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PROTEIN SYNTHESIS
Table of Contents
One-gene-one-protein|The structure of hemoglobin|Viruses contain DNA
RNA links the information in DNA to the sequence of amino acids in protein
Transcription: making an RNA copy of a DNA sequence|The Genetic Code
Protein Synthesis|Mutations redefined|Links
One-gene-one-protein |Back to Top
During the 1930s, despite great advances, geneticists had several frustrating questions
yet to answer:
What exactly are genes?
How do they work?
What produces the unique phenotype associated with a specific allele?
Answers from physics, chemistry, and the study of infectious disease gave rise to the
field of molecular biology. Biochemical reactions are controlled byenzymes,and
often are organized into chains of reactions known asmetabolic pathways.Loss ofactivity in a single enzyme can inactivate an entire pathway.
Archibald Garrod, in 1902, first proposed the relationship through his study of
alkaptonuria and its association with large quantities "alkapton". He reasoned
unaffected individuals metabolized "alkapton" (now called homogentistic acid) to
other products so it would not buildup in the urine. Garrod suspected a blockage of the
pathway to break this chemical down, and proposed that condition as "an inborn error
of metabolism". He also discovered alkaptonuria was inherited as a recessive
Mendelian trait.
George Beadle and Edward Tatum during the late 1930s and early 1940s established
the connection Garrod suspected between genes and metabolism. They used X rays to
cause mutations in strains of the moldNeurospora. These mutations affected a single
genes and single enzymes in specific metabolic pathways. Beadle and Tatum
proposed the "one gene one enzyme hypothesis" for which they won the Nobel Prize
in 1958.
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Since the chemical reactions occurring in the body are mediated by enzymes, and
since enzymes are proteins and thus heritable traits, there must be a relationship
between the gene and proteins. George Beadle, during the 1940s, proposed that
mutant eye colors inDrosophilawas caused by a change in one protein in a
biosynthetic pathway.
In 1941 Beadle and coworker Edward L. Tatum decided to examine step by step the
chemical reactions in a pathway. They usedNeurospora crassaas an experimental
organism. It had a short life-cycle and was easily grown. Since it ishaploidfor much
of its life cycle, mutations would be immediately expressed. The meiotic products
could be easily inspected. Chromosome mapping studies on the organism facilitated
their work.Neurosporacan be grown on a minimal medium, and it's nutrition could
be studied by its ability to metabolize sugars and other chemicals the scientist could
add or delete from the mixture of the medium. It was able to synthesize all of the
amino acids and other chemicals needed for it to grow, thus mutants in synthetic
pathways would easily show up. X-rays induced mutations inNeurospora, and the
mutated spores were placed on growth media enriched with all essential amino acids.
Crossing the mutated fungi with non-mutated forms produced spores which were then
grown on media supplying only one of the 20 essential amino acids. If a spore lacked
the ability to synthesize a particular amino acid, such as Pro (proline), it would only
grow if the Proline was in the growth medium. Biosynthesis of amino acids (the
building blocks of proteins) is a complex process with many chemical reactions
mediated by enzymes, which if mutated would shut down the pathway, resulting in
no-growth. Beadle and Tatum proposed the "one gene one enzyme"theory. One gene
codes for the production of one protein. "One gene one enzyme" has since been
modified to "one gene one polypeptide"since many proteins (such as hemoglobin) are
made of more than one polypeptide.
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The Beadle and Tatum experiment that suggested the one gene one enzyme
hypothesis. Images from Purves et al., Life: The Science of Biology, 4th Edition, by
Sinauer Associates (www.sinauer.com)and WH Freeman (www.whfreeman.com),
used with permission.
The Structure of Hemoglobin |Back to Top
Linus Pauling used electrophoresis to separatehemoglobinmolecules. Sickle-cell
anemia (h) is a recessive allele in which a defective hemoglobin is made, ultimately
causing pain and death to those individuals homozygous recessive for the trait.
Pauling reasoned that if Beadle and Tatum were correct, there should be a slight (but
detectable) difference between the structure of a normal (HH) and sickle cell (hh)
hemoglobin due to genetic differences. Heterozygotes (Hh, also sampled by Pauling)
make both normal and "sickle cell" hemoglobins. Later, Vernon Ingram discovered
that the normal and sickle-cell hemoglobins differ by only 1 (out of a total of
300)amino acids.
Viruses Contain DNA |Back to Top
The coats of viruses act asantigens,initiating an antigen-specificantibodyresponse.
Remember that vaccines work by either prompting the immune system to make
antibodies or by supplying antibodies. If a virus (or anything else for that matter)
mutates its antigens, the immune system is forever playing catch-up.
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RNA Links the Information in DNA to the Sequence of Amino Acids in Protein
|Back to Top
Ribonucleic acid (RNA)was discovered after DNA. DNA, with exceptions in
chloroplasts and mitochondria, is restricted to the nucleus (in eukaryotes,
thenucleoidregion in prokaryotes). RNA occurs in the nucleus as well as in thecytoplasm (also remember that it occurs as part of theribosomesthat line the rough
endoplasmic reticulum).
Scientists for some time had suspected such a link between DNA and proteins. Cells
of developing embryos contain high levels of RNA. Rapidly growingE. colihas half
its mass as ribosomes. Ribosomes are 2/3 RNA (a type of RNA known asribosomal
RNAor rRNA) and 1/3 protein. RNA is synthesized from viral DNA in an infected
cell before protein synthesis begins. Some viruses, for example Tobacco Mosaic Virus
(TMV) have RNA in place of DNA. If RNA extracted from a virus was injected into a
host cell the cell began to make new viruses. Clearly RNA was involved in proteinsynthesis.
Crick's central dogma. Information flow (with the exception ofreverse transcription)
is from DNA to RNA via the process oftranscription,and thence to protein
viatranslation.Transcription is the making of an RNA molecule off a DNA template.
Translation is the construction of anamino acid sequence(polypeptide) from an RNA
molecule. Although originally called dogma, this idea has been tested repeatedly with
almost no exceptions to the rule being found (saveretroviruses).
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The central dogma. Image from Purves et al., Life: The Science of Biology, 4th
Edition, by Sinauer Associates (www.sinauer.com)and WH Freeman
(www.whfreeman.com), used with permission.
The blue-background graphics throughout this chapter are from the University of
Illinois'DNA and Protein Synthesissite.
Messenger RNA (mRNA)is the blueprint for construction of a protein.Ribosomal
RNA(rRNA) is the construction site where the protein is made.Transfer RNA
(tRNA)is the truck delivering the proper amino acid to the site at the right time.
RNA has ribose sugar instead of deoxyribose sugar. The baseuracil(U) replaces
thymine (T) in RNA. Most RNA is single stranded, although tRNA will form a
"cloverleaf" structure due tocomplementarybase pairing.
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Transcription: making an RNA copy of a DNA sequence |Back to Top
RNA polymeraseopens the part of the DNA to be transcribed. Only one strand of
DNA (thetemplate strand)is transcribed. RNA nucleotides are available in the region
of the chromatin (this process only occurs during Interphase) and are linked together
similar to the DNA process.
The Genetic Code: Translation of RNA code into protein |Back to Top
The code consists of at least three bases, according to astronomer George Gamow. To
code for the 20 essential amino acids agenetic codemust consist of at least a 3-base
set (triplet) of the 4 bases. If one considers the possibilities of arranging four things 3
at a time (4X4X4), we get 64 possible code words, or codons (a 3-base sequence on
the mRNA that codes for either a specific amino acid or a control word).
The genetic code was broken by Marshall Nirenberg and Heinrich Matthaei, a decade
after Watson and Crick's work. Nirenberg discovered that RNA, regardless of its
source organism, could initiate protein synthesis when combined with contents of
broken E. coli cells. By adding poly-U to each of 20 test-tubes (each tube having a
different "tagged" amino acid) Nirenberg and Matthaei were able to determine that the
codon UUU (the only one in poly-U) coded for the amino acid phenylalanine.
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Steps in breaking the genetic code: the deciphering of a poly-U mRNA. Image from
Purves et al., Life: The Science of Biology, 4th Edition, by Sinauer Associates
(www.sinauer.com) and WH Freeman (www.whfreeman.com), used with permission.
Likewise, an artificial mRNA consisting of alternating A and C bases would code for
alternating amino acids histidine and threonine. Gradually, a complete listing of the
genetic code codons was developed.
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Deciphering the code: poly CA. Image from Purves et al., Life: The Science of
Biology, 4th Edition, by Sinauer Associates (www.sinauer.com) and WH Freeman
(www.whfreeman.com), used with permission.
The genetic code consists of 61 amino-acid coding codons and three termination
codons, which stop the process of translation. The genetic code is thus redundant(degenerate in the sense of having multiple states amounting to the same thing), with,
for example, glycine coded for by GGU, GGC, GGA, and GGG codons. If a codon is
mutated, say from GGU to CGU, is the same amino acid specified?
The genetic code. Image from Purves et al., Life: The Science of Biology, 4th Edition,
by Sinauer Associates (www.sinauer.com)and WH Freeman (www.whfreeman.com),
used with permission.
Protein Synthesis |Back to Top
Prokaryotic gene regulation differs from eukaryotic regulation, but since prokaryotes
are much easier to work with, we focus on prokaryotes at this point.Promotersaresequences of DNA that are the start signals for the transcription of mRNA.
Terminators are the stop signals. mRNA molecules are long (500- 10,000
nucleotides).
Ribosomes are the organelle (in all cells) where proteins are synthesized. They consist
of two-thirds rRNA and one-third protein. Ribosomes consist of a small (inE. coli,
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30S) and larger (50S) subunits. The length of rRNA differs in each. The 30S unit has
16S rRNA and 21 different proteins. The 50S subunit consists of 5S and 23S rRNA
and 34 different proteins. The smaller subunit has a binding site for the mRNA. The
larger subunit has two binding sites for tRNA.
Subunits of a ribosome. Image from Purves et al., Life: The Science of Biology, 4th
Edition, by Sinauer Associates (www.sinauer.com)and WH Freeman
(www.whfreeman.com), used with permission.
Transfer RNA (tRNA) is basically cloverleaf-shaped. tRNA carries the proper amino
acid to the ribosome when the codons call for them. At the top of the large loop arethree bases, theanticodon,which is the complement of thecodon.There are 61
different tRNAs, each having a different binding site for the amino acid and a
different anticodon. For the codon UUU, the complementary anticodon is AAA.
Amino acid linkage to the proper tRNA is controlled by the aminoacyl-tRNA
synthetases. Energy for binding the amino acid to tRNA comes from ATP conversion
to adenosine monophosphate (AMP).
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Two models of tRNA. Image from Purves et al., Life: The Science of Biology, 4th
Edition, by Sinauer Associates (www.sinauer.com)and WH Freeman
(www.whfreeman.com), used with permission.
Translation is the process of converting the mRNA codon sequences into an amino
acid sequence. Theinitiator codon(AUG) codes for the amino acid N-formylmethionine (f-Met). No transcription occurs without the AUG codon. f-Met is
always the first amino acid in a polypeptide chain, although frequently it is removed
after translation. The intitator tRNA/mRNA/small ribosomal unit is called the
initiation complex. The larger subunit attaches to the initiation complex. After
theinitiationphase the message gets longer during theelongationphase.
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Translation. Image from Purves et al., Life: The Science of Biology, 4th Edition, by
Sinauer Associates (www.sinauer.com)and WH Freeman (www.whfreeman.com),
used with permission.
New tRNAs bring their amino acids to the open binding site on the ribosome/mRNA
complex, forming a peptide bond between the amino acids. The complex then shifts
along the mRNA to the next triplet, opening the A site. The new tRNA enters at the A
site. When the codon in the A site is a termination codon, a releasing factor binds to
the site, stopping translation and releasing the ribosomal complex and mRNA.
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Termination. Image from Purves et al., Life: The Science of Biology, 4th Edition, by
Sinauer Associates (www.sinauer.com)and WH Freeman (www.whfreeman.com),
used with permission.
Often many ribosomes will read the same message, a structure known as a polysome
forms. In this way a cell may rapidly make many proteins.
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Many ribosomes translating the same message, a polysome. Image from Purves et
al., Life: The Science of Biology, 4th Edition, by Sinauer Associates
(www.sinauer.com) and WH Freeman (www.whfreeman.com), used with permission.
The illustration below is from Genentech's Access Excellence site, which may be
reeached by clickinghere.The drawing is availableathttp://www.gene.com/ae/AB/GG/protein_synthesis.html
Mutations Redefined |Back to Top
We earlier defined mutations as any change in the DNA. We now can refine that
definition: a mutation is a change in the DNA base sequence that results in a change
of amino acid(s) in the polypeptide coded for by that gene. Alleles are alternate
sequences of DNA bases (genes), and thus at the molecular level the products of
alleles differ (often by only a single amino acid, which can have a ripple effect on an
organism by changing ). Addition, deletion, or addition of nucleotides can alter the
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polypeptide. Point mutations are the result of the substitution of a single base. Frame-
shift mutations occur when the reading frame of the gene is shifted by addition or
deletion of one or more bases. With the exception of mitochondria, all organisms use
the same genetic code. Powerful evidence for the common ancestry of all living
things.
Links |Back to Top
The Genetic Code
The genetic code consists of 64 triplets ofnucleotides.
These triplets are called codons.With three exceptions,
each codon encodes for one of the 20amino acidsused
in the synthesis of proteins. That produces someredundancy in the code: most of the amino acids being
encoded by more than one codon.
One codon, AUGserves two related functions:
it signals the start oftranslation
it codes for the incorporation of the amino acidmethionine(Met) into the
growing polypeptide chain
The genetic code can be expressed as either RNA codons or DNA codons. RNAcodons occur inmessenger RNA(mRNA) and are the codons that are actually "read"
during the synthesis of polypeptides (the process calledtranslation). But each mRNA
molecule acquires its sequence of nucleotides bytranscriptionfrom the corresponding
gene. Because DNA sequencing has become so rapid and because most genes are now
being discovered at the level of DNA before they are discovered as mRNA or as a
protein product, it is extremely useful to have a table of codons expressed as DNA. So
here are both.
Note that for each table, the left-hand column gives the first nucleotide of the codon,
the 4 middle columns give the second nucleotide, and the last column gives the third
nucleotide.
The RNA CodonsSecond nucleotide
Index to this page
The RNA Codons
The DNA Codons
Codon Bias Exceptions to the Code
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U C A G
U
UUU Phenylalanine(Phe) UCU Serine(Ser) UAU Tyrosine(Tyr) UGU Cysteine(Cys) U
UUC Phe UCC Ser UAC Tyr UGC Cys C
UUA Leucine(Leu) UCA Ser UAA STOP UGA STOP A
UUG Leu UCG Ser UAG STOP UGG Tryptophan(Trp) G
C
CUU Leucine(Leu) CCU Proline(Pro) CAU Histidine(His) CGU Arginine(Arg) U
CUC Leu CCC Pro CAC His CGC Arg C
CUA Leu CCA Pro CAA Glutamine(Gln) CGA Arg A
CUG Leu CCG Pro CAG Gln CGG Arg G
A
AUU Isoleucine(Ile) ACU Threonine(Thr) AAU Asparagine(Asn) AGU Serine(Ser) U
AUC Ile ACC Thr AAC Asn AGC Ser C
AUA Ile ACA Thr AAA Lysine(Lys) AGA Arginine(Arg) A
AUG Methionine(Met)
or START
ACG Thr AAG Lys AGG Arg G
G
GUU ValineVal GCU Alanine(Ala)GAU Aspartic
acid(Asp)GGU Glycine(Gly) U
GUC (Val) GCC Ala GAC Asp GGC Gly C
GUA Val GCA AlaGAA Glutamic
acid(Glu)GGA Gly A
GUG Val GCG Ala GAG Glu GGG Gly G
The DNA Codons
These are the codons as they are read on thesense(5' to 3') strand of DNA. Except that
the nucleotide thymidine (T) is found in place of uridine (U), they read the same as
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RNA codons. However, mRNA is actually synthesized using theantisense strand of
DNA(3' to 5') as the template. [Discussion]
This table could well be called the Rosetta Stone of life.
The Genetic Code (DNA)
TTT Phe TCT Ser TAT Tyr TGT Cys
TTC Phe TCC Ser TAC Tyr TGC Cys
TTA Leu TCA Ser TAA STOP TGA STOP
TTG Leu TCG Ser TAG STOP TGG Trp
CTT Leu CCT Pro CAT His CGT Arg
CTC Leu CCC Pro CAC His CGC Arg
CTA Leu CCA Pro CAA Gln CGA Arg
CTG Leu CCG Pro CAG Gln CGG Arg
ATT Ile ACT Thr AAT Asn AGT Ser
ATC Ile ACC Thr AAC Asn AGC Ser
ATA Ile ACA Thr AAA Lys AGA Arg
ATG Met* ACG Thr AAG Lys AGG Arg
GTT Val GCT Ala GAT Asp GGT Gly
GTC Val GCC Ala GAC Asp GGC Gly
GTA Val GCA Ala GAA Glu GGA Gly
GTG Val GCG Ala GAG Glu GGG Gly
*When within gene; at beginning of gene, ATG signals start of translation.
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Codon Bias
All but two of the amino acids (Met and Trp) can be encoded by from 2 to 6 different
codons. However, the genome of most organisms reveals that certain codons are
preferred over others. In humans, for example, alanine is encoded by GCC four times
as often as by GCG. This probably reflects a greatertranslationefficiency by the
translation apparatus (e.g., ribosomes) for certain codons over their synonyms. [More]
Exceptions to the CodeThe genetic code is almostuniversal. The same codons are assigned to the same
amino acids and to the same START and STOP signals in the vast majority of genes in
animals, plants, and microorganisms. However, some exceptions have been found.
Most of these involve assigning one or two of the three STOP codons to an amino
acid instead.
Mitochondrial genes
When mitochondrial mRNA from animals or microorganisms (but not from plants) is
placed in a test tube with the cytosolic protein-synthesizing machinery (amino acids,
enzymes, tRNAs, ribosomes) it fails to be translated into a protein.
The reason: these mitochondria use UGA to encode tryptophan (Trp) rather than as a
chain terminator. When translated by cytosolic machinery, synthesis stops where Trp
should have been inserted.
In addition, most
animal mitochondria use AUA for methionine not isoleucine and
all vertebrate mitochondria use AGA and AGG as chain terminators.
Yeast mitochondria assign all codons beginning with CU to threonine instead
of leucine (which is still encoded by UUA and UUG as it is in cytosolic mRNA).
Plant mitochondria use the universal code, and this has permittedangiospermsto
transfer mitochondrial genes to their nucleus with great ease.
Link to discussion of mitochondrial genes.
Nuclear genes
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Violations of the universal code are far rarer for nuclear genes.
A few unicellular eukaryotes have been found that use one or two (of their three)
STOP codons for amino acids instead.
Nonstandard Amino Acids
The vast majority of proteins are assembled from the 20 amino acids listed above even
though some of these may be chemically altered, e.g. by phosphorylation, at a later
time.
However, two cases have been found where an amino acid that is not one of the
standard 20 is inserted by a tRNAinto the growing polypeptide.
selenocysteine. This amino acid is encoded by UGA. UGA is still used as achain terminator, but thetranslation machineryis able to discriminate when a
UGA codon should be used for selenocysteine rather than STOP. This codon
usage has been found in certainArchaea,eubacteria,and animals (humans
synthesize 25 different proteins containing selenium).
pyrrolysine. In several species of Archaea and bacteria, this amino acid is
encoded by UAG. How the translation machinery knows when it encounters
UAG whether to insert a tRNA with pyrrolysine or to stop translation is not yet
known.
Prokaryotes and the Operon Model
Prokaryotes are sensitive to their environment, and their genetic activity is controlled by specific proteins
that interact directly with their DNA to quickly adjust to environmental changes. Genetic expressionis the
process where genotypes coded in the genes are exhibited by the phenotypes of the individuals. The
DNA is copied by the RNA and then synthesized into protein. The process of transcription, which is the
synthesis of RNA from a DNA template, is where the regulation of the gene expression is most likely to
occur. The default setting for prokaryotes appears to allow for the continual synthesis of protein to occur,
whereas in eukaryotes the system is normally off until activated.
An operon is a self-regulating series of genes that work in concert. An operon includes a special segment
of genes that are regulators of the protein synthesis, but do not code for protein, called the promoter and
operator. These segments overlap, and their interaction determines whether the process will start and
when it will stop. RNA polymerase must create RNA by moving along the chromosome and reading the
genes in the process of transcription.
RNA polymerase first attaches to the promoter segment, which signals the beginning of a particular DNA
sequence. If not blocked, it passes over the operator and reaches the protein-producing genes where it
creates the mRNA that instructs the ribosomes to create the desired protein. This process continues until
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the system is blocked by repressor proteins. Repressors bind with the operator and prevent RNA
polymerase from proceeding to create mRNA by prohibiting access to the remainder of the protein-
producing genes. As long as the repressor is binding with the operator, no proteins are made. However,
when an induceris present, it binds with the repressor, causing the repressor to change shape and
release from the operator. When this happens, the RNA polymerase can proceed with transcription, and
protein synthesis begins and continues until another repressor binds with the operator. Refer to the
illustration Transcription regulation.
Transcription regulation.
The lacoperon model is probably the most studied and well known. In bacteria, such as E. coli, three
genes are part of an operon that code for three separate enzymes needed for the breakdown of lactose, a
simple sugar. A regulatory gene, located before the operon, continually makes repressor proteins that
bind with the operator and prohibit the function of RNA polymerase. The system therefore remains off
until a flood of lactose molecules binds with all available repressors and prevents their attachment to the
operator. When the operator is free, the production of the enzyme to break down lactose continues until
enough of the lactose molecules are broken down to then release repressors to recombine with the
operator to stop production of the enzymes.
Two additional types of operons exist that operate in the same way except for the function of the operator.
The trpoperon differs because the repressor is active only when bonded to a specific molecule. For the
remainder of the time, it remains unbonded and inactive in the absence of that molecule. Finally, in a
positive twist, activatorsare used by a third type of operon to bond directly with the DNA, which allows the
RNA polymerase to work more efficiently. Absent the activators, RNA polymerase proceeds at a slow
rate.
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