CHAPTER 12 TRANSLATION

TRANSLATION
Language of nucleic acids is translated into
the language of proteins
mRNA directed protein synthesis mature
mRNA codes for the polymerization of
proteins in the ribosome
Ribosome site of protein synthesis
Gene (mRNA) produced by
transcription; serves as the basis for
the protein that will be produced
Sequence of gene dictates
sequence of protein amino acids
Nucleic acid sequence of the gene is
read by tRNA creates that
sequence of amino acids for protein
synthesis
Actual formation in three steps: (1) initiation,
(2) elongation, and (3) termination
Involves the following components:
1. Ribosomes
2. Gene (mRNA)
3. Activated tRNA
4. Enzymes
5. Guanosine and adenosine
triphosphates
RIBOSOME
Located in the cytoplasm
66% RNA and 44% protein
Has two subunits: (1) heavier and (2) lighter
Prokaryotes 70s ribosome 50s heavy
and 30s light
Eukaryotes 80s ribosome 60s heavy
and 40s light
Large unit of ribosome designated with
three sites:
o A aminoacyl
o P peptidyl
o E exit
GENE (mRNA)
Codon triplet of nucleotides part of a
gene that is equivalent to one nucleotide
Anticodon tRNA translates the gene by
reading the correct codon by a
complementary anticodon
Primary structure of protein more codons
being read, more amino acids are
connected together by tRNAs
Reading of the gene 5 to 3 end
Translated protein is produced rom N
terminal to C terminal
There are 64 codons but less than 64 types
of anticodon of tRNA
PROPERTIES OF GENE TRANSLATION
1. TRIPLET AND NONAMBIGUOUS RULE
a pattern of three nucleotides code for only

2.
3.

4.

5.

one amino acid; no codon can encode more

than one kind of amino acid
DEGENERATE an amino acid may have
more than one codon coding for it
NON-OVERLAPPING nucleotides for a
codon cannot be read again on the
succeeding codon
NO PUNCTUATION/COMMALESS
nucleotide next to the last codon is the first
nucleotide of the next codon no
intervening bases in between
ALMOST UNIVERSAL most species have
the common codon-amino acid correlation
2nd base U will produce a hydrophobic
amino acid
Similar 1st base amino acid produces are
products or precursors of each other

tRNA
Reads the mRNA sequence while
processing the amino acid sequence
Further aids translation efficiency and
accuracy by considering wrong codon
sequences through wobble bases
Wobble base third base of the codon has
the variation, compared to the first and
second bases
Silent mutation a change in the DNA
sequence (3rd base) does not lead to a
change in the amino acid product
AMINO ACID ACTIVATION
tRNA serves as an adaptor for amino
acids and must be connected to them to be
able to equate them with the correct codon
upon reading
attached to an amino acid
activated
activated by aminoacly-tRNA
synthesases
Two steps of activation:
1. Amino acid covalently bonded
(through addition of ATP) to adenine
nucleotide produces aminoacylAMP
2. Ester linkage between amino acid
and either: (1) 3-hydroxyl or (2) 2hydroxyl on ribose of 3 end of tRNA
2 classes of aminoacyl-tRNA synthetases
Class I binds to 2 hydroxyl
Class II binds to 3 hydroxyl
Aminoacyl-tRNA synthetases is the primary
proofreading mechanism of translation
assures the right amino acid to the right
tRNA
INITIATION
3 protein initiation factors:

IF-1 catalyzes separation of

ribosomal subunits (30s & 50s)
o IF-2 binds GTP; aids selection of
initiator RNA
o IF-3 facilitates binding of mRNA to
30s; prevents premature 50s binding
Steps to initiation:
1. Ribosomal subunits are separated
by IF-1
2. 30s initiation complex mRNA
combines with lighter subunit (30s)
and places the first two codons to
the P and A regions aided by IF-3
3. 50s initiation complex 50s subunit
is binded with tRNA aided by IF-2
4. 70s initiation complex initiation
complexes combine
5. The tRNA for the first codon goes to
the P region and hydrogen bonds
the respective anticodon
ELONGATION
Three binding sites of tRNA present on
the 50s subunit (larger unit of ribosome)
Binds incoming
A AMINOACYL
aminoacyl-tRNA
Binds a tRNA that
P PEPTIDYL
carries a
polypeptide chain
Carries an
uncharged tRNA
E EXIT
that is about to be
released by a
ribosome
o

Steps to elongation:
a. Aminoacyl-tRNA binding
o Elongation factor detects
functional codon tRNA for
the second codon moves
toward the A region through
the elongation factor
b. Peptide bond formation between
the first and second amino acids
catalyzed by peptidyl transferase
o Amino acid on the A site
performs nucleophillic attack
on the carbonyl group of the
amino acid in the P site
forms dipeptidyl-tRNA at the
A site
o Causes a tRNA to be present
at the P site with no amino
acid attached (uncharged
tRNA)

c. Translocation takes place before

another amino acid can be added to
the growing chain
o Uncharged tRNA from the P
site moves to the E site
o Peptidyl-tRNA from the A site
moves to the P site
d. Arrival of new tRNA on the A site b
elongation factors
TERMINATION
Stop signal codons: UAA, UAG, UGA
Release factors
Binds to UAA &
RF1
UAG
Binds to UAA &
RF2
UGA
Does not bind;
facilitates the
RF3
activity of the other
two

Steps to termination:
1. Release factors recognize stop
codons
2. Release factors move towards the A
region
3. Peptidyl transferase is affected by
release factors hydrolyzes ester
bond between P tRNA and attached
amino acid synthesis stops and
the initiation complexes disassemble
POST-TRANSLATIONAL PROCESSES
Products of translation may undergo several
processes:
1. Folding towards the native form
2. Modification towards functional form
3. Degradation
4. Protein targeting
FOLDING
Most proteins can self-fold into their native
form
Some proteins cannot fold into the native
form unless helped by chaperones
MODIFICATION
The primary structure itself may be
enzymatically modified to its native form by
the following ways:
1. The N-terminal amino acid is
trimmed away
2. Amino acid residues are modified to
become other residues
hydroxylation
3. The native protein may be modified
to its functional form by addition of
prosthetic groups or bonding with
other biomolecules

DEGRADATION
Mutations in the gene may go through the
proofreading mechanism of tRNA and
create wrong sequences in protein
Proteases/proteasomes degrades wrong
proteins
Degradation well controlled process which
usually needs molecular signal that trigger
these enzymes
Ubiquitin-proteasome pathway
Common pathway using ubiquitin as
a signal for protease activation
towards the protein is it binded to
Ubiquitin 76 amino acid
polypeptide binds with a very
positively charged N-terminal of a
non-functional protein by help of E3
(ubiquitin ligase)
E1-ubiquitin activating
enzyme
E2-ubiquitin conjugating
enzyme
PROTEIN TARGETING
Proteins that are mature and fully functional
must be delivered to the right parts of the
cell
Proteins may be delivered toward the
cytoplasm or through membrane-bound
organelles
Amino acid sequences within the protein
(signal sequences) trigger transfer by the
proper organelles
Endoplasmic reticulum site where
ribosomes produce proteins that have to go
through membranes, lysosomes or export
Golgi apparatus final transport of all
proteins for delivery