Microbial Structure

LECTURE PRESENTATIONS
For BROCK BIOLOGY OF MICROORGANISMS, THIRTEENTH EDITION

Michael T. Madigan, John M. Martinko, David A. Stahl, David P. Clark
Chapter 3
Cell Structure and
Lectures by Function in Bacteria
and Archaea
John Zamora
Middle Tennessee State University
© 2012 Pearson Education, Inc.

I. Cell Shape and Size
• 3.1 Cell Morphology
• 3.2 Cell Size and the Significance of
Smallness

3.1 Cell Morphology
• Morphology = cell shape
• Major cell morphologies (Figure 3.1)
– Coccus (pl. cocci): spherical or ovoid
– Rod: cylindrical shape
– Spirillum: spiral shape
• Cells with unusual shapes
– Spirochetes, appendaged bacteria, and
filamentous bacteria
• Many variations on basic morphological types

Figure 3.1
Coccus Spirochete
Stalk Hypha
Rod Budding and
appendaged bacteria
Spirillum
Filamentous bacteria

3.1 Cell Morphology
• Morphology typically does not predict physiology,
ecology, phylogeny, etc. of a prokaryotic cell
• Selective forces may be involved in setting the
morphology
– Optimization for nutrient uptake (small cells and
those with high surface-to-volume ratio)
– Swimming motility in viscous environments or
near surfaces (helical or spiral-shaped cells)
– Gliding motility (filamentous bacteria)

3.2 Cell Size and the Significance of
Smallness
• Size range for prokaryotes: 0.2 µm to >700 µm in
diameter
– Most cultured rod-shaped bacteria are between
0.5 and 4.0 µm wide and <15 µm long
– Examples of very large prokaryotes
• Epulopiscium fishelsoni (Figure 3.2a)
• Thiomargarita namibiensis (Figure 3.2b)
• Size range for eukaryotic cells: 10 to >200 µm in
diameter

Figure 3.2

Smallness
• Surface-to-Volume Ratios, Growth Rates, and
Evolution
– Advantages to being small (Figure 3.3)
• Small cells have more surface area relative to cell
volume than large cells (i.e., higher S/V)
– support greater nutrient exchange per unit cell
volume
– tend to grow faster than larger cells

Figure 3.3
r = 1 µm
r = 1 µm Surface area (4pr2) = 12.6 µm2
4
Volume ( 3 pr3) = 4.2 µm3
Surface
=3
Volume
r = 2 µm
r = 2 µm
Surface area = 50.3 µm2
Volume = 33.5 µm3
Surface
= 1.5
Volume

Smallness
• Lower Limits of Cell Size
– Cellular organisms <0.15 µm in diameter are
unlikely
– Open oceans tend to contain small cells (0.2–
0.4 µm in diameter)

II. The Cytoplasmic Membrane and
Transport
• 3.3 The Cytoplasmic Membrane
• 3.4 Functions of the Cytoplasmic Membrane
• 3.5 Transport and Transport Systems

3.3 The Cytoplasmic Membrane in
Bacteria and Archaea
• Cytoplasmic membrane:
– Thin structure that surrounds the cell
– 6–8 nm thick
– Vital barrier that separates cytoplasm from
environment
– Highly selective permeable barrier; enables
concentration of specific metabolites and
excretion of waste products

3.3 The Cytoplasmic Membrane
• Composition of Membranes
– General structure is phospholipid bilayer
(Figure 3.4)
• Contain both hydrophobic and hydrophilic
components
– Can exist in many different chemical forms as a
result of variation in the groups attached to the
glycerol backbone
– Fatty acids point inward to form hydrophobic
environment; hydrophilic portions remain exposed
to external environment or the cytoplasm
Animation: Membrane Structure

Figure 3.4
Glycerol
Fatty acids
Phosphate
Ethanolamine
Hydrophilic
region
Fatty acids Hydrophobic

region
Hydrophilic
region
Glycerophosphates
Fatty acids

• Cytoplasmic Membrane (Figure 3.5)
– 6–8 nm wide
– Embedded proteins
– Stabilized by hydrogen bonds and hydrophobic
interactions
– Mg2+ and Ca2+ help stabilize membrane by forming
ionic bonds with negative charges on the
phospholipids
– Somewhat fluid

Figure 3.5
Out
Phospholipids Hydrophilic
groups
6–8 nm
Hydrophobic
groups
In
Integral
membrane Phospholipid
proteins molecule

• Membrane Proteins
– Outer surface of cytoplasmic membrane can
interact with a variety of proteins that bind
substrates or process large molecules for transport
– Inner surface of cytoplasmic membrane interacts
with proteins involved in energy-yielding reactions
and other important cellular functions

• Membrane Proteins (cont’d)
– Integral membrane proteins
• Firmly embedded in the membrane
– Peripheral membrane proteins
• One portion anchored in the membrane

• Membrane-Strengthening Agents
– Sterols
• Rigid, planar lipids found in eukaryotic membranes
Strengthen and stabilize membranes
– Hopanoids
• Structurally similar to sterols
• Present in membranes of many Bacteria

• Archaeal Membranes
– Ether linkages in phospholipids of Archaea
(Figure 3.6)
– Bacteria and Eukarya that have ester linkages in
phospholipids
– Archaeal lipids lack fatty acids, have isoprenes
instead
– Major lipids are glycerol diethers and tetraethers
(Figure 3.7a and b)
– Can exist as lipid monolayers, bilayers, or mixture
(Figure 3.7d and e)
Figure 3.6
Ester
Ether
Bacteria Archaea
Eukarya

Figure 3.7a
Phytanyl
CH3 groups
Glycerol diether Isoprene unit

Figure 3.7b
Biphytanyl
Diglycerol tetraethers

Figure 3.7c
Crenarchaeol

Figure 3.7d
Out
Glycerophosphates
Phytanyl
Membrane protein
In
Lipid bilayer

Figure 3.7e
Out
Biphytanyl
In
Lipid monolayer

3.4 Functions of the Cytoplasmic
Membrane
• Permeability Barrier (Figure 3.8)
– Polar and charged molecules must be
transported
– Transport proteins accumulate solutes against
the concentration gradient
• Protein Anchor
– Holds transport proteins in place
• Energy Conservation

Figure 3.8
Permeability barrier: Protein anchor: Energy conservation:

Prevents leakage and functions Site of many proteins that Site of generation and use of the
as a gateway for transport of participate in transport, proton motive force
nutrients into, and wastes out bioenergetics, and chemotaxis
of, the cell

3.5 Transport and Transport Systems
• Carrier-Mediated Transport Systems (Figure 3.9)
– Show saturation effect
– Highly specific

Figure 3.9
Transporter saturated
Rate of solute entry
with substrate
Transport
Simple diffusion
External concentration of solute

• Three major classes of transport systems in
prokaryotes (Figure 3.10)
– Simple transport
– Group translocation
– ABC system
• All require energy in some form, usually proton
motive force or ATP

Figure 3.10
Simple transport: Out In
Driven by the energy
in the proton motive
force
Transported
substance
Group translocation:
Chemical modification
of the transported
substance driven by
phosphoenolpyruvate
1
2
ABC transporter: 3
Periplasmic binding
proteins are involved
and energy comes
from ATP

• Three transport events are possible: uniport,
symport, and antiport (Figure 3.11)
– Uniporters transport in one direction across the
membrane
– Symporters function as co-transporters
– Antiporters transport a molecule across the
membrane while simultaneously transporting
another molecule in the opposite direction

Figure 3.11
Out
In
Uniporter Antiporter Symporter

• Simple Transport:
– Lac Permease of Escherichia coli (Figure 3.12)
• Lactose is transported into E. coli by the simple
transporter lac permease, a symporter
• Activity of lac permease is energy driven
• Other symporters, uniporters, and antiporters

Figure 3.12
Out
In
Sulfate Potassium Phosphate Sodium-proton Lac permease
symporter uniporter symporter antiporter (a symporter)

• The Phosphotransferase System in E. coli
(Figure 3.13)
– Type of group translocation: substance
transported is chemically modified during
transport across the membrane
– Best-studied system
– Moves glucose, fructose, and mannose
– Five proteins required
– Energy derived from phosphoenolpyruvate

Figure 3.13
Glucose
Out
Cytoplasmic
membrane
Nonspecific components Specific components

Enz
IIC Direction
PE of glucose
transport
Enz HPr Enz Enz
IIa IIb
Pyruvate
In
Direction of P transfer
Glucose 6–P

3.5 Transport and Transport Proteins
• ABC (ATP-Binding Cassette) Systems
(Figure 3.14)
– >200 different systems identified in
prokaryotes
– Often involved in uptake of organic
compounds (e.g., sugars, amino acids),
inorganic nutrients (e.g., sulfate, phosphate),
and trace metals
– Typically display high substrate specificity
– Contain periplasmic binding proteins

Figure 3.14
Peptidoglycan
Periplasmic
Periplasm binding protein
Transported
Out substance
Membrane-
spanning
transporter
ATP-
hydrolyzing
In protein

3.5 Transport and Transport Proteins
• Protein Export
– Translocases: responsible for exporting proteins
through and inserting into prokaryotic membranes
• Sec translocase system: exports proteins and
inserts integral membrane proteins into the
membrane
• Type III secretion system: common in pathogenic
bacteria; secreted protein translocated directly into
host

III. Cell Walls of Prokaryotes
• 3.6 The Cell Wall of Bacteria: Peptidoglycan
• 3.7 The Outer Membrane
• 3.8 Cell Walls of Archaea

3.6 The Cell Wall of Bacteria:
Peptidoglycan
Peptidoglycan (Figure 3.16)
– Rigid layer that provides strength to cell wall
– Polysaccharide composed of
• N-acetylglucosamine and N-acetylmuramic acid
• Amino acids
• Lysine or diaminopimelic acid (DAP)
• Cross-linked differently in gram-negative bacteria
and gram-positive bacteria (Figure 3.17)

Figure 3.16
N-Acetylglucosamine N-Acetylmuramic acid
Glycan tetrapeptide
N-Acetyl
group
Lysozyme-
sensitive
Peptide bond
cross-links
L-Alanine
D-Glutamic acid
Diaminopimelic
acid
D-Alanine

Figure 3.17 Polysaccharide
backbone
Interbridge
Peptides
Escherichia coli
(gram-negative)
Staphylococcus aureus
(gram-positive)
Y
Peptide bonds
X
Glycosidic bonds

Peptidoglycan
• Gram-Positive Cell Walls (Figure 3.18)
– Can contain up to 90% peptidoglycan
– Common to have teichoic acids (acidic
substances) embedded in the cell wall
• Lipoteichoic acids: teichoic acids covalently
bound to membrane lipids

Figure 3.18
Peptidoglycan
cable
Ribitol
Teichoic acid Peptidoglycan

Wall-associated
protein
Lipoteichoic
acid
Cytoplasmic membrane

Peptidoglycan
• Prokaryotes That Lack Cell Walls
– Mycoplasmas
• Group of pathogenic bacteria
– Thermoplasma
• Species of Archaea

3.7 The Outer Membrane
• Total cell wall contains ~10% peptidoglycan
(Figure 3.20a)
• Most of cell wall composed of outer membrane
(aka lipopolysaccharide [LPS] layer)
– LPS consists of core polysaccharide and
O-polysaccharide
– LPS replaces most of phospholipids in outer
half of outer membrane
– Endotoxin: the toxic component of LPS

Figure 3.20a
O-polysaccharide Core polysaccharide
Lipid A Protein Out
Lipopolysaccharide
(LPS)
Porin
Outer 8 nm
membrane
Cell
wall
Phospholipid
Peptidoglycan
Periplasm
Lipoprotein
Cytoplasmic
membrane In

• Porins: channels for movement of hydrophilic low-
molecular weight substances (Figure 3.20b)
• Periplasm: space located between cytoplasmic
and outer membranes
– ~15 nm wide
– Contents have gel-like consistency
– Houses many proteins

Figure 3.20b
Periplasm
Cytoplasmic Outer membrane
membrane

• Structural differences between cell walls of
gram-positive and gram-negative Bacteria are
responsible for differences in the Gram stain
reaction

3.8 Cell Walls of Archaea
• No peptidoglycan
• Typically no outer membrane
• Pseudomurein
– Polysaccharide similar to peptidoglycan
(Figure 3.21)
– Composed of N-acetylglucosamine and N-
acetyltalosaminuronic acid
– Found in cell walls of certain methanogenic
Archaea
• Cell walls of some Archaea lack pseudomurein

Figure 3.21 N-Acetyltalosaminuronic
acid
Lysozyme-insensitive
N-Acetyl
group
N-Acetylglucosamine
Peptide
cross-links

3.8 Cell Walls of Archaea
• S-Layers
– Most common cell wall type among Archaea
– Consist of protein or glycoprotein
– Paracrystalline structure (Figure 3.22)

Figure 3.22

IV. Other Cell Surface Structures and
Inclusions
• 3.9 Cell Surface Structures
• 3.10 Cell Inclusions
• 3.11 Gas Vesicles
• 3.12 Endospores

3.9 Cell Surface Structures
• Capsules and Slime Layers
– Polysaccharide layers (Figure 3.23)
• May be thick or thin, rigid or flexible
– Assist in attachment to surfaces
– Protect against phagocytosis
– Resist desiccation

Figure 3.23
Cell Capsule

• Fimbriae
– Filamentous protein structures (Figure 3.24)
– Enable organisms to stick to surfaces or form
pellicles

Figure 3.24
Flagella
Fimbriae

• Pili
– Filamentous protein structures (Figure 3.25)
– Typically longer than fimbriae
– Assist in surface attachment
– Facilitate genetic exchange between cells
(conjugation)
– Type IV pili involved in twitching motility

Figure 3.25
Virus-
covered
pilus

3.10 Cell Inclusions
• Carbon storage polymers
– Poly-b-hydroxybutyric acid (PHB): lipid (Figure
3.26)
– Glycogen: glucose polymer
• Polyphosphates: accumulations of inorganic
phosphate (Figure 3.27)
• Sulfur globules: composed of elemental sulfur
• Magnetosomes: magnetic storage inclusions
(Figure 3.28)

Figure 3.26
b-carbon
Polyhydroxyalkanoate

Figure 3.27
Polyphosphate
Sulfur

Figure 3.28

3.11 Gas Vesicles
• Gas Vesicles
– Confer buoyancy in planktonic cells
(Figure 3.29)
– Spindle-shaped, gas-filled structures made of
protein (Figure 3.30)
– Gas vesicle impermeable to water

Figure 3.29

Figure 3.30

3.11 Gas Vesicles
• Molecular Structure of Gas Vesicles
– Gas vesicles are composed of two proteins:
GvpA and GvpC (Figure 3.31)
– Function by decreasing cell density

Figure 3.31
Ribs
GvpA
GvpC

3.12 Endospores
• Endospores
– Highly differentiated cells resistant to heat, harsh
chemicals, and radiation (Figure 3.32)
– “Dormant” stage of bacterial life cycle
(Figure 3.33)
– Ideal for dispersal via wind, water, or animal gut
– Only present in some gram-positive bacteria

Figure 3.32
Terminal Subterminal Central

spores spores spores

Figure 3.33
Vegetative cell
Developing spore
Sporulating cell
Mature spore
3.12 Endospores
• Endospore Structure (Figure 3.35)
– Structurally complex
– Contains dipicolinic acid
– Enriched in Ca2+
– Core contains small acid-soluble proteins
(SASPs)

Figure 3.35
Exosporium
Spore coat
Core wall
Cortex
DNA

3.12 Endospores
• The Sporulation Process
– Complex series of events (Figure 3.37)
– Genetically directed

Figure 3.37
Coat
Spore coat, Ca2+

Free endospore Maturation, uptake, SASPs,
cell lysis dipicolinic acid
Stage VI, VII

Growth Germination Stage V
Cortex
Vegetative Sporulation Cell wall
cycle stages Cytoplasmic
membrane
Cell Asymmetric
division cell division;
commitment Stage IV
to sporulation, Cortex
Stage I formation
Prespore
Septum
Engulfment
Mother cell
Stage II Stage III

V. Microbial Locomotion
• 3.13 Flagella and Motility
• 3.14 Gliding Motility
• 3.15 Microbial Taxes

3.13 Flagella and Motility
• Flagellum (pl. flagella): structure that assists
in swimming
– Different arrangements: peritrichous, polar,
lophotrichous (Figure 3.38)
– Helical in shape
Animation: The Prokaryotic Flagellum

Figure 3.38

• Flagellar Structure
– Consists of several components (Figure 3.41)
– Filament composed of flagellin
– Move by rotation

Figure 3.41
15—20 nm
L
Filament P
Flagellin MS
Outer Hook
membrane
(LPS)
L Ring
Rod
P Ring
Periplasm Peptidoglycan
Rod
MS Ring
Basal MS Ring
body
Mot
C Ring protein
C Ring
Cytoplasmic Mot protein Fli proteins Mot protein

membrane (motor switch)
45 nm

• Flagellar Synthesis
– Several genes are required for flagellar
synthesis and motility (Figure 3.43)
– MS ring made first
– Other proteins and hook made next
– Filament grows from tip

Figure 3.43
Filament
synthesis
Late Hook-
hook filament
Outer Cap junction Filament
membrane Early hook
MS/C Motor (Mot)
ring proteins P ring L ring
Peptidoglycan Cytoplasmic membrane

• Flagella increase or decrease rotational speed in
relation to strength of the proton motive force
• Differences in swimming motions (Figure 3.44)
– Peritrichously flagellated cells move slowly in a
straight line
– Polarly flagellated cells move more rapidly and
typically spin around

Figure 3.44
Tumble—flagella
pushed apart
(CW rotation)
Bundled
flagella
(CCW rotation)
Flagella bundled
(CCW rotation)
Peritrichous
Reversible flagella
CCW rotation CW rotation
Unidirectional flagella
Cell
stops,
CW rotation reorients
CW rotation
Polar
3.14 Gliding Motility
• Gliding Motility
– Flagella-independent motility (Figure 3.46)
– Slower and smoother than swimming
– Movement typically occurs along long axis of cell
– Requires surface contact
– Mechanisms
• Excretion of polysaccharide slime
• Type IV pili
• Gliding-specific proteins

Figure 3.46
In
Cytoplasmic
membrane
Peptidoglycan
Outer
membrane
Out
Movement of outer Surface
Movement of cell membrane proteins

3.15 Microbial Taxes
• Taxis: directed movement in response to chemical
or physical gradients
– Chemotaxis: response to chemicals
– Phototaxis: response to light
– Aerotaxis: response to oxygen
– Osmotaxis: response to ionic strength
– Hydrotaxis: response to water

• Chemotaxis
– Best studied in E. coli
– Bacteria respond to temporal, not spatial,
difference in chemical concentration
– “Run and tumble” behavior (Figure 3.47)
– Attractants and receptors sensed by
chemoreceptors

Figure 3.47
Tumble Attractant
Tumble
Run
Run
No attractant present: Attractant present:

Random movement Directed movement

• Measuring Chemotaxis (Figure 3.48)
• Measured by inserting a capillary tube
containing an attractant or a repellent in a
medium of motile bacteria
• Can also be seen under a microscope

Figure 3.48
Control
Attractant
Repellent
Attractant
Cells per tube
Control
Repellent
Time

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LECTURE PRESENTATIONS

For BROCK BIOLOGY OF MICROORGANISMS, THIRTEENTH EDITION

© 2012 Pearson Education, Inc.

© 2012 Pearson Education, Inc.

© 2012 Pearson Education, Inc.

© 2012 Pearson Education, Inc.

© 2012 Pearson Education, Inc.

© 2012 Pearson Education, Inc.

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Fatty acids Hydrophobic

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Permeability barrier: Protein anchor: Energy conservation:

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External concentration of solute

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Uniporter Antiporter Symporter

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Nonspecific components Specific components

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Teichoic acid Peptidoglycan

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O-polysaccharide Core polysaccharide

Lipid A Protein Out

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