Translation

13_Translation

Protein synthesis

tRNA

tRNA adapts the RNA and protein world. Each tRNA is unique in the anticodon region that “reads the mRNA. The 3′ end of tRNA, 5′-CCA-3′, is the acceptor stem where a specific amino-acyl transferase attaches the appropriate amino acid to charge the tRNA.

TRNA-Phe yeast en
Cloverleaf configuration of a tRNA illustrates the intramolecular base-pairing. The anticodon loop is in red and is where the mRNA is “read” by the ribosome to bring about the correct amino acid.

61 types of tRNA may exist within a cell that correspond to the 61 possible coding codons. However, some cells contain less than 61 due to the inclusion of wobble

bases in the anticodon that aid in recognition of redundant codon where the third base is variable with the same amino acid.

TRNA-Phe yeast 1ehz
A three dimensional render of the secondary and tertiary structure adopted tRNA.

Ribosomes

Ribosomes are large complexes of protein and RNA. There are two subunits, a large and small subunit. In eukaryotes, the large subunit is 60S and the small subunit is 40S with an assembled size of 80S. Prokaryotes have a large subunit of 50S and small subunit of 30S with an assembled size of 60S. The small subunit comes in contact with the mRNA and assembles around it.
Ribosome mRNA translation en
In prokaryotes, the 16S rRNA contains a small sequence that specifies the reverse complement of the Shine-Dalgarno sequence. mRNA from prokaryotes contain the Shine-Dalgarno sequence that pauses the ribosome to signify that the next proximal AUG sequence is the correct start codon. This sequence is often referred to as the ribosome binding site (RBS).

Protein translation
In eukaryotes, secreted or membrane bound proteins are generated on the rough endoplasmic reticulum. The mRNA encoding secreted proteins contain codons that correspond to a signal sequence that is recognized by the signal recognition particle once it is translated. Once these amino acids come in contact with the signal recognition protein, the ribosome-mRNA complex is ferried to the endoplasmic reticulum where the growing peptide chain is fed through the ER membrane.

 

Protein Recycling

Proteasome

Ubiquitylation
E1 (ubiquitin activating enzyme) prepares ubiqutin to enter the ubiquitin pathway. E1-ubiquitin transfers ubiquitin to an E2 (ubiquitin conjugating enzyme) which will interact with an E3 (ubiquitin ligase) to ubiquitinate a substrate for degradation.
Proteins in cells have a lifespan. Proteins targeted towards degradation within the cytoplasm are tagged with a protein called ubiquitin. Ubiquitin is covalently bonded to the N-terminus of a specific lysine residue on proteins by any number of ubiquitin ligase enzymes (E3). Ubiquitin also serves as a substrate for additional tagging by E3 ligases to form polyubiquitinylated proteins that are targeted to the 26S proteasome. The proteasome is a large multimeric protein complex that serves to degrade cytosolic proteins that have been targeted by the ubiquitin pathway.