Translation Degenerate: more than one

triplet can code for the

- the synthesis of polypeptides same amino acid; Leu,
using the genetic code from RNA. Ser, and Arg, for
- Nucleic acids and proteins are example, are each coded
like two languages written with for by six triplets
different type of letters Universal: the same in
- mRNA simply tells the RNA viruses, prokaryotes, and
eukaryotes; the only
exceptions are some
codons in mitochondria

There are 64 codons

- 61 code for 20 amino acids
- 3 serve as stop codons

The ribosome moves along the

mRNA three bases at a time
rather than one or two at a
time.

- Sequence of amino acid in a

polypeptide was specified by the
sequence of nucleotide in the DNA.
- DNA unlikely to serve as a
template!
- mRNA as an intermediate in
the flow of information
from DNA to protein.

The GENETIC CODE specifies how an

mRNA sequence is translated to a
polypeptide.
- how the ribosome reads the mRNA

Features of the Genetic Code

- Triplet (codons)(by 3s)
- Nonoverlapping (di na ulet
babasahin)
- Commaless (dirediretso REQUIREMENTS FOR TRANSLATION
babasahin)
- Degenerate - RNAs (mRNA, 1 tRNA - 1 a.a., rRNA)
- Universal (set of codons is - Ribosome
- Protein Factors (IFs, EFs, RFs)
iisa)
- Activated Substances
Features of the genetic code
Triplet: a sequence of three
bases (codon) is needed
to specify one amino acid
Nonoverlapping: no bases are
shared between
consecutive codons
Commaless: no intervening
bases between codons
THE ROLE OF tRNA IN TRANSLATION

It serves as adaptor molecule,

that provides physical and
informational link between
mRNA and the polypeptide being
synthesized.

Structure of tRNA
Acceptor arm
D arm
Anticodon loop
V loop
TψC arm

anticodon - complementary w/
codon

Anti codon loop – recognize

individual codons

aaRS – attaches to 3’ acceptor

Activated amino acid – a.a. bound

to the tRNA

1 a.a. = 1 aaRS

Very specific with the a.a. they

bind to the tRNA

CODON-ANTICODON INTERACTION

Wobble base pairing is a non-

standard base pairing between the
base at 5’ end of anticodon and
the base at 3’ end of codon.

AMINOACYLATION: CHARGING OF
tRNA

Specific aminoacyl-tRNA
synthetases (aaRS) link amino
acids with their respective
tRNAs in a two-step reaction.

Energy from ATP is used to

activate the amino acid, which
is then transferred to the
tRNA molecule.
 Phases of Translation

Initiation Phase

In all organisms, synthesis of

Last letter on the 3’ end of polypeptide chain starts at the
the nucleotide – wobble N-terminal end, and grows from
position N-terminus to C-terminus

Anti codon /tRNA - 5’ end / Initiation requires:

first letter • fmet-tRNA – attached to
the N-formylmethanione;
start a.a.; first a.a.
Standard used in prokaryotes
• initiation codon (AUG) of
A-U mRNA
• 30S ribosomal subunit
Wobble base pairing • 50S ribosomal subunit
G-C/U • initiation factors IF-1,
U- A/G IF-2, & IF-3
I – A/C/U • GTP, Mg2+
Forms the initiation complex

Always AUG
is the
initiation
codon

Anti codon
of fmet –
tRNA – UAG
(direction
3’ to 5’ )

Ribosomes –
3 sites of
binding/
attachment
(E, P, A)
(50s
subunit)

30s – bind
to purine
rich leader
sequence

The
Structure
of
Ribosome
Shine-Dalgarno Sequence • elongation factors EF-Tu
(Elongation factor
temperature-
unstable), EF-Ts (EF
temperature-stable),
and EF-G (EF-GTP)
•GTP, and Mg2+

3 steps of Elongation phase

- 3’-UAC-5’ triplet on
tRNAfmet recognizes the AUG
1. aa-tRNA binding
triplet (the start codon)
when it occurs at the 2. Peptide bond formation

beginning of the mRNA 3. Translocation

sequence that directs
polypeptide synthesis
- Start codon is preceded by
a Shine-Dalgarno purine-
rich leader segment, 5’-
GGAGGU-3’, which usually
lies about 10 nucleotides
upstream of the AUG start
signal and acts as a
ribosomal binding site.

Internal methionine – madaming AUG

inside Step 1
an aminoacyl-tRNA is bound
to the A site
Shine – Dalgarno the P site is already
- malapit na yung AUG para sa
occupied
ribosome na marecognize
2nd amino acid bound to
70S initiation complex.
Elongation Phase Defined by the mRNA
Step 2
Binding sites for tRNA on the 50S EF-Tu is released in a
subunit : P (peptidyl) site, A reaction requiring EF-
(aminoacyl) site, E (exit) Ts
site. Step 3
the peptide bond is
Elongation requires: formed, the P site is
• 70S ribosome uncharged
• codons of mRNA Step 4
• aminoacyl-tRNAs the uncharged tRNA is
released
 the peptidyl-tRNA is
translocated to the P
site
EF-G and GTP are required
the next aminoacyl-tRNA
occupies the empty A
site

Posttranslational
Processing and
Modifications

Newly synthesized
polypeptides are
frequently modified
before they reach their
final form where they
exhibit biological
activity
• N-formylmethionine in
prokaryotes is cleaved/
cut

• specific bonds in
precursors are cleaved,
as for example,
preproinsulin to
proinsulin to insulin

• leader sequences are

removed by specific
Termination phase proteases of the
endoplasmic reticulum;
Chain termination requires the Golgi apparatus then
directs the finished
• stop codons (UAA, UAG, or
UGA) of mRNA protein to its final
RF-1 (Release factor-1) destination
•
which binds to 5′-UAA-3′
and 5′-UAG-3’ • factors such as heme groups
may be attached
• RF-2 (Release factor-2)
which binds to 5′-UAA-3′
and 5′-UGA-3′ • disulfide bonds may be
formed
• RF-3 (with bound GTP)which
does not bind to any • amino acids may be
termination codon, but modified, as for
facilitates the binding example, conversion of
of RF-1 and RF-2 proline to
The entire complex dissociates. hydroxyproline
• other covalent
modifications; e.g.,
addition of
carbohydrates
Start fmet-tRNA

Most of the time protein not that

active after termination

Leader sequences for them to know

where the protein is needed

Proteases – subtrate : protein