Genetic code

&
Translation
 Gene 1 Gene 3

DNA molecule

Gene 2

DNA strand

TRANSCRIPTION

RNA

Codon
TRANSLATION

Polypeptide
Amino acid
 The Genetic Code
The genetic code is the set of rules by which
information encoded in genetic material
(DNA or mRNA sequences) is translated
into proteins (amino acid sequences) by
living cells.
It is a set of 3 nucleotides on the mRNA known as
CODON.

(Since there are 4 bases, there are 43 = 64 possible

codons, which must code for 20 different amino acids.)
 The Genetic Code
 is almost universal, used in both prokaryotes and eukaryotes.

 AUG is used as the start codon. All proteins are initially

translated with methionine in the first position, although it is
often removed after translation. There are also internal
methionine in most proteins, coded by the same AUG codon.

 There are 3 stop codons, also called “nonsense” codons.

Proteins end in a stop codon, which codes for no amino acid.

Genetic code is degenerate, many amino acids

specified by more than one codon.

Only tryptophan and methionine are encoded by a

single codon.
• An exercise in translating the genetic code
Transcribed strand

DNA

Transcription

RNA

Start Stop
codon Translation codon

Polypeptide
nslation/Protein Synthe
Stage 1: Activation of Amino Acids
 Activation of carboxyl group of each amino acid to facilitate
formation of a peptide bond.
 Link formation between each new amino acid and the
information in the mRNA that encodes it.
Stage 2: Initiation
Formation of initiation complex,
Initiation codon in mRNA (AUG), 30S & 50S ribosomal subunit,
Initiation factors (IF-1, IF-2, IF-3)
Stage 3: Elongation

Stage 4: Termination
Transfer RNA molecules serve as
interpreters during translation
• In the cytoplasm, a ribosome Amino acid attachment site
attaches to the mRNA and
translates its message into a
polypeptide
• The process is aided by
transfer RNAs
• one specific type of tRNA is Hydrogen bond
required for each amino acid
• Atleast 32 tRNA are required
for 20 amino acids. some RNA polynucleotide chain
amino acids have more than
one specific tRNA molecule

Anticodon
Figure 10.11A
Amino acid attachment site: Each tRNA molecule has an
attachment site for a specific amino acid at its 3'-end. The carboxyl
group of the amino acid is in an ester linkage with the 3'-hydroxyl
of the ribose portion of the adenosine (A) nucleotide in the —CCA
sequence at the 3'-end of the tRNA. When a tRNA has a covalently
attached amino acid, it is said to be charged; when it does not, it is
said to be uncharged. The amino acid attached to the tRNA
molecule is said to be activated.

Anticodon: Each tRNA molecule also contains a three-base

nucleotide sequence—the anticodon—that pairs with a specific
codon on the mRNA. This codon specifies the insertion into the
growing peptide chain of the amino acid carried by that tRNA.
• Each tRNA molecule has a triplet anticodon on one end
and an amino acid attachment site on the other

Amino acid
attachment
site

Anticodon
Figure 10.11B, C
 Prokaryotic Eukaryotic
Ribosomal Machine
1. The ribosome binds mRNA such that its codons can be
read with high fidelity.
2. The ribosome includes specific binding sites for tRNA
molecules.
3. The ribosome mediates the interactions of non ribosomal
protein factors that promote polypeptide chain initiation,
elongation, and termination.
4. The ribosome catalyzes peptide bond formation.
5. The ribosome undergoes movement so that it can translate
sequential codons.
6. The small ribosomal subunit binds mRNA and is
responsible for the accuracy of translation by ensuring
correct base-pairing between the codon in the mRNA and
the anticodon of the tRNA.
7. The large ribosomal subunit catalyzes formation of the
peptide bonds that link amino acid residues in a protein.
A, P, and E sites on the ribosome:
 The ribosome has three binding sites for tRNA molecules-the A, P,
and E sites-each of which extends over both subunits.
 During translation, the A site binds an incoming aminoacyl-tRNA as
directed by the codon currently occupying this site.
 This codon specifies the next amino acid to be added to the growing
peptide chain.
 The P-site codon is occupied by peptidyl-tRNA.
 The E site is occupied by the empty tRNA as it is about to exit the
ribosome.
 Ribosome build polypeptides

Next amino acid

Growing to be added to
polypeptide polypeptide
tRNA P site A site
molecules
Growing
Large polypeptide
subunit
tRNA

P A
mRNA
mRNA
binding
site
Codons

mRNA Small
subunit

Figure 10.12A-C
 Stage 1: Activation of Amino Acids

Aminoacyl-tRNA synthetases esterify the 20 amino acids to

their corresponding tRNAs. Each enzyme is specific for one amino
acid and one or more corresponding tRNAs.

(1) Activation: it activates an amino acid for peptide bond formation

(2) Proof reading: it ensures appropriate placement of the amino

acid in a growing polypeptide.

Amino acid  tRNA  ATP  aminoacyl-tRNA  AMP  Ppi

Aminoacyl-tRNA synthetases catalyze a
two-step reaction that results in the covalent
attachment of the carboxyl group of an amino
acid to the 3'-end of its corresponding
(cognate) tRNA. The overall reaction requires
adenosine triphosphate (ATP), which is
cleaved to adenosine monophosphate (AMP)
and inorganic pyrophosphate (PPi)
 Stage 2: Initiation
Starts after assembly of all
translational factors. Two ribosomal
subunits, the mRNA to be
translated, the aminoacyl-tRNA
specified by the first codon in the
message, GTP and initiation factors
that facilitate the assembly of this
initiation complex. In prokaryotes,
three initiation factors are known
(IF-1, IF-2, and IF-3), whereas in
eukaryotes, there are over ten
(designated eIF to indicate
eukaryotic origin)
An initiation codon marks the start of a
mRNA message

AUG = methionine
Start of genetic message

End
• mRNA, a specific tRNA, and the ribosome subunits
assemble during initiation

Large
Initiator tRNA ribosomal
subunit
P site
A site

Start
codon Small ribosomal
mRNA subunit

1 2

Figure 10.13B
 Elongation

• The mRNA moves a codon at a time relative to the

ribosome
• A tRNA pairs with each codon, adding an amino acid to the
growing polypeptide
• 3 STEPS; binding of aminoacyl tRNA, peptide bond formation,
and Translocation
• A STOP codon causes the mRNA-ribosome complex to fall
apart
 Amino acid

Polypeptide
A
P site site
Anticodon

mRNA
1 Codon recognition

mRNA
movement

Stop
codon

New 2 Peptide bond

peptide
formation
bond

3
Translocation

translocation, the ribosome moves one codon toward the

Figure 3' end of the
10.14

mRNA
a b

What molecules are present

Red object = ? in this photo?
TERMINATION
 Translation
Nucleus

Lysine mRNA
Phenylalanine
tRNA
Methionine

Ribosome

mRNA Start codon

 Translation (continued)

Growing polypeptide
chain

Ribosome
tRNA

Anticodon Amino Acid

on tRNA tRNA

mRNA

mRNA Codon on
mRNA
Translation direction
• Summary of transcription and translation
DNA TRANSCRIPTION

Stage 1 mRNA is
mRNA
transcribed from a
RNA
polymerase DNA template.

Amino acid
TRANSLATION
Stage 2 Each amino
Enzyme acid attaches to its
proper tRNA with the
help of a specific
enzyme and ATP.
tRNA

Initiator Anticodon
tRNA Stage 3 Initiation of
Large polypeptide synthesis
ribosomal
subunit The mRNA, the first
tRNA, and the
ribosomal subunits
Start Small
Codon ribosomal come together.
mRNA
subunit
 New
peptide
Growing bond Stage 4 Elongation
polypeptide forming
A succession of tRNAs
add their amino acids to
the polypeptide chain as
the mRNA is moved
through the ribosome,
one codon at a time.
Codons
mRNA
Polypeptide

Stage 5 Termination
The ribosome recognizes
a stop codon. The poly-
peptide is terminated and
Stop Codon released.
Post-Translational Modifications
1. Trimming
• Many proteins are made in the form of large precursor molecules
which are not functionally active (called Zymogens/Proenzymes).
• They become activated through cleavage when they reach their
proper sites of action, by the action of other enzymes / non-enzymes
factors.
• E.g: Conversion of inactive Pepsinogen into active pepsin, by the
action of HCl.
2. Covalent Modification
(i) Phosphorylation
• Addition of phosphate group to amino acid residues of proteins (Ser, Thr,
Tyr).
• Catalyzed by family of enzymes Protein Kinases.
(ii) Glycosylation
• Addition of carbohydrate chain to protein.
• Occurs only in those proteins which have to become the part of cell
membrane.

(iii) Hydroxylation
• Collagen is hydroxylated in ER.

(iv) Others
• Carboxylation.
• Biotinylation
• Farnisylation(attachment of lipid groups).
Link of Videos
• https://www.youtube.com/watch?v=5bLEDd-PSTQ
• https://www.youtube.com/watch?v=gG7uCskUOrA