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Thesis Defense

The document provides an overview of translation, detailing its role in protein synthesis from mRNA templates and the components involved, including ribosomes and tRNA. It outlines the steps of translation: activation of amino acids, initiation, elongation, termination, and post-translational modifications. Additionally, it discusses the structure of ribosomes, the genetic code, and various inhibitors of translation.

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sivnir6
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5 views26 pages

Thesis Defense

The document provides an overview of translation, detailing its role in protein synthesis from mRNA templates and the components involved, including ribosomes and tRNA. It outlines the steps of translation: activation of amino acids, initiation, elongation, termination, and post-translational modifications. Additionally, it discusses the structure of ribosomes, the genetic code, and various inhibitors of translation.

Uploaded by

sivnir6
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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translation-

protein synthesis
A Shruthi shamyuktha
MBBS-phase 1
Overview

central dogma
definition
components of translation
ribosome structure
sites of ribsomes
genetic code
Steps
inhibitors
Central dogma:
It is the theory that states that genetic
information flows from DNA to RNA to
protein in Unidirectional manner.
What is
translation?
Translation is the synthesis of protein from
an mRNA template.

it is a cytoplasmic process, in which the


genetic information present in the form of
codons on mRNA, is translated in terms of
amino acids of the protein molecule.
Components required for
translation:
mRNA

tRNA

Ribosomes(rRNA+protein)

Amino acids

Enzymes (Aminoacyl- tRNA synthetases)

Energy- (ATP and GTP)

initiation, elongation and releasing factors


Structure of ribosomes
ribosomes are large complexes
of protein and ribosomal RNA
(predominates)

Subunits: large and small

sizes are given in terms of


sedimentation coefficient or S
(svedberg values)
prokaryotic and eukaryotic
ribosomes are similar in structure
and function
Sites in ribosome: ribosomes have three binding sites
for T RNA molecules: A,P,E.

A site-binds to aminoacyl tRNA. it


specifies the next amino acid
to be added to the growing
peptide chain

P site-occupied by peptidyl tRNA


.it carries the chain of amino acid
that has already been synthesised

E site-occupied by empty tRNA to


exit the ribosome
Genetic code feautures:

it is universal, specific,
degenerate(1 aminoacid
it helps in identification of the correspondence
with 1 codon coding for it)
between a sequence of nucleotides and a and non-overlapping
sequence of amino acid.
they refer to codons ( nucleotide triplet) that Start codon: AUG
(methionine) for trabslation
encodes for a specific aminoacid.
Stop codons:
UAA,UAG,UGA. they do not
code for amino acid and
they help in termination
Steps of translation:
ACTIVATION OF AMINOACID
(CHARGING REACTION)

INITIATION

ELONGATION

TERMINATION

POST-TRANSATIONAL MODIFICATIONS
activation of aminoacid: all amino acids are covalently
attached to their respective T RNA
to form aminoacyl tRNA at the
expense of ATP by aminoacyl tRNA
synthetase.(highly specific)
it is a two step reaction.
step1: The amino acid gets attached
to the enzyme utilising ATP to form
enzyme AMP amino acid complex.
step 2: the amino acid is
transferred to the 3’ end of the
tRNA to form aminoacyl tRNA
Initiation:
Recognition step:
eukaryotes, the first amino acid
incorporated is methionine(AUG)
the first AUG triplet codon after
the marker sequence is identified
as the start codon by the ribosome
The marker sequence is known as
Shine- Dalgarno in eukaryotes.
Initiation: Formation of preinitiation
complex:
The poly A tail interact with
60S initiation factor(e-IF) that is bound
to the cap of mRNA.
it helps in attachment of 40 S
ribosomal subunit to 5’ end of
mRNA.
40S The IF-2, GTP, met-tRNA and 40 S
ribosomal subunit are complex to
form PIC.
The Met RNA has the anticodon
UAC
Initiation: Binding of mRNA to PIC:

PIC binds with mRNA facilitated by


5’ methylated cap of mRNA.
Requires atp
it is the rate limiting step of
translation
Leads to the formation of 43S
initiation complex
Initiation: Formation of 80S complex:

initiation complex complex binds


with 60 S ribosomal unit to form
80S ribosome. Requires hydrolysis
of GDP.
Elongation:
Binding of aminoacyl tRNA to A site:
The next codon in mRNA,
determines the incoming amino
acid.
elongation factor 1(EF-1) and GTP
are complexed with incoming
aminoacyl tRNA.
GTP is hydrolysed to GDP & tRNA
binds to A site and EF1 released.
Elongation:

Peptide bond formation:

The alpha amino group at the


incoming amino acid in A site forms
a peptide bond with carboxyl group
of peptidyl tRNA of P site.
catalysed by peptidyl transferase.
what is an example of ribozyme as
RNA acts as enzyme.
Elongation: Translocation of ribosome on mRNA:
tRNA fixed at P side does not carry
any amino acid and therefore
released from the ribosome.
the peptidyl tRNA is transfered to
the P side by (EF-2).
the new aminoacyl tRNA is fixed to
the A site by base pairing with the
mRNA codon. Requies hydrolysis of
GTP to GDP
elongation is repeated till
polypeptide chain synthesis is
completed
Termination:
After successive addition of
aminoacids, ribosome reaches the
termination codon (UAA,UAG or
UGA) on mRNA.
A site remains free as there is no
tRNA. Releasing factor RF1 binds to
this site.
RF1 binds with RF3 & GTP to form a
complex which hydrolyses the
peptide chain at p site with
hydrolysis of GTP to GDP.
Termination:

The completed peptide chain is


released finally
80S ribosome dissociates into it’s
components 60S and 40S
free tRNAand free mRNA is also
released
Post translational
modifications :
Proteolytic cleavage:

modification of polypeptides by
partial proteolysis. it’s called as
trimming.
Carried out by endoproteases
resulting in the release of active
molecule.
ex: conversion of proinsulin to
insulin.
Post translational
modifications :
covalent alteration:

Gamma carboxylation: glutamic


acid residues of prothrombin under
the influence if vit k
hydroxylation: proline and lysine in
collagen with help of vit c
phosphorylation: OH group of
serine, threonine or tyrosine by
kinases ex: glycogen phosphorylase
Post translational
modifications :
covalent alteration:
glycosylation: carbohydrates are
attached to serine or threonine
through through O-glycosidic
linkages and to aspargine or
glutamine by N-glycosidic linkages
Acetylation: of lysine residues of
histones modulate transcriptional
activity of chromatin.
Post translational
modifications :
protein degradation:
the protein to be degraded marked
by attachment of ubiquitin ( small
conservational protein)
it is degraded by proteosomes
faulty degradation leads to
PRIONS.
inhibitors of translation:
Thank you :)

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