Prokaryotic Translation

The Ribosome has 3 major sites

Exit site (E site)

Aminoacyl site (A site)
Peptidyl site (P site)
Stages of Translation
Step 1: Initiation
Initiation Complex

The formation of complex requires the

participation of three initiation factors (IF):
IF1, IF2, and IF3.

First, IF1 and IF3 bind to the 30S subunit.

IF1 and IF3 prevent the association of the 50S

subunit.
Next, the mRNA binds to the 30S subunit.
Step 2: Elongation

Under normal cellular conditions, a polypeptide can elongate at a rate of

15 to 20 amino acids per second in bacteria and

2 to 6 amino acids per second in eukaryotes!

1st

A charged tRNA carrying a single amino acid binds to the A site with

help of EF-Tu GTP.

This binding occurs because the anticodon in the tRNA is complementary to

the codon in the mRNA

The hydrolysis of GTP by the elongation factor, EF-Tu, provides

energy for the binding of a tRNA to the A site.

2nd
Who will ensures the proper recognition between the mRNA and correct tRNA?

The 16S rRNA

can detect when an incorrect tRNA is bound at the A site and

prevents elongation until the mispaired tRNA is released from the A site.

Decoding function of the ribosome

3rd The next step of elongation is the peptidyl transfer reaction—

the polypeptide is removed from the tRNA in the P site

and transferred to the amino acid at the A site.
4th The next step of elongation is the Ribosome Translocation reaction—

This moves the tRNAs at the P and A sites to the E and P sites, respectively.
Finally, the uncharged tRNA exits the E site.

New charged tRNA can enter the empty A site, and

the same series of steps can add the next amino acid to the growing polypeptide

Factor required for translocation EF-G

Step 3: Termination

Termination occurs when a stop codon is reached in the mRNA

The stop codons are not recognized by a tRNA with a complementary sequence.

Instead, they are recognized by proteins known as Release factors

 Three-dimensional structures of release factor proteins are
“molecular mimics” that resemble the structure of tRNAs.

Such proteins can specifically bind to a stop codon sequence.

In bacteria,

RF1 recognizes UAA and UAG, and

RF2 recognizes UGA and UAA.
A third release factor, RF3, is also required.
In the first step, RF1 or RF2 binds to
the stop codon at the A site