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From Genes to Proteins Translation
Ch. 17
Sections 17.4, 17.5, 17.6, & 17.7
To assist you in your note
taking…
Key vocabulary terms are in

green, bold, underlined font
Overview of Concepts
1. The genetic code is a triplet

code
2. Translation is directed by RNA
molecules
3. RNA plays many different roles
in protein synthesis
4. Point mutations may affect
protein formation
The triplet code
There are 20 amino

acids (the monomers of
proteins) but only 4
nucleotides (the
monomers of nucleic
acids)
How can just 4 bases
code for 20 different
amino acids?
The triplet code
The genetic code is

based on triplets of
bases: a series of
nonoverlapping, three
nucleotide “words”
We call these base
triplets in the mRNA
codons
How did scientists
figure out it was 3
bases for each codon?
The triplet code
4 nucleotides (A,C,T,G) x 1 in a sequence =

4
different combinations
4 nucleotides x 2 in a sequence =

16 different
combinations
4 different nucleotides x 3 in a sequence =

64
different combinations (for 20 AA’s)
Only UGG codes for
tryptophan

The triplet code
The code is redundant

but unambiguous
Each codon codes for only
1 amino acid unambiguous
Some amino acids are
coded for by more than
one codon - redundant
AGU & AGC both
code for serine
How did scientists figure out what
amino acid each codon codes for?
1960s - Nierenberg & Mathaei
Used artificial RNA triplets in
tubes with the components for
building proteins
Made chains of uracil first UUUUUUUUU
Got all phenylalanines in a chain, so

UUU must code for phenylalanine.

Within a few years, they had

decoded all 64 codons
What is translation?
Translation is the

process by which a
cell interprets the
codons along an
mRNA molecule and
builds a polypeptide
Who translates the code?
Transfer RNA (tRNA)

is the interpreter of
the genetic code

tRNA is the molecule

responsible for
converting the genetic
code of nucleotides
to the protein code of
amino acids
How does tRNA work?
The cell already has all 20

amino acids in its cytoplasm

(either makes them itself or they are
taken in through the organism’s diet)

Each tRNA is a strand about

80 bases long
Some bases are
complementary to each
other so it can hydrogen
bond to itself

Takes on a clover-leaf shape
tRNA
On one end of the tRNA

is an amino acid
On the other end is an
anticodon
The anticodon is

complementary to the
codon in the mRNA
So codon by

codon, the tRNAs
deposit amino
acids in the
prescribed order,
and the ribosome
joins them into a
polypeptide chain
Some practice
 DNA template strand:

ACCGGTCAGTAC
1. Make the mRNA from this template
2. What will be the tRNA anticodons?
Ribosomes
 Ribosomes are the sites of

protein synthesis

 They are made up of

ribosomal RNA (rRNA) &
protein
 Composed of 2 subunits:
large & small
 Subunits are made in the

nucleolus
 They join together at the
mRNA to make a functional
ribosome
Ribosomes
Ribosomes bring

together the mRNA
and the tRNAs bearing
the correct amino
acids and bond those
amino acids in the
correct order
There are 3 sites on
the ribosome that
function in this
capacity: the E site,
the P site, and the A
site
A site - holds the tRNA with the next amino

acid to be added to the chain
P site - holds the tRNA carrying the growing
polypeptide chain
E site - releases tRNAs from the ribosome
here

P

A
Translation has 3 stages
Initiation
Elongation
Termination
Initiation
Brings together mRNA, the first tRNA

with the first amino acid, and the large
& small subunits of the ribosome
The first amino acid is methionine
(codon AUG, the start codon)
This establishes the reading frame
The whole thing is
called a “translation
initiation complex”
and GTP energy is
required to build it
Elongation
 More amino acids

are added to the
growing chain
 There are 3
steps catalyzed
by protein
elongation
factors
STEP 1 - Codon Recognition
 the anticodon on the
tRNA H-bonds with the
codon in the A site
1. 2 GTPs for energy are
used up here
2. An elongation factor
protein catalyzes this
step
STEP 2 - Peptide Bond Formation
The large subunit catalyzes the formation of a
peptide bond between the amino acid in the
A site and the amino acid in the P site
STEP 3 Translocation
The ribosome
moves the tRNA
in the A site to
the P site
The empty tRNA in
the P site is
moved to the E
site and released
GTP energy is
required here
Termination
Happens when one of the 3 stop

codons reaches the A site on the
ribosome
A release factor protein binds to the
stop codon & hydrolysis occurs to free
the polypeptide chain
Polyribosomes
Several ribosomes

can be working at
the same mRNA
strand at the same
time
Strings of these
ribosomes are called
polyribosomes
This helps the cell
make more proteins
more quickly
Proteins
 As the polypeptide chain

is being formed, it will
begin to coil & fold in to
its 3-D shape
 The gene determines
the order of the amino
acids - the primary
structure
 The primary structure
determines the
secondary and tertiary
structure
Proteins
 Proteins may be further

modified by the addition
of sugars, lipids, or
phosphate groups
 Enzymes may cleave the
polypeptide chain into
smaller chains
 2 or more polypeptide
chains may join to make
the quaternary structure
of a functional protein
Proteins
All translation begins in the cytosol on free

ribosomes
If the protein is destined to become part
of an organelle or is to be shipped outside
the cell, the ribosome will move to the ER
and become an attached ribosome
Proteins
There will be a signal peptide (a sequence

of amino acids) that is recognized by a
protein-RNA complex called a signal
recognition particle (SRP)
This particle brings the ribosome to the
ER and translation continues there
Types of RNA
 mRNA - messenger RNA (the

code)
 tRNA - transfer RNA (brings
amino acids)
 rRNA - ribosomal RNA (the
ribosome)
 Pre-mRNA - the primary
transcript before editing
 snRNA - part of sliceosomes
 SRP RNA - part of the signal
recognition particle
 & others
What makes RNA so versatile?
1. It can H-bond to

itself & to other
nucleic acids
2. It has functional
groups that allow it
to act as an enzyme
Point Mutations
A point mutation is a

change in a single base pair
in a gene
They can have catastrophic
consequence, or none at all
There are 3 main types:
Substitution
Insertion
Deletion
Substitution mutations
A base pair is replaced with a different

base pair
Because there is redundancy in the genetic
code, this may cause no problem at all
It could also lead to a malformed protein
and be the difference between life and
death
Substitution
 Think of it like a sentence:
 Normal sentence would read
 THE DOG BIT THE CAT
 A point mutation might make the sentence

read:

 THE DOG BIT THE CAR

This changes the meaning of the sentence, but
not dramatically.
Changing a single base can cause a

dramatic change:
The base change codes for a different

amino acid, making a different protein
Example: sickle cell anemia
 Changing a single base

may not cause any
change at all:
 The changed base may still

code for the same amino
acid
 Proline is coded for by
CCC, CCA, CCG, and CCU,
So a change in the last base
won’t make any difference
to the amino acid that is
added to the protein
chain.
Insertions & Deletions
•These mutations add an extra
letter or two or delete letters
•These mutations disrupt the
reading frame and are usually
more severe
•Because of this they are called
frameshift mutations
Frameshift Mutations
 Think of it as a sentence again:
 THE DOG BIT THE CAT
 Adding an extra letter makes it:
 THH EDO GBI TTH ECA T
 It changes the entire sentence to nonsense.

This kind of mutation has a more dramatic
effect on the DNA sequence and is usually
lethal

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AP Bio Ch 17 part 2 translation

  • 1. From Genes to Proteins Translation Ch. 17 Sections 17.4, 17.5, 17.6, & 17.7
  • 2. To assist you in your note taking… Key vocabulary terms are in green, bold, underlined font
  • 3. Overview of Concepts 1. The genetic code is a triplet code 2. Translation is directed by RNA molecules 3. RNA plays many different roles in protein synthesis 4. Point mutations may affect protein formation
  • 4. The triplet code There are 20 amino acids (the monomers of proteins) but only 4 nucleotides (the monomers of nucleic acids) How can just 4 bases code for 20 different amino acids?
  • 5. The triplet code The genetic code is based on triplets of bases: a series of nonoverlapping, three nucleotide “words” We call these base triplets in the mRNA codons How did scientists figure out it was 3 bases for each codon?
  • 6. The triplet code 4 nucleotides (A,C,T,G) x 1 in a sequence = 4 different combinations 4 nucleotides x 2 in a sequence = 16 different combinations 4 different nucleotides x 3 in a sequence = 64 different combinations (for 20 AA’s)
  • 7. Only UGG codes for tryptophan The triplet code The code is redundant but unambiguous Each codon codes for only 1 amino acid unambiguous Some amino acids are coded for by more than one codon - redundant AGU & AGC both code for serine
  • 8. How did scientists figure out what amino acid each codon codes for? 1960s - Nierenberg & Mathaei Used artificial RNA triplets in tubes with the components for building proteins Made chains of uracil first UUUUUUUUU Got all phenylalanines in a chain, so UUU must code for phenylalanine. Within a few years, they had decoded all 64 codons
  • 9. What is translation? Translation is the process by which a cell interprets the codons along an mRNA molecule and builds a polypeptide
  • 10. Who translates the code? Transfer RNA (tRNA) is the interpreter of the genetic code tRNA is the molecule responsible for converting the genetic code of nucleotides to the protein code of amino acids
  • 11. How does tRNA work? The cell already has all 20 amino acids in its cytoplasm (either makes them itself or they are taken in through the organism’s diet) Each tRNA is a strand about 80 bases long Some bases are complementary to each other so it can hydrogen bond to itself Takes on a clover-leaf shape
  • 12. tRNA On one end of the tRNA is an amino acid On the other end is an anticodon The anticodon is complementary to the codon in the mRNA
  • 13. So codon by codon, the tRNAs deposit amino acids in the prescribed order, and the ribosome joins them into a polypeptide chain
  • 14. Some practice  DNA template strand: ACCGGTCAGTAC 1. Make the mRNA from this template 2. What will be the tRNA anticodons?
  • 15. Ribosomes  Ribosomes are the sites of protein synthesis  They are made up of ribosomal RNA (rRNA) & protein  Composed of 2 subunits: large & small  Subunits are made in the nucleolus  They join together at the mRNA to make a functional ribosome
  • 16. Ribosomes Ribosomes bring together the mRNA and the tRNAs bearing the correct amino acids and bond those amino acids in the correct order There are 3 sites on the ribosome that function in this capacity: the E site, the P site, and the A site
  • 17. A site - holds the tRNA with the next amino acid to be added to the chain P site - holds the tRNA carrying the growing polypeptide chain E site - releases tRNAs from the ribosome here P A
  • 18. Translation has 3 stages Initiation Elongation Termination
  • 19. Initiation Brings together mRNA, the first tRNA with the first amino acid, and the large & small subunits of the ribosome The first amino acid is methionine (codon AUG, the start codon) This establishes the reading frame The whole thing is called a “translation initiation complex” and GTP energy is required to build it
  • 20. Elongation  More amino acids are added to the growing chain  There are 3 steps catalyzed by protein elongation factors
  • 21. STEP 1 - Codon Recognition  the anticodon on the tRNA H-bonds with the codon in the A site 1. 2 GTPs for energy are used up here 2. An elongation factor protein catalyzes this step
  • 22. STEP 2 - Peptide Bond Formation The large subunit catalyzes the formation of a peptide bond between the amino acid in the A site and the amino acid in the P site
  • 23. STEP 3 Translocation The ribosome moves the tRNA in the A site to the P site The empty tRNA in the P site is moved to the E site and released GTP energy is required here
  • 24.
  • 25. Termination Happens when one of the 3 stop codons reaches the A site on the ribosome A release factor protein binds to the stop codon & hydrolysis occurs to free the polypeptide chain
  • 26. Polyribosomes Several ribosomes can be working at the same mRNA strand at the same time Strings of these ribosomes are called polyribosomes This helps the cell make more proteins more quickly
  • 27. Proteins  As the polypeptide chain is being formed, it will begin to coil & fold in to its 3-D shape  The gene determines the order of the amino acids - the primary structure  The primary structure determines the secondary and tertiary structure
  • 28. Proteins  Proteins may be further modified by the addition of sugars, lipids, or phosphate groups  Enzymes may cleave the polypeptide chain into smaller chains  2 or more polypeptide chains may join to make the quaternary structure of a functional protein
  • 29. Proteins All translation begins in the cytosol on free ribosomes If the protein is destined to become part of an organelle or is to be shipped outside the cell, the ribosome will move to the ER and become an attached ribosome
  • 30. Proteins There will be a signal peptide (a sequence of amino acids) that is recognized by a protein-RNA complex called a signal recognition particle (SRP) This particle brings the ribosome to the ER and translation continues there
  • 31. Types of RNA  mRNA - messenger RNA (the code)  tRNA - transfer RNA (brings amino acids)  rRNA - ribosomal RNA (the ribosome)  Pre-mRNA - the primary transcript before editing  snRNA - part of sliceosomes  SRP RNA - part of the signal recognition particle  & others
  • 32.
  • 33. What makes RNA so versatile? 1. It can H-bond to itself & to other nucleic acids 2. It has functional groups that allow it to act as an enzyme
  • 34. Point Mutations A point mutation is a change in a single base pair in a gene They can have catastrophic consequence, or none at all There are 3 main types: Substitution Insertion Deletion
  • 35. Substitution mutations A base pair is replaced with a different base pair Because there is redundancy in the genetic code, this may cause no problem at all It could also lead to a malformed protein and be the difference between life and death
  • 36. Substitution  Think of it like a sentence:  Normal sentence would read  THE DOG BIT THE CAT  A point mutation might make the sentence read:  THE DOG BIT THE CAR This changes the meaning of the sentence, but not dramatically.
  • 37. Changing a single base can cause a dramatic change: The base change codes for a different amino acid, making a different protein Example: sickle cell anemia
  • 38.  Changing a single base may not cause any change at all:  The changed base may still code for the same amino acid  Proline is coded for by CCC, CCA, CCG, and CCU, So a change in the last base won’t make any difference to the amino acid that is added to the protein chain.
  • 39. Insertions & Deletions •These mutations add an extra letter or two or delete letters •These mutations disrupt the reading frame and are usually more severe •Because of this they are called frameshift mutations
  • 40. Frameshift Mutations  Think of it as a sentence again:  THE DOG BIT THE CAT  Adding an extra letter makes it:  THH EDO GBI TTH ECA T  It changes the entire sentence to nonsense. This kind of mutation has a more dramatic effect on the DNA sequence and is usually lethal