Professional Documents
Culture Documents
Eukaryotic Translation
Eukaryotic Translation
The broad outlines of eukaryotic protein synthesis are the same as in prokaryotic
protein synthesis. The genetic code is generally the same (some microorganisms and
eukaryotic mitochondria use slightly different codons), rRNA and protein sequences are
recognizably similar, and the same set of amino acids is used in all organisms.
However, specific differences exist between the two types of protein synthesis at all
steps of the process.
Initiation
Both prokaryotes and eukaryotes initiate protein synthesis with a specialized methionyl‐
tRNA in response to an AUG initiation codon. Eukaryotes, however, use an initiator met
—tRNA met I—that is not formylated. Recognition of the initiator AUG is also different.
Only one coding sequence exists per eukaryotic mRNA, and eukaryotic mRNAs are
capped. Initiation, therefore, uses a specialized cap‐ binding initiation factor to position
the mRNA on the small ribosomal subunit. Usually, the first AUG after the cap (that is,
3′ to it) is used for initiation.
Elongation
Most differences in elongation result from the fact that the eukaryotic cell has different
compartments, which are separated by membranes. Both prokaryotic and eukaryotic
cells, of course, have an inside and outside; however, eukaryotic proteins can be
targeted to, for example, the mitochondrion.
Translating ribosomes in eukaryotes are located in different places in the cell depending
on the fate of their proteins. Free polysomes are in the cytoplasm and synthesize
cytoplasmic proteins and those that are bound for most intracellular organelles, for
example, the nucleus. Members of the second class of polysomes, membrane‐bound
polysomes, are attached to the endoplasmic reticulum (forming the rough ER), and
synthesize exported proteins. In cells that are actively secreting enzymes or hormones
(for example, those in the pancreas), most of the protein synthesis occurs on the rough
ER.
The messages encoding exported proteins must be recognized. For example, the
digestive proteases are made in the pancreas. If they are released into the pancreas
rather than the intestine, they will self‐digest the organ that makes them. Carrying out
this export efficiently is obviously important. The signal hypothesis explains how
proteins destined for export are discriminated. Proteins that are destined for export
contain a short (less than 30 amino acids long) sequence made up
ofhydrophobic amino acids at their amino terminus. Because peptide synthesis occurs
in the amino‐to‐carboxy direction, the signal peptide is the first part of the protein that
is made. Signal peptides are not found in most mature secreted proteins because they
are cleaved from the immature proteins during the secretion and maturation process.
See Figure 1.
Figure 1
Figure 2