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From RNA to Proteins


In protein synthesis, the translation of RNA into a polypeptide, and the involvement of the ribosomes are the most important parts of the process.


Legend to the Diagrams

Initiation

initiation

In the first step in protein synthesis, the small 30S subunit of the ribosomeask Dr Chromo! binds to the mRNA molecule (Diagram 1): this contains triplet codon (AUG, or GUG) at which protein synthesis starts.
In bacteria, the first AA-tRNAask Dr Chromo! to initiate translation is always a formyl derivative of methionine called FMet-tRNAask Dr Chromo!.

The ribosome is able to discriminate between an AUG within an RNA sequence and at the beginning of mRNA. When this codon appears in the middle of messenger RNA, a normal methionine is incorporated.

In eukaryotes, synthesis is started by a special initiation Met-tRNA, but the methionine is not formylated. However, the initial methionine is usually split off from the finished polypeptide.

The start of translation requires three protein factors, and the binding of an initiator Fmet-tRNA (or Met) to the first AUG codon found on mRNA.



Step 1 of Elongation

Diagram   2
Binding of the bigger subunit of the ribosome to the small one , to form the complete 70S ribosome (Diagram 2).

Diagram  3
Then the second AA-tRNA arrives in the Aminoacyl site (acceptor site), and binds to the complex (Diagram 3).

Diagram   4
The reaction between the first amino acid and the second one leads to the formation of a peptide bondask Dr Chromo!. A molecule of water is released ( it is a condensationask Dr Chromo! reaction) (Diagram 3b). This only happens after hydrolysis of a GTP into GDP which allows the elongation factor to leave. This delay allows for proof reading as a wrong tRNA would leave before the reaction takes place.

Step 2 of Elongation

The second tRNA has now moved into place and the now free tRNA has been released. Translocation can take place: it is the transfer of the newly formed dipeptide into the peptidyl site (the first one, also called donor site) (Diagram 4) when the ribosome shifts 3 nucleotides.

The third AA (R)-tRNA can then bind to the mRNA / ribosome complex, and a new peptide bond is formed (Diagram 5).


Step 3 of Elongation

This step is a repeat of step two, to show that once the process starts, it is fast, and repetitive. Diagram 6 a and b

Animation

To summarize this, why not see the movie?



Termination

Termination of the polypeptide occurs when the ribosome reaches a "Stop" Codon.

Chain termination leads to the release of a polypeptide, and tRNA, and the dissociation of the ribosome into 30S and 50S subunits. Stop codons are triplets which are not recognized by any tRNA (UAA, UAG, UGA), but by two proteins: the releasing factors (R), (R1 recognizes UAG and UAA, R2 recognizes UAA and UGA).

The polypeptide released will be processed in different parts of the cell, depending on its role, and destination. All the processing involved depends on the polypeptide sequence, therefore on the mRNA sequence (and therefore on the original DNA base sequence).


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