TRANSLATION

DNA TO RNA TO PROTEINS

The genes on the DNA code
for a particular protein

This code must be copied

and sent by a message to
the structures involved in
protein synthesis

This message is sent via

RNA specifically mRNA

The message is then

interpreted/translated and a
protein is thus made
 TRNA
a type of RNA found in the cytoplasm.
Made of a single-stranded of RNA looped back on
itself.

tRNA is only about 80 nucleotides long, and it folds

up by complementary base pairing to form a
clover-leaf structure.
 TRNA
Each tRNA molecule has a particular anticodon
that pair with a codon on mRNA and determines
the type of amino acid with which the tRNA will
bind.

There are 64 different tRNA molecules, each with a

different anticodon sequence complementary to
the 64 different codons on mRNA.
 EACH TRNA HAS THE FOLLOWING:

At one end of the molecule there is an amino acid

binding site- always with a CCA base sequence.
Two loops of nucleotides formed by some base
pairing.
On the middle loop there is a triplet nucleotide
sequence called theanticodon three bases that
identify with the amino acid.
 mRNA TRNA

essentially linear folds into a clover-leaf shape

number of nucleotides varies /
length of a gene about 80 nucleotides long

carries the code for proteins consists of a single anticodon

in form of codons, in form of 3
adjacent nucleotides coding for
an amino acid
attaches to an amino acid and
carries it to ribosome
no place of attachment for
amino acid
 RIBOSOME
Used in translation in protein synthesis

Composed of large and small subunits

Which comprises of RNA and protein

Function is to hold in position mRNA, tRNA and

enzymes controlling the process
 RIBOSOME
The small subunit provides a structural site for
mRNA and allows movement of the components in
translation.

The large subunit helps to hold the mRNA and

tRNA during translation.

When the peptide linkage is formed between the

amino acids, the mRNA moves down one codon
EACH RIBOSOME HAS 3 SITES:
Amino acyl Site ( A site) - Accepts the
tRNA-amino acid complex.

Peptidyl Site ( P site) - Holds the

lengthening polypeptide

Exit Site ( E site) - Releases the used

tRNA- amino acid complex
EACH RIBOSOME HAS 3 SITES:
A Site - Accepts
the tRNA-amino acid
complex.
P Site - Holds the
lengthening
polypeptide

E Site -
Releases the used
tRNA- amino acid
THE GENETIC CODE
 THE GENETIC CODE

START signal : only one Codon. AUG which codes for

the amino acid Methionine.

STOP signals : Three codons.

ATT
ATC
ACT
 TRANSLATION

Translation is the synthesis of proteins on the

ribosome.
Translation is the process by which the code for

making the protein- now carried by the mRNA

molecule- is used to line up amino acids in a particular
sequence and link them together to make a
polypeptide.
TRANSLATION
amino acid
tRNA

single stranded mRNA

}

Codon (3 bases)
IMPORTANT PLAYERS
tRNA = transfer RNA
Anticodon on one end and aa on other
Ribosome = enzyme that gathers the correct
tRNA and makes the peptide bond between
two amino acids
Initiator tRNA = aa Met; begins translation
Peptide = the newly formed sequence of aas.
Stop codons = stop translation.
Release factor- releases the mRNA molecule
from the ribosomal complex
 TRANSLATION

Note: Actually a different tRNA for each different codon

AMINO ACID ACTIVATION
NB. THIS OCCURS BEFORE TRANSLATION BEGINS.
AMINO ACID ACTIVATION
In-order for amino acids to assembled together, they have
to be labelled or identified using the same three base
codes.

Since amino acids do not have bases, they are attached to

molecules of RNA that do.

Therefore, each amino acid is attached to a specific tRNA

molecule which has an anticodon which corresponds to the
specific amino acid that it carries.
AMINO ACID ACTIVATION
Enzymes called tRNA transferase in the cytoplasm have
active sites that accepts specific amino acids and tRNA
molecules.
The tRNA transferase recognize the specific tRNA for
each type of amino acid.
The amino acid attached to the specific tRNA molecule
using energy.
For eg. A tRNA with anticodon UAC will have
methionine laded onto its amino acid binding site.
 TRANSLATION

Process is made up of initiation,

elongation and termination
STEP 1 INITIATION
TRANSLATION INITIATION
 INITIATION
The small ribosomal subunit attaches to the mRNA
molecule where the start codon (AUG) is located.
N.B Six bases / two codons will be enclosed by the
ribosome each time.
A tRNA with the specific anticodon (UAC) that is
complementary to the start codon (AUG) binds with the
mRNA at the A site .
 INITIATION

The larger ribosomal subunit now binds to the smaller unit,

forming a ribosomal complex. The tRNA binds to the first active
site (P site) on the ribosome. Translation may now begin

N.B Only the first tRNA enters at the P site. Every other tRNA
will enter the ribosome at the A site
 INITIATION

When the tRNA carrying Meth enters the A site, the mRNA
moves so that the whole complex carrying the Methionine
moves to occupy the P site thus emptying and exposing
an empty A site.
TRANSLATION
STEP 2 ELONGATION
 ELONGATION

The next tRNA with the specific amino acid dictated by the
codon arrives in the A site of the large subunit.
It binds with the complementary codon on the mRNA.
A peptide bond is formed between the two amino acids
in the ribosomes resulting in elongation of the strand.
The enzyme Peptidyl Transferase catalyses the
formation of the peptide bond between the two amino
acids
 ELONGATION

For example, the second codon on the mRNA strand is

UCG. The tRNA bearing the anticodon AGC and the amino
acid Serine moves in an occupy the now free A site.
The enzyme peptidyl-transferase will catalyse the
formation of a peptide bond between Methionine and
Serine to join the two amino acids together.
 ELONGATION

The mRNA now moves down to the third codon.

The first tRNA which carried Meth moves to occupy the E
site of the large ribosomal subunit and then exits the
ribosome.
The second tRNA which carries the dipeptide (meth-ser )
will now occupy the P site.
 ELONGATION

The next tRNA with the corresponding anticodon to the

mRNA codon will now arrive in the now empty A site and
another peptide bond will form with this new amino acid
and the Meth- Ser.
The elongation process is continuous and will continue
until a STOP codon is reached on the mRNA strand.
PEPTIDE BONDS

Peptide bonds form between two amino acids:

 ELONGATION

The mRNA moves down one codon and another specific

amino acid is added based on the codon on the mRNA.
This continues until a stop signal is encountered
TRANSLATION ELONGATION
STEP 3 TERMINATION
 TERMINATION

When a STOP codon is reached, the termination factors

removes the mRNA and the completed polypeptide is
released and the ribosomal subunits separates. This is
called Termination.
NB. There is no tRNA with an anticodon for a stop codon,
so translation stops.
TERMINATION
 TERMINATION
The process continues
until the ribosome finds a
stop codon. The
subunits detach from one
another, the mRNA is
released, and the
polypeptide chain moves
down the ER for further
processing. The initial
met is removed and the
chain is folded into its
final shape.
TRANSLATION TERMINATION

Simple as reading a stop codon

UAA, UAG or UGA

Ribosome releases
peptide
Transcription TRANSLATION

synthesis of proteins from mRNA.

synthesis of mRNA from DNA

occurs in cytoplasm /ribosomes.

occurs in the nucleus

linking of amino acids.

linking of nucleotides

peptide bonds formed

phosphodiester bonds formed
involves the joining of codons and
Involves producing codons anticodons

catalysed by RNA polymerase catalysed by various enzymes in

ribosomes
CHROMOSOMES

Chromosomes highly coiled

condensed packages of DNA
 POST-TRANSLATION
The new polypeptide is now floating loose in the
cytoplasm if translated by a free ribosome.
It might also be inserted into a membrane, if translated by
a ribosome bound to the endoplasmic reticulum.
Polypeptides fold spontaneously into their active
configuration, and they spontaneously join with other
polypeptides to form the final proteins.
Protein modification occurs in the endoplasmic reticulum
and Golgi Apparatus
Sometimes other molecules are also attached to the
polypeptides: sugars, lipids, phosphates, etc. All of these
have special purposes for protein function.
POST-TRANSLATIONAL MODIFICATION

In Eukaryotes, proteins often need to be altered

before they become fully functional.
Modifications are carried out by other enzymes and
include: chain cutting, adding sugars (to make
glycoproteins) or lipids (to make lipoproteins).
These changes occur in the Golgi Apparatus
 PROTEIN MODIFICATION

Addition of hydrophobic groups for membrane

localization
Addition of cofactors for enhanced enzymatic
activity
Unique modifications of translation factors
Addition of smaller chemical groups
Addition of other proteins or peptides
Changing the chemical nature of amino acids
 Methylation- addition of a methyl group
Glycosyliation- addition of a gycosyl group

See post-translational modification on wikipedia

CHROMATIN

DNA is associated with histone proteins to form a

complex calledchromatin.
The histones helps to hold the DNA in coils and
they help to determine which genes will be
expressed at particular times in particular cells.
 NUCLEOSOME

http://scienceblogs.com/transcript/2006/08/08/nucleosome-binding-sites-1 /
CHROMATIN

During most of the life of a cell the chromatin is

dispersed throughout the nucleus and cannot be
seen with a light microscope.
CHROMATIN

Heterochromatin- more dense form of chromatin

which is mostly coiled up to produce a dark area and
is not used for transcription. More visible

Euchromatin- less dense form of chromatin which is

less coiled to produce a light area and is used for
transcription. Less visible
CHROMATIN

Just before cell division the DNA is replicated so

there is temporarily twice the normal amount DNA.
Following replication the chromatin then coils up
even tighter to form short fat bundles called
chromosomes.
Chromosome are about 100000 times shorter
than fully stretched DNA and are thick enough to
be seen under the microscope.
 CHROMOSOME

Each chromosome is roughly X-shaped because it

contains two replicated copies of the DNA called
sister chromatids.
The two arms of the X are therefore identical. They
are calledchromatids, and are joined at
thecentromere.
CHROMOSOME
 CHROMATIN VS CHROMOSOMES
Chromatin: is a mass of uncoiled DNA and associated
proteins called histones.
Chromatin appears to be loosely coiled, long thin threads
spread throughout the nucleus.

Chromosomes: when cell division begins, DNA coils around

the proteins
forming visible structures called chromosomes.

A pair of chromatids joined by a centromere form the

chromosome. It therefore consists of a pair of sister
POST-TRANSLATIONAL MODIFICATION

The phenotype of an organism is all its features,

both internal and external that are direct result of
gene action and the interaction between the genes
and the environment.