TRANSLATION

 The last stage of central dogma.

 Cistron-a unit of DNA or RNA responsible for controlling a
specific body character.
 Muton is mutable unit that could be up to five nucleotides long.
 Recon is the smallest unit that participates in a recombination
event.
 Regulon a group of genes that are coordinately regulated.
 Translation
Important components needed for translation
1. Aminoacids
2. Ribosomes- Amino acid site Peptidyl site
3. mRNA
4. tRNA
5. Enzymes
a. Aminoacid activating system( amino acyl tRNA synthetase)
b. Peptide polymerase system
6. ATP for energy source
7. GTP for synthesis of peptide bonds
8 . Initiation and transcription factors
9. Various Inorganic Factors(eg.,K+,Mg+NH+)
Activation of Aminoacid

1. AA+ ATP+ Aminoacyl Synthetase

Aminoacyl Adenylate + Pyrophosphate

2.AA-AMP-ENZYME + tRNA

AA-tRNA + AMP + Enzyme

 Translation in Prokaryotes
 Initiation: the important change seen in prokaryotes
is in place of methionine , N-Formyl methionine is
the initiator codon in prokaryotes.
 Initiation is important step in translation where an
30S pre-initiation complex form with the association
of (mRNA, 30S ribosome, fmet-tRNA, three
proteins called as initiation factors, GTP
 Shine Dalgarno sequence: It is an 8 to 13 nucleotide
length an untranslated region of mRNA which
consists of ribosome binding site occurs near to
AUG codon which is also base pairs with 16srRNA
 Initiation
 1st step: the fmet-tRNA charged with first
aminoacid binds with the 30S ribosome at the P
site
 2nd step: fmet-tRNA-30S ribosome binds to 50S
Subunit to form the complete 70S Initiation
Complex.
 Energy for this process is provided by Hydrolysis
of GTP brought to initiation complex by IF2
Protein
 After initiation two parts of ribosome hold mRNA
in the form ribbon at both side.
 Four binding sites are located on the ribosome, one for
mRNA and three for tRNA
 The three tRNA sites are labeled P, A, and E
 The P site, called the peptidyl site, binds to the tRNA
holding the growing polypeptide chain of amino acids.
 The A site (acceptor site), binds to the aminoacyl tRNA,
which holds the new amino acid to be added to the
polypeptide chain. The E site (exit site), serves as a
threshold
 Amino acid, any of a group of organic molecules that
consist of a basic amino group (―NH2), an acidic
carboxyl group (―COOH), and an organic R group (or
side chain) that is unique to each amino acid.
Elongation
 In this stage second tRNA binds to the ribosome at
the A site with the help of proteins called as
elongation factors.
 EF-Tu protein provides proper positioning of
aminoacid which also provides energy for the process
by carrying a molecule of GTP.
 Next important step is formation of peptide bond
between two amino acid takes place by replacing first
aminoacid to top second aminoacid
 Ensuring bond between carboxyl group of first amino
acid to the amino group of second aminoacid.
 The resulting compound is dipeptide reaction is catalysed
by peptidyl transferase enzyme.
 The energy for this reaction is provided by dissolution
amino acyl bond between its first amino acid and its
tRNA.
 Next step in elongation is translocation which involves.
(a) Ejection of discharged fmet-tRNA from P site
(b) Movement of physical lifting of dipeptide from A site.
(c) movement of mRNA in 5’ to 3’ direction for further
processing.
Termination:
 Elongation continues until the ribosome encounters
terminator codons UAA,UGA and UAG.
 These terminator codon are recognized by protein
release factors(RF-s),RF1 recognizes UAA and UAG
while RF2 recognizes UGA where as RF3
stimulates both RF1 and RF2
 Enzyme peptidyl transferase releases polypeptide
from tRNA which now serve as hydrolysae enzyme
and 70S ribosome dissociate in to two parts 50S and
30S and leave mRNA.