ANTIBIOTICS

An antibiotic is a type of antimicrobial substance active against bacteria and is the most
important type of antibacterial agent for fighting bacterial infections.
Antibiotics either kill or inhibit the growth of bacteria. They do this by killing the bacteria or by
keeping them from copying themselves or reproducing.

A limited number of antibiotics also possess antiprotozoal activity.

Antibiotic medications are widely used in the treatment and prevention of such infections.
Antibiotics are not effective against viruses such as the common cold or influenza. Drugs which
inhibit viruses are termed antiviral drugs or antivirals rather than antibiotics.

The first antibiotic to be invented was penicillin. Penicillin-based antibiotics, such as ampicillin,
amoxicillin, and penicillin G, are still available to treat a variety of infections and have been
around for a long time.

Classes of antibiotics
Antibiotics are commonly classified based on their mechanism of action, chemical structure, or
spectrum of activity.
Most target bacterial functions or growth processes.
Those that target the bacterial cell wall (penicillins and cephalosporins) or
Those that target the cell membrane (polymyxins), or
Those that interfere with essential bacterial enzymes (rifamycins, quinolones, and sulfonamides)
have bactericidal activities.
Protein synthesis inhibitors (macrolides and tetracyclines)
Target specificity
Further categorization is based on their target specificity:
Narrow-spectrum- antibiotics target specific types of bacteria, such as gram-negative or gram-
positive.
Broad-spectrum antibiotics affect a wide range of bacteria.
Following a 40-year break in discovering new classes of antibacterial compounds, four new
classes of antibiotics have been brought into clinical use in the late 2000s and early 2010s:

1
cyclic lipopeptides (suchas daptomycin), glycylcyclines (such
as tigecycline), oxazolidinones (such as linezolid), and lipiarmycins (such as fidaxomicin).
Action specific
Bactericidal- kill susceptible bacteria;
Bacteriostatic-inhibit growth of bacteria, hosts immune responses necessary to eradicate bacteria
E.g Those that target proein synthesis are usually bacteriostatic (with the exception of
bactericidal aminoglycosides).

Action depends on in vitro growth conditons, bacterial density and test duration
Factors that determine the spectrum of antibiotic activity include:
 ability to penetrate the bacterial cell – since most bacterial targets are located in the cell’s
interior
 how widespread the target is among different bacterial species
 bacterial resistance to the antibiotic.

Some infections – such as pneumonia, tuberculosis, blood poisoning, gonorrhoea, and foodborne
diseases – are becoming harder, and sometimes impossible, to treat as pathogens are becoming
resistant to antibiotics thus less effective.
Antibiotic resistance
Antibiotic resistance occurs when bacteria change in response to the use of these antibiotics.
The resistant bacteria cause infections that are harder to treat than those caused by non-resistant
bacteria.
Antibiotics such as penicillin and erythromycin, which used to have a high efficacy against many
bacterial species and strains, have become less effective, due to the increased resistance of many
bacterial strains.
Microbes resistant to multiple antimicrobials are called multidrug resistant (MDR). Those
considered extensively drug resistant (XDR) or totally drug-resistant (TDR) are sometimes
called "superbugs"

Emergence of resistance often reflects evolutionary processes that take place during antibiotic
therapy. The antibiotic treatment may select for bacterial strains with physiologically or

2
genetically enhanced capacity to survive high doses of antibiotics. Under certain conditions, it
may result in preferential growth of resistant bacteria, while growth of susceptible bacteria is
inhibited by the drug.

Resistant microbes are more difficult to treat, requiring alternative medications or higher doses
of antimicrobials. These approaches may be more expensive, more toxic or both.
All classes of microbes can develop resistance. Fungi
develop antifungal resistance. Viruses develop antiviral resistance.

Mechanisms of Antibiotic Resistance

The four main mechanisms by which microorganisms exhibit resistance to antimicrobials are:
1. Drug inactivation or modification:
Alters drug:
Bacteria make an altered 30S ribosomes that does not bind to the drug.
Bacteria make an altered penicillin-binding proteins, that do not bind to the drug.
Bacteria make a form of 50S ribosome that does not binds to the drug.
Bacteria make an altered DNA topoisomerase that does not binds to the drug.
Bacteria make an altered polymerase that does not binds to the drug.
Bacteria make an altered enzyme that does not binds to the drug.
Destroys drug
Plasmid encode enzymes that chemically alter the drug (e.g., by acetylation or phosphorylation),
thereby inactivating it.
Plasmid encode beta-lactamase, which open the beta-lactam ring, inactivating it.
Plasmid encode an enzyme that acetylate the drug, thereby inactivating it.

2. Alteration of target site by:

Bacteria make an altered 30S ribosomes that does not bind to the drug.
Bacteria make an altered penicillin-binding proteins, that do not bind to the drug.
Bacteria make a form of 50S ribosome that does not binds to the drug.
Bacteria make an altered DNA topoisomerase that does not binds to the drug.
Bacteria make an altered polymerase that does not binds to the drug.

3
Bacteria make an altered enzyme that does not binds to the drug

3. Reduced drug accumulation and inhibits drug entry by:

Bacteria change shape of the outer membrane porin proteins, preventing drug from entering cell.
New membrane transport system prevent drug from entering cell.
New membrane transport system pumps drug out of cell.
4. Alteration of metabolic pathway: e.g., some sulfonamide-resistant bacteria do not
require para-aminobenzoic acid (PABA), an important precursor for the synthesis of folic
acid and nucleic acids in bacteria inhibited by sulfonamides. Instead, like mammalian
cells, they turn to utilizing preformed folic acid.

Intrinsic antibacterial resistance may be part of the genetic makeup of bacterial strains. For
example, an antibiotic target may be absent from the bacterial genome.
Intrinsic antibiotic mechanisms are normally chromosome-encoded and include:
1. Non-specific efflux pumps (which likely evolved as a general response to environmental
toxins).
2. Antibiotic inactivating enzymes, or
3. Mechanisms that serve as permeability barriers.

Antimicrobial resistance is something that can develop naturally as an evolutionary response to

continued exposure of antimicrobials.
As explained by Darwin's theory of natural selection, organisms that are able to adapt better to
their environment will be the ones that survive and continue to produce offspring. As a result, the
types of microorganisms that are able to survive overtime with continued attack by certain
antimicrobial agents will naturally become more prevalent in the environment, and
antimicrobials without this resistance will become obsolete.
Antibiotics increase selective pressure in bacterial populations, causing vulnerable bacteria to
die; this increases the percentage of resistant bacteria which continue growing. Even at very low
levels of antibiotic, resistant bacteria can have a growth advantage and grow faster than
vulnerable bacteria.

4
Over time most of the strains of bacteria and infections present will be the type resistant to the
antimicrobial agents being used to treat them, making this agent now ineffective to defeat most
microbes. With the increased use of antimicrobial agents becoming much more common, it is
speeding up this natural process.
Acquired resistance
Molecular mechanisms
Acquired resistance results from a mutation in the bacterial chromosome or in extra-
chromosomal DNA. This often results from an inheritable resistance, or through horizontal gene
transfer.

Several molecular mechanisms of antibacterial resistance exist:

Vertical transmission of mutations:
The spread of antibacterial resistance often occurs through vertical transmission of mutations
during growth.
Vertical gene transfer is the transfer of genetic information, including any genetic mutations,
from a parent to its offspring. Bacteria reproduce by binary fission, where the cell divides into
two identical daughter cells. As in humans, the genetic information in bacteria is encoded in
DNA, which is packed into chromosomes. During binary fission, the chromosomal DNA is
copied, so that each new daughter cell inherits an exact copy of the parent cell’s chromosomes.

Horizontal genetic exchange: Horizontal gene transfer, or horizontal transfer, is the primary
mechanism of spread of antibiotic resistance that allows bacteria to spread antibiotic resistance
genes rapidly between different bacterial types. Horizontal transfer is more likely to happen in
locations of frequent antibiotic use. For instance, antibacterial resistance genes can be exchanged
between different bacterial strains or species via plasmids that carry these resistance genes.
Plasmids that carry several different resistance genes can confer resistance to multiple
antibacterials.

Cross-resistance to several antibacterials may also occur when a resistance mechanism encoded
by a single gene conveys resistance to more than one antibacterial compound. Cross-

5
resistance is the tolerance to a usually toxic substance as a result of exposure to a similarly
acting substance. It is a phenomenon affecting e.g. pesticides and antibiotics.
Every year, nearly half a million new cases of multidrug-resistant tuberculosis (MDR-TB) are
estimated to occur worldwide.

New resistance mechanisms are emerging and spreading globally, threatening our ability to treat
common infectious diseases.
“Superbugs", now contribute to the emergence of diseases that were for a while well controlled.
For example, emergent bacterial strains causing tuberculosis that are resistant to previously
effective antibacterial treatments pose many therapeutic challenges.
CAUSES OF ANTIBIOTIC RESISTANCE
Discovery of antibiotics and their development for treatment of infectious diseases is the biggest
success story in the history of chemotherapy.
However, widespread and indiscriminate use of antibiotics has led to selection of resistant strains
to every antibiotic that has been introduced so far. Antibiotic resistance occurs naturally, but
misuse of antibiotics in humans and animals is accelerating the process.

Rising drug resistance is caused mainly by use of antimicrobials in humans and other animals,
and spread of resistant strains between the two.
Growing resistance has also been linked to dumping of inadequately treated effluents from the
pharmaceutical industry, especially in countries where bulk drugs are manufactured.

With resistance to antibiotics becoming more common there is greater need for alternative
treatments. Calls for new antibiotic therapies have been issued, but new drug development is
becoming rarer.
Where antibiotics can be bought without a prescription, the emergence and spread of resistance
is made worse. In countries without standard treatment guidelines, antibiotics are often over-
prescribed by health workers and veterinarians and over-used by the public.
In summary, the 6 main causes of antibiotic resistance have been linked to:
 Over-prescription of antibiotics

6
  Self medication by consumers; the taking of medicines on one's own initiative or on
another person's suggestion, who is not a certified medical professional.
 Patients not finishing the entire antibiotic course
 Overuse of antibiotics in livestock and fish farming
 Poor infection control in health care settings
 Poor hygiene and sanitation
 Absence of new antibiotics being discovered
PREVENTION AND CONTROL
Preventive measures include only using antibiotics when needed, thereby stopping misuse of
antibiotics or antimicrobials. Behaviour changes must also include actions to reduce the spread
of infections through vaccination, hand washing, practising safer sex, and good food hygiene.
One strategy to address bacterial drug resistance is the discovery and application of compounds
that modify resistance to common antibacterials. Resistance modifying agents are capable of
partly or completely suppressing bacterial resistance mechanisms. For example, some resistance-
modifying agents may inhibit multidrug resistance mechanisms, such as drug efflux from the
cell, thus increasing the susceptibility of bacteria to an antibacterial. Targets include:
 The efflux inhibitor Phe-Arg-β-naphthylamide.
 Beta-lactamase inhibitors, such as clavulanic acid and sulbactam.
Metabolic stimuli such as sugar can help eradicate a certain type of antibiotic-tolerant bacteria by
keeping their metabolism active.

Narrow-spectrum antibiotics are preferred over broad-spectrum antibiotics when possible, as

effectively and accurately targeting specific organisms is less likely to cause resistance, as well
as side effects.
For people who take these medications at home, education about proper use is essential. Health
care providers can minimize spread of resistant infections by use of
proper sanitation and hygiene, including handwashing and disinfecting between patients, and
should encourage the same of the patient, visitors, and family members.

7
MONOSACCHARIDE STRUCTURE
All monosaccharides have the same general formula of (CH2O)n, which designates a central
carbon molecule bonded to two hydrogens and one oxygen. The oxygen will also bond to a
hydrogen, creating a hydroxyl group.
The chemical formula that most monosaccharides have is Cx(H2O)y, where generally x≥ 3.
The molecule is always formed by three elements and three elements only:
Carbon (C), Hydrogen (H) and Oxygen (O).
The molecule of monosaccharides is very small and compact in size. This is another reason we call
monosaccharides simple sugars.
Because carbon can form 4 bonds, several of these carbon molecules can bond together. One of
the carbons in the chain will form a double bond with an oxygen, which is called a carboxyl
group.
A Glucose is one of the most common monosaccharides in nature, used by nearly every form of
life. This simple monosaccharide is composed of 6 carbons. All monosaccharides have the same
general formula of (CH2O)n, which designates a central carbon molecule bonded to two
hydrogens and one oxygen. The first carbon is the carboxyl group. The oxygen will also bond to
a hydrogen, creating a hydroxyl group.
If this carboxyl occurs at the end of the chain, the monosaccharide is in the aldose family. If
the carboxyl group is in the middle of the chain, the monosaccharide is in the ketose family.
Typically, monosaccharides with more than 5 carbons exist as rings in solutions of water. The
hydroxyl group on the fifth carbon will react with the first carbon.
The hydroxyl group gives up its hydrogen atom when it forms a bond with the first carbon. The
double bonded oxygen on the first carbon bonds with a new hydrogen when the second bond
with the carbon is broken. This forms a fully connected and stable ring of carbons.

AMINO ACID STRUCTURE

 Each amino acid contains a central C atom, an amino group (NH2), a carboxyl group
(COOH), and a specific R group.
 The R group determines the characteristics (size, polarity, and pH) for each type of amino
acid.

8
  Peptide bonds form between the carboxyl group of one amino acid and the amino group of
another through dehydration synthesis.
 A chain of amino acids is a polypeptide.
Amino acids are the monomers that make up proteins. Each amino acid has the same
fundamental structure , which consists of a central carbon atom, also known as the alpha (α)
carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. In
the aqueous environment of the cell, the both the amino group and the carboxyl group are
ionized under physiological conditions, and so have the structures -NH 3+ and -COO–,
respectively. Every amino acid also has another atom or group of atoms bonded to the central
atom known as the R group. This R group, or side chain, gives each amino acid proteins specific
characteristics, including size, polarity, and Ph.
Amino acid structure
Amino acids have a central asymmetric carbon to which an amino group, a carboxyl group, a
hydrogen atom, and a side chain (R group) are attached. This amino acid is unionized, but if it
were placed in water at pH 7, its amino group would pick up another hydrogen and a positive
charge, and the hydroxyl in its carboxyl group would lose and a hydrogen and gain a negative
charge.

Types of Amino Acids

The name “amino acid” is derived from the amino group and carboxyl-acid-group in their basic
structure. There are 21 amino acids present in proteins, each with a specific R group or side
chain. Ten of these are considered essential amino acids in humans because the human body

9
cannot produce them and they must be obtained from the diet. All organisms have different
essential amino acids based on their physiology.
Peptide Bonds
The sequence and the number of amino acids ultimately determine the protein’s shape, size, and
function. Each amino acid is attached to another amino acid by a covalent bond, known as a
peptide bond. When two amino acids are covalently attached by a peptide bond, the carboxyl
group of one amino acid and the amino group of the incoming amino acid combine and release a
molecule of water. Any reaction that combines two monomers in a reaction that generates H 2O
as one of the products is known as a dehydration reaction, so peptide bond formation is an
example of a dehydration reaction
Polypeptide Chains
The resulting chain of amino acids is called a polypeptide chain. Each polypeptide has a free
amino group at one end. This end is called the N terminal, or the amino terminal, and the other
end has a free carboxyl group, also known as the C or carboxyl terminal. When reading or
reporting the amino acid sequence of a protein or polypeptide, the convention is to use the N-to-
C direction. That is, the first amino acid in the sequence is assumed to the be one at the N
terminal and the last amino acid is assumed to be the one at the C terminal.
DNA MOLECULE STRUCTURE
DNA is made up of molecules called nucleotides.
Each nucleotide contains a phosphate group, a sugar group and a nitrogen base.
The four types of nitrogen bases are adenine (A), thymine (T), guanine (G) and cytosine (C).
The order of these bases is what determines DNA's instructions, or genetic code.
Nucleotides are attached together to form two long strands that spiral to create a structure called
a double helix. If you think of the double helix structure as a ladder, the phosphate and sugar
molecules would be the sides, while the bases would be the rungs. The bases on one strand pair
with the bases on another strand: adenine pairs with thymine, and guanine pairs with cytosine.
Watson and Crick proposed that DNA is made up of two strands that are twisted around each
other to form a right-handed helix. The two DNA strands are antiparallel, such that the 3ʹ end of
one strand faces the 5ʹ end of the other (Figure 6). The 3ʹ end of each strand has a free hydroxyl
group, while the 5ʹ end of each strand has a free phosphate group. The sugar and phosphate of
the polymerized nucleotides form the backbone of the structure, whereas the nitrogenous bases

10
are stacked inside. These nitrogenous bases on the interior of the molecule interact with each
other, base pairing.

DNA
DNA molecules contain the genetic information and RNA molecules convert this genetic
information into amino acid sequences. The basic unit is called a nucleotide, which is composed
of a sugar-phosphate backbone attached to one of four nitrogenous bases; cytosine, guanine,
adenine or thymine.

Basic Features of DNA

1. DNA molecule is double stranded, containing two polynucleotide strands wound around each
other.
1. .The two strands are anti-parallel: that is, one strand runs 5' to 3' while the other runs 3' to 5.
2. It has complementary base-pairing of its four nucleotides.
3. The backbone of each consists of altering deoxyribose and phosphate groups.
4. The double helix makes a complete turn in just over 10 nucleotide base pairs, so each turn
takes a little more than the 34.
5. The diameter of the helix is 20 angstrom.

DNA molecule consists of two long polynucleotide chains composed of four types
of nucleotide subunits.
Each of these chains is known as a DNA chain, or a DNA strand. Hydrogen bonds between
the base portions of the nucleotides hold the two chains together.

The nucleotides are covalently linked together in a chain through the sugars and phosphates,
which thus form a “backbone” of alternating sugar-phosphate-sugar-phosphate.
C joins to G, and G to C by three hydrogen bonds, indicated by the dotted lines. A joins to T and
T to A by two hydrogen bonds.

The way in which the nucleotide subunits are lined together gives a DNA strand a chemical
polarity.

11
If we think of each sugar as a block with a protruding knob (the 5′ phosphate) on one side and a
hole (the 3′ hydroxyl) on the other.
Each completed chain, formed by interlocking knobs with holes, will have all of its subunits
lined up in the same orientation. Moreover, the two ends of the chain will be easily
distinguishable, as one has a hole (the 3′ hydroxyl) and the other a knob (the 5′ phosphate) at its
terminus.
This polarity in a DNA chain is indicated by referring to one end as the 3′ end and the other as
the 5′ end.
The three-dimensional structure of DNA—the double helix—arises from the chemical and
structural features of its two polynucleotide chains. Because these two chains are held together
by hydrogen bonding between the bases on the different strands, all the bases are on the inside of
the double helix, and the sugar-phosphate backbones are on the outside In each case, a bulkier
two-ring base (a purine) is paired with a single-ring base (a pyrimidine); A always pairs with T,
and G with C.

Nucleotides are composed of a five-carbon sugar to which are attached one or more phosphate
groups and a nitrogen-containing base. In the case of the nucleotides in DNA, the sugar is
deoxyribose attached to a single phosphate group (hence the name deoxyribonucleic acid), and
the base may be either adenine (A), cytosine (C), guanine (G), or thymine (T).
COMPLEMENTARY BASE PAIRING
Base pairing takes place between a purine and pyrimidine. In DNA, adenine (A) and thymine (T)
are complementary base pairs, and cytosine (C) and guanine (G) are also complementary base
pairs, explaining Chargaff’s rules.
The base pairs are stabilized by hydrogen bonds; adenine and thymine form two hydrogen bonds
between them, whereas cytosine and guanine form three hydrogen bonds between them.
This complementary base-pairing enables the base pairs to be packed in the energetically most
favorable arrangement in the interior of the double helix. In this arrangement, each base pair is of
similar width, thus holding the sugar-phosphate backbones an equal distance apart along the
DNA molecule. To maximize the efficiency of base-pair packing, the two sugar-phosphate
backbones wind around each other to form a double helix, with one complete turn every ten base
pairs.

12
Because only the base differs in each of the four types of subunits, each polynucleotide chain in
DNA is analogous to a necklace (the backbone) strung with four types of beads (the four bases
A, C, G, and T).
The symbols (A, C, G, and T) are also commonly used to denote the four different nucleotides—
that is, the bases with their attached sugar and phosphate groups.

The bases carry biological information that must be copied accurately for transmission to the
next generation each time a cell divides to form two daughter cells.

13
DNA encodes information through the order, or sequence, of the nucleotides along each strand.
Each base—A, C, T, or G—can be considered as a letter in a four-letter alphabet that spells out
biological messages in the chemical structure of the DNA.

The complete set of information in an organism's DNA is called its genome, and it carries the
information for all the proteins the organism will ever synthesize. The term genome is also used
to describe the DNA that carries this information. The amount of information contained in
genomes is staggering: for example, a typical human cell contains 2 meters of DNA. Written out
in the four-letter nucleotide alphabet, the nucleotide sequence of a very small
human gene occupies a quarter of a page of text.
The complete sequence of nucleotides in the human genome would fill more than a thousand
books the size of this one. In addition to other critical information, it carries the instructions for
about 30,000 distinct proteins.

RNA
Ribonucleic acid (RNA) is typically single stranded and contains ribose as its pentose sugar and
the pyrimidine uracil instead of thymine.
RNA is typically single stranded and is made of ribonucleotides that are linked by
phosphodiester bonds.
A ribonucleotide in the RNA chain contains ribose (the pentose sugar), one of the four
nitrogenous bases (A, U, G, and C), and a phosphate group.
The subtle structural difference between the sugars gives DNA added stability, making DNA
more suitable for storage of genetic information, whereas the relative instability of RNA makes it
more suitable for its more short-term functions.

The RNA-specific pyrimidine uracil forms a complementary base pair with adenine and is used
instead of the thymine used in DNA. Even though RNA is single stranded, most types of RNA
molecules show extensive intramolecular base pairing between complementary sequences within
the RNA strand, creating a predictable three-dimensional structure essential for their function

14
Ribonucleotides contain the pentose sugar ribose instead of the deoxyribose found in
deoxyribonucleotides. (b) RNA contains the pyrimidine uracil in place of thymine found in
DNA.
There are three main types of RNA, all involved in protein synthesis.
 Messenger RNA (mRNA) serves as the intermediary between DNA and the synthesis of
protein products during translation.
 Ribosomal RNA (rRNA) is a type of stable RNA that is a major constituent of ribosomes.
It ensures the proper alignment of the mRNA and the ribosomes during protein synthesis
and catalyzes the formation of the peptide bonds between two aligned amino acids during
protein synthesis.
 Transfer RNA (tRNA) is a small type of stable RNA that carries an amino acid to the
corresponding site of protein synthesis in the ribosome. It is the base pairing between the
tRNA and mRNA that allows for the correct amino acid to be inserted in the polypeptide
chain being synthesized.

Functions of RNA in Protein Synthesis

Cells access the information stored in DNA by creating RNA to direct the synthesis of proteins
through the process of translation. Proteins within a cell have many functions, including
building cellular structures and serving as enzyme catalysts for cellular chemical reactions that
give cells their specific characteristics. The three main types of RNA directly involved in protein
synthesis are messenger RNA (mRNA), ribosomal RNA (rRNA), and transfer RNA (tRNA).
In 1961, French scientists François Jacob and Jacques Monod hypothesized the existence of an
intermediary between DNA and its protein products, which they called messenger RNA.
[1]
Evidence supporting their hypothesis was gathered soon afterwards showing that information
from DNA is transmitted to the ribosome for protein synthesis using mRNA. If DNA serves as
the complete library of cellular information, mRNA serves as a photocopy of specific
information needed at a particular point in time that serves as the instructions to make a protein.
The mRNA carries the message from the DNA, which controls all of the cellular activities in a
cell. If a cell requires a certain protein to be synthesized, the gene for this product is “turned on”
and the mRNA is synthesized through the process of transcription.

15
The mRNA then interacts with ribosomes and other cellular machinery to direct the synthesis of
the protein it encodes during the process of translation.
mRNA is relatively unstable and short-lived in the cell, especially in prokaryotic cells, ensuring
that proteins are only made when needed.

rRNA and tRNA are stable types of RNA.

In prokaryotes and eukaryotes, tRNA and rRNA are encoded in the DNA, then copied into long
RNA molecules that are cut to release smaller fragments containing the individual mature RNA
species.
rRNA
In eukaryotes, synthesis, cutting, and assembly of rRNA into ribosomes takes place in the
nucleolus region of the nucleus, but these activities occur in the cytoplasm of prokaryotes.
Neither of these types of RNA carries instructions to direct the synthesis of a polypeptide, but
they play other important roles in protein synthesis.
rRNA is a major constituent of ribosomes, composing up to about 60% of the ribosome by mass
and providing the location where the mRNA binds. Ribosomes are composed of rRNA and
protein.
rRNA ensures the proper alignment of the mRNA, tRNA, and the ribosomes.
The rRNA also has an enzymatic activity (peptidyl transferase) and catalyzes the formation of
the peptide bonds between two aligned amino acids during protein synthesis.

Transfer RNA carries the correct amino acid to the site of protein synthesis in the ribosome. It is
the base pairing between the tRNA and mRNA that allows for the correct amino acid to be
inserted in the polypeptide chain being synthesized.
Any mutations in the tRNA or rRNA can result in global problems for the cell because both are
necessary for proper protein synthesis.

16