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Cell Cycle and Cell Division NOTES

The document discusses the cell cycle, including mitosis and meiosis, highlighting their significance in growth, repair, and reproduction. It details the phases of the cell cycle, the processes of mitosis and meiosis, and the importance of these processes in maintaining genetic continuity and diversity. Additionally, it covers biomolecules, their classifications, and the structure and function of proteins.

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0% found this document useful (0 votes)
7 views

Cell Cycle and Cell Division NOTES

The document discusses the cell cycle, including mitosis and meiosis, highlighting their significance in growth, repair, and reproduction. It details the phases of the cell cycle, the processes of mitosis and meiosis, and the importance of these processes in maintaining genetic continuity and diversity. Additionally, it covers biomolecules, their classifications, and the structure and function of proteins.

Uploaded by

janvibiswas964
Copyright
© © All Rights Reserved
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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eCell Cycle and Cell Division

Important Points
 Cell Cycle
 Mitosis
 Meiosis

 Meiosis I

 Meiosis II

Cell Cycle and Cell Division


Cell division is essential for growth, repair and reproduction. Many cell
cycles transform a single cell to a multicellular organism.

Cell Cycle

 Cell growth, DNA replication and cell division constitute a cell cycle

 Events happening in a cell cycle is genetically controlled

 Duration of cell cycle varies in different organisms and different types of cells. The average
duration of the human cell cycle is 24 hrs, whereas a yeast cell completes one cell cycle in 90
minutes

 The cell cycle is divided into Interphase and M phase

 Interphase: Cell growth and replication of DNA. It constitutes 95% of the duration of a cell
cycle

 M Phase: Mitosis (cell division)

Phases of the Cell Cycle


A. Interphase
Interphase is the time lapse between two successive M phases of cell division. The cell
prepares for division, grows and DNA replication takes place. Interphase is further divided
into three phases: G1, S, G2
 G1 Phase or Gap 1: It is the gap between previous mitosis and DNA replication of the
next cell cycle
 S Phase or Synthesis: In this phase DNA replication takes place. The DNA content of
the cell doubles and centriole duplicates. It is important to note that the
chromosome number remains the same
 G2 Phase or Gap 2: Cell continues to grow and prepare for mitosis. Protein synthesis
takes place. In an adult human being, there are many cells, which do not divide, e.g.
heart cells divide occasionally only to replace injured and dead cells. These cells
enter an inactive phase called G0 or quiescent stage of the cell cycle

B. M Phase: This is the phase where actual cell division occurs. The number of chromosomes
in the parent and daughter cells remains the same so it is also known as equational division.

Karyokinesis, i.e. nuclear division is followed by cytokinesis, i.e. division of the cytoplasm to
give rise to two daughter cells
Mitosis

 Mitosis mostly occurs in the diploid somatic cells of animals with few
exceptions, haploid male drone of honey bees
 In plants, mitosis happens in both haploid and diploid cells
 Mitosis is responsible for genetic continuity and growth and repair of
multicellular organisms
 In humans, the epithelial lining, lining of gut and blood cells are replaced
continuously
 In plants, meristematic tissues divide continuously throughout their life
 Mitosis accounts for the asexual reproduction or vegetative propagation,
where identical individuals are formed
 Karyokinesis occurs in four sequential stages:
1. Prophase
2. Metaphase
3. Anaphase
4. Telophase
 Karyokinesis is followed by cytokinesis
 Prophase
 Chromosomes untangle and condense
 Two chromatids attached to the centromere can be seen clearly
 Each of the duplicated centrosomes radiates microtubules (asters)
 Mitotic apparatus constitutes spindle fibres and asters
 Golgi bodies, nucleolus, endoplasmic reticulum and nuclear
membrane disappear
 Metaphase
 Complete disintegration of the nuclear envelope
 Two sister chromatids attached by the centromere aligned at the
equator, i.e. metaphase plate
 Each chromatid is attached to spindle fibres from opposite poles at
kinetochores
 Anaphase
 Splitting of centromere and two sister chromatids separate and go
towards the opposite poles
 Sister chromatids now become the daughter chromosomes
 Telophase:
 Chromosomes cluster at opposite poles and decondense
 Nuclear envelope develops around each cluster of chromosomes
and two daughter nuclei are formed
 The nucleolus, endoplasmic reticulum and Golgi apparatus are
reformed
Cytokinesis: Separation of cytoplasm takes place after two nuclei are formed.
Cell organelles get distributed between daughter cells.
In some organisms like fungi, algae and plant cells, cytokinesis is not
immediately followed by karyokinesis and the multinucleate stage is formed
known as a syncytium, e.g. liquid endosperm in coconut, coenocytic hyphae
of Rhizopus, etc.

Significance of mitosis  Growth and development - A single cell zygote


grows into full blown baby ( 6×1022 cells) by repeated mitosis. Plants are able
to grow throughout their life due to mitotioc division in their apical and lateral
meristems. Increases in tissue mass, results from increase in cell number called
hyperplasmic. Hnece, mitosis is essential for growth and development of a
multicellular organism.  Maintenance of cell size: An overgrown somatic cell is
induced to divide so that mitosis helps in maintaining a proper surface volume
ratio. It has also a high nucleocytoplasmic ratio which is brought back to
efficient level through divisions. These ratios are important for proper
functioning of cell distribution of all the chromosomes. This helps in proper co-
ordination among daughter cells.  Healing and regeneration – For healing of
wounds new cells are produced by Mitosis some organism are able to
regenerate missing part of body also whole organism though mitosis  Reparing
– the mechanism for replacing old or worn out cells is called repairing. In
human body roughly 5 ×109 cells are lost from skin surface, lining of alimentary canal, blood cell
etc. these are replaced by new cells formed through mitosis.  Evidence of basic relationship – The
mechanism of mitosis are similar in the majority of organism, showing basic similarity and
relationship among them

Meiosis
 Meiosis is also known as reduction division

 Haploid gametes formed during sexual reproduction (gametogenesis) are due to meiosis

 Meiosis is responsible for maintaining conservation of the number of chromosomes in


different individuals of the same species

 Meiosis also accounts for the genetic variation or differences between two individuals of the
same species

 There are two sequential cell divisions, i.e. Meiosis I and Meiosis II

 DNA replication occurs only once in the S phase before meiosis I

 In meiosis I, the pairing of homologous chromosomes is followed by recombination between


non-sister chromatids and formation of two haploid daughter cells

 Meiosis II is like a mitotic division and at the end of meiosis, 4 haploid daughter cells are
formed
Meiosis I
Prophase I
It is an extended stage and further divided into various stages:
 Leptotene- Chromosomes start condensing
 Zygotene- Pairing of homologous chromosomes. Synapsis is
characterized by the formation of the synaptonemal complex.
Chromosomes appear as bivalent or tetrad
 Pachytene- Crossing over takes place between non-sister chromatids and
recombination nodule is formed. It is an enzyme-mediated process. The
enzyme responsible for crossing over is Recombinase
 Diplotene- Synaptonemal complex dissolve and homologous
chromosomes separate from each other, except at the crossovers
forming Chiasmata (the ‘X’ shaped structure). Oocyte of some
vertebrates can remain at the diplotene stage for years, e.g.
human primary oocytes remain in this stage until puberty when
ovulation occursLampbrush chromosomes found in the oocyte of
amphibians are formed at the diplotene stage.
 Diakinesis- Nucleolus disappears, chiasmata separate and nuclear
envelope also starts degenerating
Metaphase I
Bivalent chromosomes align at the equator and homologous chromosomes get
attached to the spindles from opposite poles
Anaphase I
Homologous chromosomes move to opposite poles. Unlike mitosis, sister
chromatids remain attached
Telophase I
Nucleolus and nuclear envelope reappear, chromosomes collect at the poles
This is followed by cytokinesis and dyad of haploid cells are formed
Meiosis II
Meiosis I is followed by a short-lived and transient interkinesis. There is no
DNA replication at this stage.
Meiosis II is more like mitosis and each haploid cell forms 2 more haploid cells
so, after both meiotic divisions, we get 4 haploid cells from one diploid cell.
Prophase II
The nuclear envelope disappears
Metaphase II
Chromosomes align in the centre and kinetochore of sister chromatids get
attached to spindles from opposite poles
Anaphase II
Centromere splits and sister chromatids separate. They move to opposite poles
Telophase II
Nuclear membrane reappears
Cytokinesis follows and we get 4 haploid daughter cells, i.e. tetrad

Cytokinesis  Cytoplasm divides at its middle by furrowing in an animal cell


and by cell plate formation in a plant cell. This produces two daughter cells.
The latter have half the number of chromosomes and half the amount of
nuclear DNA. These cells are mature gametes in animals and spores in plants. 
Cytokinesis may occur after each nuclear division. In such cases, it is said to be
of successive type. First the diploid parent cell divides by heterotypic division
into two haploid cells, which then produce four haploid cells by homotypic
division. The four daughter cells may form a linear or isobilateral tetrad. Often
cytokinesis is delayed until both the nuclear divisions are completed, so that
four cells are simultaneously formed, each with a haploid nucleus. The
cytoplasmic division in such cases is said to be of simultaneous type

Significance of meiosis  Formation of gametes – Meiosis forms gametes


that are essential for sexual reproduction.  Genetic information – It switches
on the genetic information for the development of gametes or gametophytes
and switches off the sporophytic information  Meiosis facilitates stable sexual
reproduction – Without the halving of ploidy, or chromosome count,
fertilization would result in zygotes that have twice the number of
chromosomes than the zygotes from the previous generation. Successive
generations would have an exponential increase in chromosome count,
resulting in an unwildy genome that would cripple the reproductive fitness of
the species. Most importantly, however, meiosis produces genetic variety in
gametes that propagates to offspring. Recombination and independent
assortment allows for a greater diversity of genotype in the population. As a
system of creating diversity, meiosis allows a species to maintain stability under
environment changes.  Crossing over- It introduces new combination of traits
or variations.  Mutations – Chromosomal and genomatic mutations can take
place by irregularities of meiotic divisions. Some of these mutations are useful
to the organism and are perpetuated by natural selection.  Evidence of basic
relationship of organisms – Details of meiosis is essentially similar in the
majority of organisms showing their basic similarity and relationship .

Biomolecules NOTES
Biomolecules include both micromolecules, e.g. amino acids, nitrogenous bases, fatty acids,
sugar, etc. and macromolecules, such as carbohydrates, proteins, lipids and nucleic acids.

Living organisms are made up of organic as well as inorganic substances. For analysing the
organic constituents of living tissue, we mix it with CCl3COOH (Trichloroacetic acid) and
make a slurry by grinding. We get two fractions:
Acid soluble fraction- Organic micromolecules (biomolecules) (mol wt. 18-800
Da) and inorganic compounds, e.g. phosphate, sulphate, etc. It mostly
accounts for the cytoplasm

Acid insoluble fraction- Polymeric macromolecules (mol wt. >10 thousand Da)
and also lipid (a component of the cell membrane and form water-insoluble
vesicles on fragmentation)

The inorganic constituents can be estimated by analysing the ash formed after
burning a tissue completely.

All the macromolecules are homo or heteropolymers of various simple


compounds.

Protein- Polymer of amino acids


Carbohydrates (Polysaccharides)- Polymer of simple sugars, e.g. glucose,
fructose
Fats- Fatty acids and glycerol
Nucleic acids- Nitrogenous bases, sugar and phosphate
Water constitutes 70-90% of cells. Proteins are 10-15%, nucleic acids are 5-7%,
carbohydrates are 3%, lipids are 2% and the rest 1% are ions.
Amino acids, fatty acids, sugars, etc. are called primary metabolites, which take
part in the physiological processes. Other than these, there are varied
compounds present in the cells of plants, microbes and fungi, which are
called secondary metabolites. Some of the secondary metabolites have
ecological significance.
Secondary metabolites can be grouped under various categories:
Pigments (anthocyanins, carotene, etc.), drugs (curcumin, vinblastine, etc.),
gum, rubber, toxins (ricin, abrin), alkaloids (codeine, morphine), essential oils,
terpenoids, lectins (concanavalin A), etc.

Proteins
Proteins perform many vital functions in the living organisms. Proteins are
present as enzymes (trypsin, lipases, amylase, etc.), hormones (Insulin), tissue
fibres are made up of proteins (collagen, elastin, etc.). Some of the protein
molecules take part in transportation (GLUT-4) across a membrane and also
fight infection (antibodies).
RuBisCO (Ribulose bisphosphate carboxylase oxygenase), the enzyme in carbon
fixation, is the most abundant protein present in the biosphere. Collagen is the
most abundant protein present in animals.

Protein Structure
Protein is a heteropolymer of amino acids. A linear protein molecule has a
sequence of amino acids, that are linked by a peptide bond. Proteins are also
known as polypeptides.
Amino Acids

 Amino acids are organic compounds


They are substituted methanes. The 𝜶- carbon has various substituents
so they are also called 𝜶- amino acids

 The 𝜶- carbon has an amino group, carboxylic group, hydrogen and a


variable R group
 Based on the nature of the R group, there are 20 amino acids present in
proteins
 Amino acids can exist in a zwitterionic form, which changes according to
the pH of the solution to NH3+ (at low pH) or COO– (at high pH)
 Essential amino acids are required through diet. There are 9 essential
amino acids: valine, leucine, isoleucine, phenylalanine, tryptophan,
lysine, histidine, methionine and threonine
 Non-essential amino acids are formed inside the body and include
glycine, alanine, arginine, aspartic acid, asparagine, cysteine, glutamine,
glutamic acid, serine, proline and tyrosine
 Amino acids can be basic (lysine), acidic (glutamic acid) or neutral
(valine) based on the R group present
 Tryptophan, tyrosine and phenylalanine have an aromatic side chain
Primary Structure of protein is a long chain of amino acids in a specific
sequence. The amino acid chain starts from N’ and ends with C’. amino acids
are linked by C-N peptide bonds. The peptide bond is formed between the
carboxyl (-COOH) of one amino acid and amino group (-NH2) of another amino
acid. The process of peptide bond formation involves dehydration, one water
molecule is released.

amino acids is folded right-handed to form 𝜶-helix or are arranged as 𝛃-


Secondary Structure of a protein has a helical structure. The long thread of

pleated sheets, which consist of 𝛃-strands, laterally joined by at least 2-3


hydrogen bonds.
Tertiary Structure of protein is highly folded. Protein chains are folded like a
hollow woollen ball. It is a three-dimensional organisation, which is required
for optimum activity.
Quaternary Structure is required when a protein is made up of more than one
polypeptide chain or has subunits. These spheres of subunits or polypeptides

E.g. Haemoglobin consists of 4 subunits, 2 subunits each of 𝛼 and 𝛽 type.


may be arranged as linear strings or form a cube or plate.

Carbohydrates or Polysaccharides
Carbohydrates are polymers of monosaccharides or simple sugars. They are the
main energy source of plants and animal cells. They have a general formula of
[Cx(H2O)y]n.
Reducing sugars- All monosaccharides are reducing sugar. Some disaccharides
are reducing, e.g. lactose, maltose, etc. They act as a reducing agent and
reduce Tollen’s, Fehling or Benedict’s reagents. They have free aldehyde or
ketone group (in a cyclic form hemiacetal or hemiketal group)
Non-reducing sugars- Sucrose (a disaccharide) is non-reducing as both the
carbonyl groups are involved in the glycosidic bond formation. All the
polysaccharides (cellulose, starch) are non-reducing
Monosaccharides- Glucose, Galactose, Fructose, ribose, etc. They are the
building blocks of polysaccharides

Disaccharides- They are the dimer of the same or different monosaccharides.


The monosaccharides are linked by a glycosidic bond between two carbons of
the monomers.
Maltose or malt sugar is made up of two 𝛼-D-glucose molecules linked by 1,4
linkage
Lactose is milk sugar and made up of 𝛽-D-galactose and 𝛽-D-glucose by 1,4
linkages
Sucrose is made up of glucose and fructose

Structure and Function of Polysaccharides


They perform various functions and provide energy to the living cells. They
constitute the cell wall stored as a food reserve. Starch, cellulose and glycogen
are homopolymers of glucose. Heteropolymers are found in pectins, gums, etc.
Cellulose is a homopolymer of 𝛽-D-glucose molecules linked by 𝛽-1,4
glycosidic bonds. Cellulose is present in the cell wall of plants. Cotton fibres are
cellulosic. Cellulose is a long-chain polymer and adjacent chains are linked by
hydrogen bonds.
Starch is a major food reserve of plants. It is a polymer of glucose. It
contains amylose and amylopectin.
 Amylose has 𝛼-1,4 linkage of D glucose. The chains are coiled to form a
secondary helical structure, which traps I2 to form a blue colour complex
In Amylopectin, linear chains are linked by 𝛼-1,4 glycosidic bonds and
branches are formed by 𝛼-1,6 linkage

Glycogen is a food reserve for animals. It is similar to glycogen in structure, but


it is more branched.
Inulin- polymer of fructose, present in many plants. It is found in roots and
rhizomes.
Complex carbohydrates- They are polymer of substituted sugars such as amino
sugars or sugar acids, e.g. N-acetylglucosamine, N-acetylmuramic acid.
 Chitin is a polymer of N-acetyl glucosamine. It is present in the
exoskeleton of insects, cell wall of fungi, scales of fish, etc.
 Peptidoglycan (Murein) is a polymer of sugar and amino acids. Sugars
present in peptidoglycan are the alternating unit of N-acetylglucosamine
and N-acetylmuramic acid. The bacterial cell wall is made up of
peptidoglycan.
Lipids
Fats, oil, wax, steroids, cholesterol are all lipids. They play an important role in
metabolism. They are high energy-yielding compounds. Lipids are water-
insoluble and found in membranes and also present as hormones and energy
reserves.
 Fatty acids are carboxylic compounds having a long chain R group
attached to it. The alkyl group could contain 1 C (methyl) to 19 carbons
and can be saturated (contains only single bonds) or unsaturated (one or
more C=C double bonds). Palmitic acid- 15 C R group, Arachidonic acid-
19 C R group
 Essential fatty acids are not formed in the body, e.g. linoleate, non-
essential amino acids are produced in the body
 Monoglycerides, diglycerides and triglycerides are esters of fatty acids
with glycerol and are known as fats. Oils have low m.p. and remain in
liquid form in winters too
 Complex lipids contain more substituent in addition to fatty acids and
alcohol. Phospholipids are present in the membrane, e.g. lecithin
 Steroids are present as hormones and have a tetracyclic structure.
Cholesterol is the main steroid and is a precursor of many steroids
hormones
 Nucleic Acids
Nucleic acids are found in all the living cells. Even a virus contains nucleic acids
(DNA or RNA). DNA and RNA contain genetic information.
 Friedrich Miescher discovered nucleic acid and named it nuclein
 They are also known as polynucleotides, a polymer of nucleotide
Nucleotide
A nucleotide has three components: a nitrogenous base, a pentose sugar and a
phosphate group

Nitrogenous base- There are two types of nitrogenous bases:


1. Purine: Adenine and Guanine
2. Pyrimidine: Thymine, Cytosine and Uracil
Sugar- DNA contains deoxyribose sugar and RNA contains ribose sugar
molecules.
Nitrogenous bases attached to sugar are called Nucleosides.
Phosphate- Phosphate group is attached to sugar by the phospho-ester bond.
Nucleosides with attached phosphates are called Nucleotides.
Nucleotides are joined by 3’- 5’ phosphodiester bonds to form polynucleotides.
DNA and RNA are polynucleotides. The long chain of polynucleotides is folded
further to form secondary and tertiary structures.

DNA
 Watson and Crick gave the double helix model
 DNA consists of antiparallel strands of polynucleotide chains, which are
coiled in the right-hand direction
 The backbone of DNA is formed by sugar and phosphate and the
nitrogenous bases are projected inside
 Nitrogenous bases of one strand are attached to the nitrogenous bases
of the antiparallel strand
Adenine pairs with thymine by two hydrogen bonds (A=T)
Guanine (G) pairs with cytosine (C) by three hydrogen bond
Each helical turn is composed of 10 base pairs with a pith of 34 Å. The
distance between any two base pairs is 3.4 Å

 DNA is packaged in the form of nucleosomes and then further to


chromatin fibres of chromosomes

To read more about DNA structure and inheritance click here

RNA
 RNA is a single-stranded polynucleotide chain
 RNA contains ribose sugar and uracil in place of thymine
 There are three types of RNA, mRNA, tRNA and rRNA
 mRNA provides the template for protein synthesis
 Ribozymes are RNA molecules. They act as an enzyme and catalyse
biochemical reactions

Enzymes
Enzymes catalyse metabolic reactions in our body. Most of the enzymes are
proteins, ribozymes are RNA, which act as an enzyme.
Enzymes have an active site where the specific substrate binds. A transient ES
complex is formed, which is converted to EP complex and then the product is
released with unchanged enzymes.
Temperature, pH and concentration of substrate regulate the enzyme activity.
Enzyme activity is also regulated by binding of other substrates, e.g.
competitive inhibitor, inhibit the reaction by binding at the active site.
Malonate inhibits the activity of succinate dehydrogenase as it binds to the
active site due to its similarity with the actual substrate, succinate.
Many enzymes have an allosteric regulation mechanism. In allosteric
regulation, effector (inhibitor or activator) binds to a site other than the active
site to bring about conformational changes and thereby affecting the activity of
the enzyme.
Product may also act as an inhibitor, this type of regulation is called feedback
regulation.
Enzymes get damaged by at the temperature above 40℃, but enzymes of
thermophilic organisms remain stable at high temp also.
Also see: Biochemical Pathways

There are six major classes of enzymes:


1. Dehydrogenases or oxidoreductases- One of the substrate gets oxidised
and another reduced, e.g. oxidases, reductases, dehydrogenases
2. Transferases- Catalyses the transfer of a group from one substrate to
another, e.g. transaminase, transketolase, transaldolase
3. Hydrolases- Hydrolysis of various bonds such as glycosidic, ester,
peptide, etc, e.g. amylases, lipases, proteases, nucleases
4. Lyases- Removal of a group by other than hydrolysis. A double bond is
formed, e.g. aldolases, decarboxylases, fumarase, citrate synthase
5. Isomerases- Formation of isomers (positional, geometrical or optical),
e.g. isomerase, epimerase, mutase
6. Ligases- joining of two compounds, i.e. formation of C-O, C-S, C-N, P-O
bonds, e.g. synthetases, carboxylases
Cofactors: Cofactors are a non-protein part of the enzyme that is required for
the activity of an enzyme. The protein part of the enzyme is known
as apoenzyme. Catalytic activity is lost after the removal of cofactors. There are
three types of cofactors:
1. Prosthetic group- They are organic compounds tightly bound to the
apoenzyme, e.g. haem is a prosthetic group of enzymes catalase and
peroxidase
2. Co-enzymes- They are organic compounds associated with the enzyme
for a short period of time. Many vitamins act as a coenzyme catalysing
various reactions, e.g. coenzymes NAD and NADP contain niacin
3. Metal ions- Many metal ions work as cofactor. They get attached to the
active site by forming a coordination bond and also form a coordination
bond with the substrate, e.g. Zn metal acts as a cofactor of
carboxypeptidase

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