequence/order of codons on mRNA determines the sequence/order of
amino acids in a polypeptide
(ii)

structure B
[3]
Sites of translation to synthesis proteins
Holds tRNA and mRNA in close proximity for translation to occur
Contains peptidyltransferase which catalyse peptide bond formation between amino acids

Question 2 AQA/JUN06/GG/Q3
(a) (i)

What is the role of RNA polymerase in transcription? [1]

(i)

join/attach RNA nucleotides / ribonucleotides via phosphodiester bonds;

Name the organelle involved in translation. [1]

ribosome

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

b) Figure 1 shows
s
some
e molecules involved in protein
p
synth
hesis.
(b

C
Complete Fig
gure 1 to sho
ow
(i) the ba
ases on the DNA strand from which the mRNA w
was transcrib
bed; CGTTA
ACCAA;
[2]
(ii) the ba
ases forming
g the anticod
dons of the tR
RNA molecu
ules. CGU UAC CAA;
Figure 2 show
ws the effectts of two diffferent mutatiions of the D
DNA on the b
base sequen
nce of the mRNA.
The table sho
ows the mRN
NA codons for
f three amiino acids.

(cc) Name the

e type of muttation repres
sented by mutation 1. [1
1]

Base subs
stitution;

(d
d) Use the in
nformation in
n the table to
o
(i) identiffy amino acid X in Figure
e 1;
alanine;
An
nderson Junior College Biology Department 2013

Tu
utorial: PROTEIN
N SYNTHESIS AND
A
GENE MUT
TATIONS

[1]

(ii) explain how each of mutation 1 and 2 may affect the polypeptide for which this section of DNA is
part of the code.
[4]
mutation 1
no change (to sequence of amino acids)
silent mutation: GCU and GCA both encodes alanine because of the degeneracy of the
genetic code
mutation 2
folding/shape/tertiary structure/position of bonds may change (reject peptide bonds)
Missense mutation: valine replaced by alanine
Question 3 Nov04
Figs. 3.1 and 3.2 are diagrams showing transcription and translation.

(a)

(b)

Identify the structures A to D. [4]

A DNA, B ribonucleoside triphosphates (accept RNA nucleotides), C mRNA, D
polypeptide chain, E RNA polymerase, F ribosome
State where in the cell transcription and translation occur. [2]

nucleus
ribosomes

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

(c)

List three additional ways in which the process of transcription differs from translation.[3]
Refer to page 23 of Protein synthesis lecture notes
Features

Monomers used

Transcription
Ribonucleoside triphosphates
/ RNA nucleotides /
ribonucelotides
Phosphodiester bonds

Translation
Amino acids

Peptide bonds

Bonds between
monomers

Enzyme involved in
forming bonds between
monomers

Template

RNA polymerase

Peptidyltransferase

DNA used as template

mRNA used as template

Reading of template is in the

3 to 5 direction

Reading of template is in the

5 to 3 direction
Amino acids added to carboxyl
end growing polypeptide chain
chain

Direction of elongation

Extend of replication/
transcription

Ribonucleotides added to free

3end growing mRNA chain

Only a certain region (gene) of the

DNA molecule is transcribed in a
single process.

Products

The whole mRNA molecule is

translated in a single process.

RNA

Polypeptide

Highlighted are the more significant points of comparisons

(d)

Briefly describe how the structure of F differs from the structure of E. [2]

Features
Consists of
Has binding sites for
Active site formed by

RNA polymerase (E)

Protein
1 single molecule
DNA
folding of polypeptide chain

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

Ribosome (F)
Protein, rRNA
2 subunits
mRNA, tRNA
Folding of rRNA

C
CHALLENGING QUESTION
Q
Question 1 NJC08
N
Prelims
The diagram below (Fig. 3.1) shows the
t process of transcripttion of DNA to form RNA
A at a particular point
in
n time

Fig. 3.1
(a
a) Describe the events that will occu
ur after the point
p
in time shown in Fig
g. 3.1 until the completio
on of
transcription. [3]
E
ELONGATION
RNA poly
ymerase continues to mo
ove along the DNA addin
ng RNA nuc
cleotides an
nd catalyzing
g the
formation of phospho
odiester bonds betwee
en adjacent R
RNA nucleottides
e of RNA strand / synthesizing RN
NA in a 5-3 direction.
to the 3 end
a compleme
entary base
e pairing witth DNA template
Order of nucleotides added is via
(max 2)
ON
TERMINATIO
RNA poly
ymerase reac
ches a polyadenylation
n signal seq
quence;
ymerase, tran
nscription co
omplex and RNA dissocciate from the
e DNA.
RNA poly
These subseq
quent diagra
ams b and c in Fig. 3.2 and
a Fig. 3.3 show what happens wh
hen an artificcially
syynthesized oligonucleoti
o
ide binds to the DNA. Th
his is a meth
hod to silencce the expresssion of the gene.

(b
b) (i) Fig.3.2 above (Diag
gram b) shows the artific
cially synthe
esized oligon
nucleotide biinding to
the majjor groove of
o the DNA, thus
t
forming
g a triple helix (triplex) in that particular region
where it binds.
Explain
n why, accorrding to Fig. 3.2, the RNA
A polymerasse cannot biind to the DN
NA at all. [2]

Triple helix is no longer comp

plementary/ too
t large to ffit / of a diffe
erent shape as compared to
double
e helix
canno
ot fit to active
e site of RNA
A polymeras
se

An
nderson Junior College Biology Department 2013

Tu
utorial: PROTEIN
N SYNTHESIS AND
A
GENE MUT
TATIONS

Diagram c above shows the scenario whereby the artificially synthesized oligonucleotide binds to the
coding region of the DNA.
(ii) With reference to Fig. 3.2 and Fig. 3.3, account for the difference between the outcomes of
Diagram b and c. [3]
Difference in outcome
In b, transcription does not occur at all/no RNA formed while in c, transcription can occur but is
terminated early / RNA formed to be incomplete or truncated
Reasons
In diagram c, Oligonucleotide does not bind to promoter / control region thus transcription complex
and RNA polymerase can bind to promoter to start transcription
But oligonucleotide disrupts the binding of RNA polymerase as it moves down / oligonucleotide
causes RNA polymerase to dissociate from DNA;
(c) Despite the differences between the outcomes of Diagram b and c, both eventually silence the
expression of the gene. Thus briefly explain what it means to silence the expression of the gene. [1]

To prevent production of the protein

by preventing production of mRNA/ transcription or causing the protein produced to be nonfunctional.

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

10

AN
NDERSON JUNIOR C
COLLEGE
H2 BIO
OLOGY 96
648
JC 1
NSWERS
NAME: AN

CL
LASS:

Evaluation
n: PROTEIN
N SYNTHE
ESIS AND GENE
G
MUT
TATIONS
Q1

Q2

Q3

TOTAL
L MARKS
25

Question 1 J98P3Q3
Before the anticodon
a
off a transfer RNA
R
molecu
ule interact w
with a codon
n on messen
nger RNA, a specific
amino acid must be atttached to th
he 3' end off the transfe
er RNA mole
ecules. Thiss is carried o
out by a
specific enz
zyme, which is able to re
ecognise a trransfer RNA
A molecule that can be linked to the specific
amino acid. Fig. 1.1 below shows a molecule off transfer RN
NA and its co
orresponding enzyme.

Fig
g. 1.1
(a) Explain what is mea
ant by the folllowing terms:
(i) codo
on [1]
sequence
s
off 3 bases/ triiplet of base
es found on m
mRNA whicch encodes for an amino acid
(ii) antic
codon [1]
sequences
s
of
o 3 bases/ triplet of bas
ses found o
on tRNA whiich undergo
oes complem
mentary
base pairin
ng with codon on mRNA

Anderson Junior College

C
Biology Department 2013

Tutorial: PROTE
EIN SYNTHESIS
S AND GENE MU
UTATIONS

11

(b) (i) Explain how the enzyme sho

own in the Fig.
F 1.1 is sp
pecific. [3]
enzyme has
s active site
es which are compleme
entary in sh
hape
to the specific amino acid
a
and its
s correspond
ding anti-co
odon on tRN
NA
Enzyme holds only 1 type of amino acid and on
ne of its specific set of tR
RNA in place
e for the
formation off covalent bo
ond between
n them
A nu
umber of can
ndidates inco
orrectly refe
erred to the a
anticodons o
on the tRNA
A binding the
e codons
on th
he enzyme
e the minimu
um number of these enz
zymes in a ccell [1]
(ii) State
20
me candidate
es confuse this with the
t
64 posssible codon
ns and mad
de reference
e to 64
Som
enzymes
d. [4]
(c) Outline how RNA is synthesized

RNA
A polymeras
se binds to promoter
p
on
n template D
DNA strand
Adds
s free RNA nucleotides
n
s / ribonucle
eoside triph
hosphates
Via complemen
c
ntary base pairing
p
with template
mRN
NA elongates in 5 to 3 direction / RNA
R

[T
Total: 10]
Question 2 Nov 11
Fig. 2.1 sho
ows a prokarryotic ribosom
me during protein synthe
esis.

Fig. 2.1

Anderson Junior College

C
Biology Department 2013

Tutorial: PROTE
EIN SYNTHESIS
S AND GENE MU
UTATIONS

12

(a)

Identify A-D. [4]

A: Large ribosomal subunit (reject ribosome)
B: Polypeptide chain (reject amino acid)
C: tRNA
D: mRNA

(b)

State the role of rRNA in protein synthesis [3]

rRNA together with the proteins, forms small & large ribosomal subunit.
Within the ribosome, rRNA are able to bind mRNA and tRNA to hold them in proximity
for translation to occur
Has enzymatic function- peptidyl transferase, to catalyse peptide bonds formation
between amino acids.
[Total: 7]

Question 2 J94P2Q1
An inherited disease in humans, which results in muscle paralysis, is caused by a dominant mutant
allele of the gene coding for a sodium ion channel protein found in the cell surface membrane of
skeletal muscle. Sequencing of DNA from normal and affected individuals has shown that the
mutation is due to a single base substitution. This results in the amino acid methionine being replaced
by valine in the segment of the protein that forms the channel.
The figure shows the base sequence analysis of the relevant part of the DNA from an affected
individual.

(a) From the sequence in the figure, identify

(i) the base that is missing in the abnormal sequence adenine (reject: adenosine) [1]
(ii) the base that has been put in its place: guanine (reject: guanosine) [1]

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

13

(b) Explain why changing a single base in the gene coding for a protein may have a major effect on
the properties of a protein. [4]

Missense mutation: change / different amino acid encoded

R-group of new amino acid different charge/polarity
Affected amino acid is found in essential region of protein (give 1 example: holds
polypeptide in its shape / forms active site/ binding site )
affects R group interactions change folding of polypeptide change tertiary structure/
3D conformation of protein

Weaker candidates referred to a codon coding for a protein! Some referred to bases being in the
actual protein formed!
(c) Suggest why single base substitution do not always have such a major effect on protein
structure. [2]

redundancy in genetic code / degenerate genetic code/ more than one codon for each amino
acid / 20 amino acids and 64 possible codons
hence a single base do not change the codon no change in amino acid

changed amino acid occurs in in non-essential region of protein

give 1 example: : not involved in holding polypeptide in its shape / does not form active site/
does not form binding site amino acid

change to amino acid with similar R group property

similar polarity/ charge folding of polypeptide is not affected

[Total: 8]

Anderson Junior College Biology Department 2013

Tutorial: PROTEIN SYNTHESIS AND GENE MUTATIONS

14