Cell Biology

Achievement Standard 2.8 90464

Cells
All living things are made up of 1 or more
cells Cells vary in shape but they are always small Small size is due to difficulty in diffusing substances Cells can be divided into 2 types:
Prokaryotes Eukaryotes

Cell Organelles
There are some organelles in cells that are present in both plant
and animal cells, and others that are present only in one or the other
Cell wall (plant only) Cell membrane Cytoplasm Nuclear membrane Nucleus Chromosomes Mitochondria Chloroplast (plant only) Centriole Vacuole Ribosome Endoplasmic reticulum (smooth and rough) Lysosome Golgi body

Cytoplasm: The nucleus controls cell metabolism; the many chemical reactions that keep the cell alive and performing its designated role.

Nucleus

Nucleus contains inherited information: The total collection of genes located on chromosomes in the nucleus has the complete instructions for constructing a total organism.

Structure of the nucleus

Nuclear membrane encloses the nucleus in eukaryotic cells Chromosomes are made up of DNA and protein and store the information for controlling the cell Nuclear pores are involved in the active transport of substances into and out of the nucleus Nucleolus is involved in the construction of ribosomes

Eukaryotes have two types of organelles with their own DNA: mitochondria chloroplasts The DNA of these organelles is replicated when the organelles are reproduced (independently of the DNA in the nucleus).

Mitochondrial DNA

Mitochondrion
Ribosome

Chloroplast
Chloroplast DNA

Unicellular Organisms
Unicellular organisms carryout all their life functions inside a
single cell.
While some of their organelles are the same as that of eukaryotes there are some that are found only in unicellular organisms. These are:
Oral Groove Ciliated channel on one side of the cell where food particles are taken in Anal Pore Specialised region of the cell surface where food vacuoles attach an rupture to the outside Eyespots Is used in light detection and phototaxic responses Contractile Vacuoles used to regulate the amount of water inside the organism by expelling it to the outside Food Vacuole space that contained ingested food particles Pseudopodia false legs to aid in ingestion of food particles

Unicellular Organisms cont..

As well as having specialised organelles, some of the cellular
processes are significantly different to those of multicellular organisms.
Gas Exchange This is usually by diffusion across the cell membrane. To increase efficiency, the organism is usually long and/or flat in shape increasing the surface area to volume ratio. Ingestion and Feeding All unicellular organisms that cannot photosynthesise must ingest small food particles as their food supply. Food particles cross the membrane by phagocytosis to form a food vacuole which is digested. Any indigestible material left in the food vacuole is discharged to the outside through the anal pore. Some unicellular organisms do not have an oral groove so they use pseudopodia to engulf the food particles. Excretion In unicellular organisms, the main waste product formed is ammonia. This is very toxic so it must be diluted by large volumes of water before being excreted. Contractile vacuoles aid in the collection and removal of wastes.

Unicellular Organisms cont..

Water regulation Since many unicellular organisms live in fresh water and are enclosed by semi-permeable membranes water is constantly moving into them. Contractile vacuoles work to collect and remove the water to ensure the cell does not burst. Locomotion For some unicellular organisms locomotion is achieved by the coordinated beating of cilia, others use flagella and Amoeba use the pseudopodia to move. Responses to External Stimuli Most movement is a response to changes in the protoplasmic contents of the organism. Some organisms have eyespots that detect the amount of visible light and trigger a phototaxic response. Reproduction This can be asexual via binary fission or, vary rarely, sexually through the exchange of genetic material

Bacteria have no membrane-bound organelles. Cellular reactions occur on the inner surface of the cell membrane or in the cytoplasm. Bacterial DNA is found in: One, large circular chromosome.
Flagellum

Several small chromosomal

structures called plasmids.

Cytoplasm (no nucleus)

Single, circular chromosome

Ribosomes Cell membrane Cell wall Plasmids

Cell Processes

Cell Membrane
Surrounds the cell and keeps it separate from the outside

medium Semi-permeable membrane that controls what goes in and out In animal cells, it is the outside layer but in plants the cell wall surrounds it
Protein

Fatty acid tails

Pore

Glycerol-phosphate heads

Membrane is called a lipid bi-layer consisting of two

hydrophillic heads on the outside and hydrophobic tails on the inside The general structure is based on the fluid mosaic model.

Cell Transport
Materials such as ions, water, molecules and
nutrients are transported within cells and in and out of cells by processes which are either passive or active.
Diffusion Through Bi-layer
Facilitated diffusion

Passive Transport
This does not require energy It can be separated into 2 types:
Diffusion Osmosis

Diffusion
The net movement of particles from an area of high
concentration to an area of low conentration.

Difference between the two areas is the concentration

gradient A large difference=large gradient=faster diffusion The rate of diffusion varies depending on:
Size of molecules Temperature of substance State of matter Concentration of chemicals

The cell membrane may contain proteins that help

facilitate diffusion

Osmosis
The net movement of water from a high
http://www.tvdsb.on.ca/WESTMIN/science/sbi3a1/cells/Osmosis.htm

concentration to a low concentration through a semipermeable membrane

Solution with not much water: hypertonic Solution with lots of water: hypotonic Solution with the same water concentration: isotonic

Active Transport
Movement against a concentration
gradient, ie from a low concentration to a high concentration It requires energy so:
Heat is given off Oxygen is used up CO2 produced Glucose used up Endocytosis Exocytosis

Two main types:

Endocytosis
Taking particles into a cell. Engulfing a liquid = pinocytosis Engulfing a solid = phagocytosis

Exocytosis
Occurs when vacuoles expel their contents
to the outside

Amino Acids

Amino acids are linked together to form proteins.

All amino acids have the same general structure, but each type differs from the others by having a unique R group. The R group is the variable part of the amino acid. 20 different amino acids are commonly found in proteins.
The 'R' group varies in chemical make-up with each type of amino acid Carbon atom Amine group Hydrogen atom Carboxyl group makes the molecule behave like a weak acid Example of an amino acid shown as a space filling model: Cysteine

Symbolic formula

Types of Amino Acid

Amino acids with different types of R groups have different chemical properties:
Forms di-sulfide bridges that can link to similar amino acids Basic Acidic

Cysteine
(forms di-sulfide bridges)

Lysine
(basic)

Aspartic acid
(acidic)

Polypeptide Chains
Amino acids are liked together in long chains by the formation of peptide bonds. Long chains of such amino acids are called polypeptide chains.
Polypeptide chain

Peptide bond

Peptide bond

Peptide bond

Peptide bond

Peptide bond

Peptide bond

Protein Function
Proteins can be classified according to their functional Hemoglobin role in an organism:
Function Structural Examples Collagen, keratin Insulin, glucagon, adrenalin, human growth hormone, follicle stimulating hormone Myosin, actin antibodies such as Gammaglobulin Hemoglobin, myoglobin amylase, lipase, lactase, trypsin

Forming the structural components of organs

Regulating cellular function (hormones) Forming the contractile elements in muscles Functioning to combat invading microbes Acting as carrier molecules Catalyzing metabolic reactions (enzymes)

Regulatory Contractile Immunological Transport Catalytic

Protein Structure
The production of a functional protein requires that the polypeptide chain assumes a precise structure comprising several levels:

Amino acid

Primary structure: The sequence of amino acids in a polypeptide chain. Secondary structure: The shape of the polypeptide chain (e.g. alphahelix).

Tertiary structure: The overall conformation (shape) of the polypeptide caused by folding.
Quaternary structure: In some proteins, an additional level of organization groups separate polypeptide chains together to form a functional protein.

Di-sulfide bridge

Alpha chain

Beta chain

Beta chain

Alpha chain Hemoglobin molecule

Enzymes
Enzymes are biological catalysts, regulating cell

metabolism. An enzyme acts on a molecule called the substrate. Enzymes are specific for the reactions they catalyze. Enzyme activity depends on the enzymes shape and its active site (the binding site for the substrate). Enzymes are often named for the substrate on which they work, and sometimes include the suffix -ase:
Lipase breaks down fats (lipids) Amylase breaks down starch (amylose/amylopectin) Lactase breaks down milk sugar (lactose) Cholinesterase breaks down the neurotransmitter acetylcholine in the nervous system

Enzyme Structure
Ribonuclease S (right) is an enzyme that breaks up RNA molecules. The red areas designate the active site and comprise certain amino acid 'R' groups. The substrate (in this case, RNA) is drawn into the active site, putting the substrate molecule under stress, thereby causing the reaction to proceed more readily.

The substrate is the chemical that an enzyme acts on

RNA

Active sites are attraction points that draw the substrate to the surface of the enzyme

Enzymes are specific catalysts. The complexity of the active site makes each enzyme specific for the substrate it acts on.

 Ribonuclease S (right) is an enzyme

Functional Enzyme

Protein-only Enzymes that breaks up RNA molecules. The red areas designate the active site Active site Enzyme comprising and comprise certain amino acid 'R' only protein groups. e.g. lysozyme The substrate (in this case, RNA) is Enzyme drawn into the active site, putting the substrate molecule under stress, thereby causing the reaction to proceed more readily. Conjugated Protein Enzymes Nearly all enzymes are made of protein, although RNA can also have enzymic Prosthetic group Coenzyme properties. Some enzymes contain only protein. Others, called conjugated protein enzymes, require additional components to complete their catalytic properties.

These may be permanently attached parts called prosthetic groups, or temporarily attached non-protein coenzymes, which detach after a reaction and may then participate with another enzyme in other reactions.

Apoenzyme Apoenzyme Prosthetic group is required for function Coenzyme is required for function

Conjugated Protein Enzymes

The prosthetic group remains more or less permanently attached Active site The coenzyme becomes detached from the apoenzyme after the reaction and may go on participate in further reactions Active site

Apoenzyme alone is inactive

Apoenzyme

Prosthetic group required Contains the apoenzyme (protein) plus a prosthetic group e.g. Flavoprotein + FAD

Coenzyme required Contains the apoenzyme (protein) plus a coenzyme (non-protein) e.g. Dehydrogenases + NAD

Mechanism of Enzyme Action

Steps in Enzyme Activity

The specificity of

the substrate is determined by the complexity of the binding sites. The wrong substrates will not fit into the active site. Some enzymes have specificity to a bond type (e.g. lipases break up any chain length of lipid).

In the induced fit model of enzyme function, the enzyme fits to its substrate somewhat like a lock and key, with the shape of the enzyme changing when the substrate fits into the cleft of the active site. Substrate molecules Two substrate molecules

are drawn into the cleft of the enzymes active site

Enzyme

The shape of the enzymes active site is modified by its interaction with the substrate(s). The shape changes force the substrate molecules to combine. The resulting end product is released by the enzyme, which returns to its normal shape, ready to receive more substrate.

Cleft Enzyme changes shape

Enzyme

Enzyme

End product is released

Enzymes are Catalysts

Catalysts are substances that
Amount of energy stored in the chemicals

increase the rate of chemical reactions. All catalysts speed up reactions by:
Influencing the stability of bonds in the reactants. Providing an alternative reaction pathway; the binding of reactants and enzyme can weaken bonds in the reactants and allow the reaction to proceed more easily.

High
Without enzyme With enzyme

Reactant

High energy

Enzymes are biological

Product

catalysts; they alter the chemical equilibrium between the reactant and the product. When the substrate attains the required energy it is able to change into the product or products.

Low energy
Low Start Direction of reaction Finish

Enzymes are Catalysts

Catalysts provide an alternative pathway of lower activation energy.
Without enzyme present, the energy needed to make the reaction proceed in the forward direction (the activation energy) is very high.

Amount of energy stored in the chemicals

High With enzyme present, the energy required for the reaction to proceed is reduced (the activation energy is lower). Reactants turn into products more readily. Product

Reactant

High energy

Low energy
Low Start Direction of reaction Finish

Effects of pH on Enzymes
Like all proteins,
enzymes are denatured (made non-functional) by extremes of pH (acid/alkaline). Within these extremes most enzymes are still influenced by pH. There is a particular pH for optimum activity for each enzyme. This is because the active sites of the enzyme can be disabled by the wrong pH.
Optimum pH for pepsin Optimum pH Optimum pH for urease for trypsin Trypsin Pepsin

Enzyme activity

Urease

Acid

pH

Alkaline

Temperature and Enzyme Activity

Reactions occur faster at
higher temperatures, but the rate of denaturation of enzymes also increases at higher temperatures. High temperatures break the disulfide bonds important for the tertiary structure of the enzyme. This destroys the active sites and therefore makes the enzyme nonfunctional.
Optimum temperature for enzyme

Enzyme activity

Too cold for the enzyme to operate

Rapid denaturation

Temperature (C)

Enzyme Concentration And Enzyme Activity

Assuming that the
amount of substrate is not limiting, an increase in enzyme concentration causes an increase in the reaction rate. Cells may increase the amount of enzyme present by increasing the rate of its synthesis to meet demand.

Rate of reaction

With ample substrate and cofactors present

Enzyme concentration

Substrate Concentration Effect on Enzyme Activity

Assuming that the amount
of enzyme is constant and non-limiting, an increase in substrate concentration causes a diminishing increase in the reaction rate. A maximum rate is obtained at a certain substrate concentration where all enzymes are occupied by substrate. The reaction rate cannot increase further.

Rate of reaction

With ample enzyme and cofactors present

Substrate concentration

 Cofactors are substances that

Effect of Cofactors on Enzymes

are essential to the catalytic activity of some enzymes. Cofactors may alter the shape of enzymes slightly to make the active sites functional or to complete the reactive site. Enzyme cofactors can be inorganic, e.g. metal ions and iron-sulfur clusters, or organic compounds, which are known as coenzymes. Many vitamins are coenzymes. Vitamins are organic molecules not synthesized by the body, e.g. vitamin K, B1, B6, and folate.
Enzyme
Once the shape of the enzyme has been modified by the cofactor, substrates A and B can react together.

The presence of the cofactor alters the shape of the enzyme

Product

 Enzyme inhibitors are

Enzyme Inhibition
substances that prevent the normal action of an enzyme and thereby slow the rate of enzyme controlled reactions. Enzyme inhibitors may or may not act reversibly. In reversible inhibition, the inhibitor is temporarily bound to the enzyme, thereby preventing its function.
Reversible inhibition is often a means by which enzyme activity is regulated in the functioning cell.

Insecticides and heavy metals, such as mercury, are poisons that inhibit enzyme activity.

In irreversible inhibition,

the inhibitor (poison) may bind permanently to the enzyme and cause it to be permanently deactivated.

Reversible Inhibition
Reversible inhibitors are used to
control the activity of enzymes. There is often an interaction between the substrate or end product and the enzyme controlling the reaction. Buildup of the end product or a lack of substrate may deactivate the enzyme. This deactivation can occur via competitive or noncompetitive inhibition.

Competitive inhibitors compete with the substrate for the active site. Noncompetitive inhibitors bind to the enzyme, but not at the active site. The substrate can bind but enzyme function is impaired. Allosteric inhibitors are non competitive inhibitors that prevent the substrate from binding.

Model of elastase and its inhibitor

Competitive Inhibition
Competitive inhibitors
compete with the substrate for the active site, thereby blocking it and preventing its attachment to the substrate. The inhibition is reversible.
Example: Malonate is a powerful inhibitor of cellular respiration because it is a competitive inhibitor of the enzyme succinate dehydrogenase in the Krebs cycle, which catalyzes the oxidation of succinate to fumarate.
Substrate

No inhibition
Enzyme

Good fit

Competitive inhibitor blocks the active site Substrate

Enzyme

Competitive inhibitor e.g. malonate

Non-Competitive Inhibition
Non-competitive
No inhibition
Substrate Good fit

inhibitors bind to the enzyme, but not at the active site, and alter its shape. The substrate is still able to bind, but the reaction rate is slowed because the enzyme is less able to perform its function. Allosteric enzyme inhibitors are non competitive inhibitors that induce a shape change that alters the active site and prevents the substrate from binding.
In this case, the enzyme ceases to function.
Allosteric inhibitor

Enzyme

Non-competitive The substrate binds to the active site inhibitor

The substrate cannot bind Active site is distorted

Enzyme

Enzyme

Non-competitive inhibitor

The inhibitor binds to the enzyme, and alters the enzymes ability to function properly.

 Irreversible enzyme inhibitors are

Irreversible Inhibition
Substrate

poisons that prevent enzyme function. Heavy metals: Certain heavy metals bind tightly and permanently to the active sites of enzymes, destroying their catalytic properties.
Example: mercury (Hg), cadmium (Cd), lead (Pb), and arsenic (As). They are generally non-competitive inhibitors, although an exception is mercury which deactivates the enzyme papain. Heavy metals are retained in the body, and lost slowly.

The inhibitor blocks the active site

The substrate cannot bind to the active site Active site

Insecticides

Papain enzyme

These can prevent the breakdown of acetylcholine (ACh), a neurotransmitter in the nervous system. They bind to the enzyme that normally breaks down the ACh, causing over stimulation of the nerves.

Energy in Cells
Every living cell needs a regular supply of energy to

power chemical processes Sources of energy are large complex molecules which make up food supply Energy is released when the bonds holding atoms together are released, usually as heat Energy is used to form adenosine-tri-phosphate (ATP) from adenosine-di-phosphate (ADP)
ADP =
Adenosine Adenosine P P P P P

Photosynthesis captures light energy and stores is in

food glucose Respiration releases energy from glucose Energy is stored at ATP until it is needed

ATP =

Respiration
Respiration is a process which makes ATP using energy in organic
molecules such as glucose glycolysis, Krebs cycle and oxidative phosphorylation (electron transport chain).

If glucose is placed in oxygen and set alight, it burns and releases a lot of

heat energy as the glucose molecules combine with oxygen to form carbon dioxide and water and the energy from glucose is rapidly transferred to heat energy. This is an oxidation reaction. You will recognise the equation: Glucose C6H12O6

In a living cell, a similar process takes place, but in a more controlled way.
+ oxygen energy + carbon dioxide + water + O2 energy + CO2 + H2 O

This actually happens in a series of reactions controlled by enzymes and the

energy in glucose is released in small stages. A sequence of reactions (like in the process of respiration) is called a metabolic pathway.

Glycolysis
pyruvate

glucose converted to

Occurs in the cytoplasm of the cell Glucose (a 6 carbon compound) is

converted into two pyruvate (pyruvic acid) molecules (a 3 carbon compound) Small amount of ATP (adenosine triphosphate) is made in this process (2 ATP)

Kreb Cycle pyruvate fed into cycle

Occurs in the matrix of the mitochondria If oxygen is available, pyruvate (pyruvic acid) formed
in glycolysis passes into a mitochondrion through the outer and inner membranes Link step to convert the pyruvate into a different molecule which then undergoes a cycle of reactions Carbon dioxide removed (called decarboxylation) and diffuses out of the mitochondrion, out of the cell and out of organism 2 ATP molecules produced Hydrogen ions (H+ ions) and electrons are also produced in Krebs cycle to be fed into the electron transport chain to make more ATP

of reactions

Oxidative Phosphorylation

(electron transport chain) - electrons produced

passed along an electron transport chain to produce ATP

This happens in the inner membrane of the mitochondrion ATP is made by the addition of inorganic phosphate Pi to ADP.

This is called a phosphorylation reaction. In respiration, this process needs oxygen so it is known as oxidative phosphorylation. The enzyme ATP synthase makes the ATP from ADP + Pi H+ ions and electrons pass through a series of reactions and energy is released as ATP. At the end of this electron transport chain, oxygen is needed. Oxygen at the end of the electron transport chain combines with electrons and hydrogen ions to form water. A lot of ATP is made in this part of respiration (34ATP molecules)

Anaerobic Respiration
When oxygen is not available, only glycolysis can occur. Therefore, a small
amount of ATP is made (2 ATP) along with pyruvate Pyruvate will inhibit glycolysis so it is converted to something else. SOLUTIONS to remove the pyruvate
ALCOHOLIC FERMENTATION Used by fungi & plants Yeast converts pyruvate to ethanol Glucose pyruvate ethanol + CO2 +2 ATP If yeast is supplied with a supply of carbohydrate, it will carry out glycolysis and alcoholic fermentation. LACTIC FERMENTATION Used by animals Pyruvate is converted to lactic acid Glucose pyruvate lactic acid +2 ATP Lactic acid build up in muscles causes the pain in exhausted muscles. The lactic acid is transported in the blood to the liver and here it is converted back to pyruvic acid and then to glucose during recovery.

The ethanol is used to make alcoholic drinks. In baking, the CO 2 is used to make bread, etc. rise This requires oxygen, which is why you continue breathing deeply after you stop exercising. You are supplying extra oxygen to the liver to deal with the lactic acid produced because of a shortage of oxygen earlier on. You are paying off an oxygen debt

Summary of Respiration

Photosynthesis
Inputs CO2, H2O, light
CO2 is absorbed from air as gas Water absorbed from environment Light red and green light most photosynthetically active C6H12O6 glucose temporarily stored as starch in leaves to be used in
respiration O2 is essentially a waste product that diffuses out

Outputs C6H12O6, O2

6CO2 + 6H2O C6H12O6 + 6O2 Occurs in all green plants Requires sunlight so leaves broad, thin and flat but

also prone to water loss Water loss decreased by waterproof cuticle which is a waxy layer on leaf Stomata present to allow CO2 in and stop water loss

Photosynthesis
Transfer of light energy into chemical potential
energy Occurs in the grana of chloroplasts Relied on by all organisms Occurs in 2 stages

The light phase Dark phase/Light independent phase (Calvin cycle)

Chlorophyll plays vital role in trapping light

energy

Light Phase
Light Energy Chlorophyll
ADP + P

ATP
Carries Energy

12H2O

12H2

6CO2

(Given off)

To dark phase

Light Independent Phase

6CO2 + 12H2 C6H12O6 + 6H2O

Chromosomes
A: Light microscope view of a chromosome from the salivary glands of the fly Simulium.

Banding: groups of genes stained

light and dark. Puffing: areas of transcription (mRNA production).

B: Scanning electron microscope (SEM) view of sex chromosomes in the condensed state during a cell division. Individual chromatin fibers are visible.

The smaller chromosome is the Y

while the larger one is the X.

C: Transmission electron microscope (TEM) view of chromosomes lined up at the equator of a cell during the process of cell division. These chromosomes are also in the condensed state.

Chromosome States
Interphase: Chromosomes are single-armed
structures during their unwound state during interphase. Dividing cells: Chromosomes are double-armed structures, having replicated their DNA to form two chromatids in preparation for cell division.
Replicated chromosome
prepared for cell division

Interphase chromosome

Chromatin

Centromere
This chromosome would not be visible as a coiled up structure, but unwound as a region of dense chromatin in the nucleus (as in the TEM of the nucleus above)

Chromatid Chromatid

Chromosome Structure
Histone proteins organize the DNA into tightly
coiled structures (visible chromosomes) during cell division. Coiling into compact structures allows the chromatids to separate without tangling during cell division.
Replicated chromosome

Chromatin: a complex
of DNA and protein

Cell

Individual atoms

Histone proteins

DNA molecule
(double helix comprising genes)

Chromosome Features
Chromosomes can be
identified by noting:
Banding patterns Position of the Banding pattern centromere Presence of satellites Length of the chromatids

Acrocentric

Submetacentric or Subterminal

Metacentric

Centromere position

These features enable

homologous pairs to be matched and therefore accurate karyotypes to be made.

Satellite endings

Chromosome length

Chromosomes Contain Genes

A single chromosome may contain
hundreds of genes.
Below are the locations of some known genes on human chromosomes:
El Rh

AMY Fy MN TYS RB CBD HEMA

ABO NP

Chromosome:

1 No. of genes: 1270

4 465

9 499

13 195

X 773

Nucleotides

The building blocks of nucleic acids (DNA and

RNA) comprise the following components:
a sugar (ribose or deoxyribose) a phosphate group

a base (four types for each of DNA and RNA)

Adenine

Phosphate

Sugar

Base

Structure of Nucleotides
The chemical structure of nucleotides:
Symbolic form

Phosphate: Links neighboring sugars Base: Four types are possible in DNA: adenine, guanine, cytosine and thymine. RNA has the same except uracil replaces thymine. Sugar: One of two types possible: ribose in RNA and deoxyribose in DNA

Nucleotide Bases
The base
Purines
Doubleringed structures Always pair up with pyrimidines Pyrimidines Single-ringed structures
Base component of a nucleotide

component of nucleotides which comprise the genetic code

Adenine

Guanin e Cytosi ne Thymi ne

Always pair up with purines

Uracil

DNA Structure
Phosphates link
neighboring nucleotides together to form one half of a double-stranded DNA molecule:
Sugar (deoxyribose)
Purine base (guanine) Pyrimidine base (cytosine)

Phosphate
Pyrimidine base (thymine)

Hydrogen bonds

Purine base (adenine)

DNA Molecule
Purines join with
pyrimidines in the DNA molecule by way of relatively weak hydrogen bonds with the bases forming cross-linkages. This leads to the formation of a double-stranded molecule of two opposing chains of nucleotides:
The symbolic diagram shows DNA as a flat structure.
Hydrogen bonds

Symbolic representation

Space-filling model

The space-filling model

shows how, in reality, the DNA molecule twists into a spiral structure

DNA Replication 1
DNA is replicated
to produce an exact copy of a chromosome in preparation for cell division. The first step requires that the coiled DNA is allowed to uncoil by creating a swivel point.
Single-armed chromosome as found in non-dividing cell

Temporary break to allow swivel

Replication fork

DNA Replication 2
New pieces of DNA
are formed from free nucleotide units joined together by enzymes. The free nucleotides (yellow) are matched up to complementary nucleotides in the original strand.
Free nucleotides are used to construct the new DNA strand

Parent strand of DNA is used as a template to match nucleotides for the new strand

The new strand of DNA is constructed using the parent strand as a template

DNA Replication 3
The two new
strands of DNA coil up into a helix. Each of the two newly formed DNA strands will go into forming a chromatid
The double strands of DNA coil up into a helix

Each of the two newly formed DNA double helix molecules will become a chromatid

 Free nucleotides with their

DNA Replication 4
corresponding bases are matched up against the template strand following the base pairing rule: pairs A T with T G pairs with A
Template strand Template strand

pairs with
pairs with

Two new strands forming

Control of DNA Replication

replication is controlled by enzymes at key stages:
Overall direction of replication

DNA

5'

3' Double strand of original (parental) DNA

Swivel point Helicase

Leading strand

RNA polymerase

DNA polymerase III

DNA polymerase III

Replication fork
DNA polymerase I

DNA ligase

3' 5' 3'

5'

The Leading Strand

Overall direction of replication

Enzymes can

build strands only in the 5 to 3 direction This means that DNA polymerase III only one The parental strand, called strand provides a 'template' for of the the leading synthesis new strand strand, can be 3' synthesized as 5' a continuous strand.

5 '

3'

Swivel point

Helicase: Splits and unwinds the twostranded DNA molecule.

Replication fork

2 The leading strand

is synthesized continuously in the 5' to 3' direction by DNA polymerase III.

5'

The Lagging Strand

complementary strand, called the lagging strand, must be constructed in fragments, which are later joined together
1

Overall direction of replication

The other

5'

3'
2

Swivel point

RNA polymerase: Makes a short RNA primer which is later removed. 3 DNA polymerase III: Extends RNA primer with short lengths of complementary DNA to make Okazaki fragments.

RNA primer

Helicase: Splits and unwinds the twostranded DNA molecule.

New complementary strand is synthesized discontinuously, in fragments 1000-2000 bp long

3'

5'

Enzyme Control of Replication 4

5' Overall direction of replication 3'

DNA polymerase I: Digests the RNA primer and replaces it with DNA

5 DNA ligase: Joins

neighboring fragments together into longer strands.

The lagging strand is formed in fragments (called Okazaki fragments) which are later joined together. 3' 3' 5'

The Cell Cycle

The process of mitosis is only
part of a continuous cell cycle where most of the cell's 'lifetime' is spent carrying out its prescribed role; a phase in the cycle called interphase. Interphase is itself divided up into three stages:
G1 First Gap S Synthesis G2 Second Gap

Synthesis of DNA to replicate chromosomes

Second gap as cell grows and ensures DNA replication is complete

G2 S

The cell cycle

G1

Mitosis

Mitosis is the process by

which the cell produces two new daughter cells from the original parent cell

First gap as cell monitors its surroundings, growing and determining whether to replicate DNA

Mitosis
Nuclear Membrane

Interphase

Centrosome, which later forms the spindle, is also replicated.

Early Prophase

Late Prophase

Cell enters mitosis

Nucleolus DNA is replicated to form 2 chromatids

DNA continues condensing into chromosomes and the nuclear membrane begins to dissolve

Chromosomes continue to coil up and appear as double-chromatids

The mitotic spindle is formed to organize the chromosomes. The spindle consists of fibers made of microtubules and proteins.

Metaphase

Anaphase
Two new nuclei form. The cell plate forms across the midline of the parent cell. This is where the new cell wall will form.

Division of the cytoplasm (cytokinesis) is complete. The two daughter cells are now separate cells in their own right.

The chromosomes segregate, pulling the chromatids apart

Cytokinesis

Telophase

Late Anaphase

Mitosis Micrographs
Cell division for somatic growth and repair

1. Interphase

2. Prophase

3. Metaphase

6. Telophase

5. Late Anaphase

4. Anaphase

Meiosis
The purpose of
meiosis is to produce haploid sex cells. Haploid sex cells Intermediate cell have only one copy of each homologous pair of autosomes plus one sex chromosome
Crossing over may occur at this stage in meiosis

2N

2N

2N

First Division (Reduction division)

1N Intermediate cell

Second Division ('Mitotic' division)

1N

Gametes (eggs or sperm)

1N

Meiosis I
The first division
of meiosis is called a reduction division because it reduces (halves) the number of chromosomes. One chromosome from each homologous pair is donated to each intermediate cell
Intermediate cell

Interphase 2N

DNA replication

Prophase 1 2N

Synapsis and crossing over

Metaphase 1
2N

Bivalents line up on the equator

Anaphase 1 Telophase 1 1N

Intermediate cell

Meiosis II
The second
Intermediate cell

NOTE: Half the full chromosome complement shown 1N

division of meiosis is called a mitotic division, because it is similar to mitosis. Sister chomatids of each chromosome are pulled apart and are donated to each gamete cell
Telophase 2 Gamete (egg or sperm)

Prophase 2

1N

Metaphase 2

Anaphase 2

1N
Gamete (egg or sperm)

Meiosis & Mitosis Compared

MEIOSIS
2N
Homologous chromosomes pair up at the equatorial plate

MITOSIS
2N

Meiosis I Reduction division

Cell division Homologous chromosomes do not pair up at the equatorial plate

Meiosis II Mitotic division

Cell division

Cell division

1N

2N