Chapter 13- Learning Objectives (mRNA Translation)

Don’t memorize the genetic code, but explain its purpose and that there are
exceptions (see
Tables 13.1, 13.2).
 ***the correspondence between a codon and the functional role that
the codon plays during translation
 **** the ability of mRNA to be translated into a specific sequence of
amino acids relies on the genetic code
 More than one codon can specify the same amino acid
 Eukaryotic organelles (mitochondria) have their own DNA that
includes a few protein-encoding genes
Outline the relationships between the coded information in a gene and the
synthesis of a polypeptide (see Figure 13.3).
 Nucleotides within DNA is transcribed to make a
complementary sequence of nucleotides within mRNA
 Sequence is then translated into a sequence of amino acids in a
polypeptide
 (tRNA molecules act as intermediates during translation)
 Codons specify particular amino acids, start codons are the first
codon at a polypeptide sequence.
 Stop codons end translation
Describe the relationship between the directionality of an mRNA and a
polypeptide (see Figure
13.4).
 Polypeptide synthesis has a directionality that parallels the order of codons
in the mRNA
o As a polypeptide is made, a peptide bond is formed between the
carboxyl group in the last amino acid and the amino group in the
amino acid being added.
 First amino acid is located at the amino-terminus, and the last amino acid is
at the carboxyl-terminus (5’ to 3’ orientation of codons)
Don’t memorize the structures of the amino acids, but describe their general
features (Figure
13.5).
  Each amino acid contains a unique R group which has chemical properties
that play a central role in determining the folding pattern of a protein (aided
by chaperones)
 Hydrophobic amino acids are in the interior of a folded protein
 Hydrophilic amino acids are on the surface of a protein where they interact
with water

Describe the four levels of protein structure (Figure 13.6).

1. Primary
2. Secondary
a. Alpha helices and beta sheets
3. Tertiary
4. Quaternary

Describe the structure and function of tRNAs (see Figures 13.9, 13.10).
 tRNA molecules recognize the codons within mRNA and carry the correct
amino acids to the site of polypeptide synthesis
 During mRNA-tRNA recognition, the anticodon in the tRNA molecule
binds to a codon in mRNA in an antiparallel manner (AU/GC)
 Cloverleaf
o 3 stem loops
o A few variable sites
 Sites differ in the number of nucleotides the contain
o Acceptor stem with a 3’ single-stranded region
 This is where an amino acid becomes attached to a tRNA


Explain how amino acids are attached to tRNAs via aminoacyl-tRNA synthetases
(see Figure
13.11).
1. synthetase recognizes a specific amino acid and ATP
2. Amino acid and ATP bind to the enzyme
3. AMP is covalently bound to the amino acid and pyrophosphate is released
4. The correct tRNA binds to the enzyme.
5. Amino acid becomes covalently attached to the 3’ end of tRNA
6. AMP is released
7. Charged tRNA is released

Describe the three stages of translation (see Figures 13.15, 13.16, 13.17, 13.18).
 INITIATION:
o mRNA and first tRNA bind to ribosomal units
o Initiator tRNA recognizes the start codon in mRNA
o mRNA, tRNA(fmet), and ribosomal subunits associate with each
other to form an initiation complex
 Uses IF1, IF2, and IF3
 IF1 and 3 bids to 30S subunit which is facilitated by the Shine-
Dalgarno sequence (promotes hydrogen bonding of mRNA to
the 30S subunit
 IF2 promotes the binding of the initiator tRNA to the mRNA
that’s already bound to the 30S subunit
o mRNA binds to 30S subunit
 facilitated by Shine-dalgarno sequence
 Shine-Dalgarno: complementary to short sequence
 Promotes hydrogen bonding of mRNA to 30S
o IF2 (bound to GTP) promotes binding of initiator tRNA to start
codon in P site
o IF1 and IF3 are released
o IF2 hydrolyzes its GTP and is released
o 50S subunit associates
 ELONGATION:
o Charged tRNA binds to A site
 EF-Tu facilitates tRNA binding and hydrolyzes GTP
o Peptidyl transferase catalyzes peptide bond formation between
polypeptide and amino acid in A site
o Polypeptide is transferred to A site
o Ribosome translocated 1 codon to the right
 Promoted by EF-G which hydrolyzes GTP
o Uncharged tRNA is released from E site
o ** process is repeated until stop codon is reached
 TERMINATION:
o Stop codon is reached
o Release factor binds to A site
o Polypeptide is cleaved from tRNA in P site
o tRNA is released
o ribosomal subunits, mRNA, and release factor dissociate