Hyperthermophiles

- Veera Thalavai Sathish Kumar

C7209-г
Extremophiles
• Organisms that thrive under "extreme
conditions".
o Alkaline
o Acidic
o Extremely cold
o Extremely hot
o Theory: liquid water is necessary for
life
• Most known extremophiles are microbes,
mostly Archaea, but can also include
bacteria.
Hyperthermophiles
• A hyperthermophile is an organism that thrives in
extremely hot environments—from 60 °C (140 °F)
upwards.
• An optimal temperature for the existence of
hyperthermophiles is above 80 °C (176 °F).
• Growth rates are often rapid
• Archaea have growth-temperature optima above
100 C, while no species of Bacteria are known to
grow above 95 C.
• The most heat-tolerant of all known Archaea is
Methanopyrus, a methanogenic organism capable
of growth at 122 C.
Then where do
Hyperthermophiles
live?
• surface of soils
• Fermenting materials such as
compost piles and silage can also
reach temperatures of 70 C.
silage
• The most extensive and extreme compost piles

high-temperature environments in
nature are associated with volcanic
phenomena.
• Many hot springs have temperatures
at or near boiling, and steam vents
(fumaroles) may reach 150–500 C. hot springs
fumaroles
• Hydrothermal vents in the bottom of the
ocean can have temperatures of350 C or
greater.
• Hot springs are abundant in the western Hydrothermal
United States, New Zealand, Iceland, vents

Japan, Italy, Indonesia, Central America,

and central Africa. Eukaryotes Bacteria

• The largest concentration of hot springs Protozoa 56 Cyanobacteria 73

in the world is in Yellowstone National Algae 55- Anoxygenic 70-

Park, Wyoming (USA). 60 Phototrophs 73

• Different springs have different chemical fungi 60-

62
Chemoorganotrophs /
Chemolithotrophs
95

compositions and pH values. Above 65 C, Archaea Chemoorganotrophs / 122

only prokaryotes are present. Chemolithotrophs
Small boiling spring in Yellowstone National
Park. This spring is superheated, having a
temperature 1–2°C above the boiling point.
The mineral deposits around the spring
consist mainly of silica and sulfur.
Photomicrograph of a microcolony of
prokaryotes that developed on a
microscope slide immersed in such a boiling
spring.
 • Their enzymes and other proteins are much more heat-stable than are those of
Protein Stability mesophiles and actually function optimally at high temperatures.
• Often differ very little in amino acid sequence from heat-sensitive forms of the
at high enzymes that catalyze the same reaction in mesophiles.
• Critical amino acid substitutions at only a few locations in the enzyme allow the

temperature: protein to fold in such a way that it is heat-stable.

• latter property is a natural resistance to unfolding in an aqueous cytoplasm.
• Increased number of ionic bonds between basic and acidic amino acids and their
often highly hydrophobic interiors.
• solutes such as di-inositol phosphate, diglycerol phosphate, and mannosylglycerate
are produced at high levels in certain hyperthermophiles, and these may also help
stabilize their proteins against thermal degradation.
 Membrane stability at high temperature:
 Hyperthermophiles, most of which are
Archaea, do not contain fatty acids in their
membranes but instead have C40
hydrocarbons composed of repeating units
of isoprene bonded by ether linkage to
glycerol phosphate.
 The architecture of the cytoplasmic
Lipid monolayer
membranes of hyperthermophiles takes a
unique twist.
 The membrane forms a lipid monolayer
rather than a lipid bilayer.
 This structure prevents the membrane from
melting (peeling apart) at the high growth
temperatures of hyperthermophiles.
Protein Folding and Thermostability
These include having highly hydrophobic cores,
which decrease the tendency of the protein to unfold
in an ionic environment, and more ionic interactions
on the protein surfaces, which also help hold the
protein together and work against unfolding.
Ultimately, it is the folding of the protein that most
affects its heat stability, and noncovalent ionic bonds
called salt bridges on a protein’s surface likely play a
major role in maintaining the biologically active
structure.
 Chaperonins: Assisting Proteins to Remain
in Their Native State
• Hyperthermophilic Archaea have special classes
of chaperonins that function only at the highest
growth temperatures. In cells of Pyrodictium
abyssi.
• for example, a major chaperonin is the protein
complex called the thermosome. This complex
keeps other proteins properly folded and
functional at high temperature, helping cells
survive even at temperatures above their
maximal growth temperature.
• Cells of P. abyssi grown near its maximum
temperature (110°C) Pyrodictium abyssi
• contain high levels of the thermosome.
DNA Stability at High Temperatures:
Solutes:
• The cytoplasm of the hyperthermophilic methanogen Methanopyrus
contains molar levels of potassium cyclic 2,3-diphosphoglycerate.
• This solute prevents chemical damage to DNA, such as depurinationor
depyrimidization from high temperatures, events that can lead to
mutation.
• Potassium di-myo-inositol phosphate protects against osmotic stress.
• Polyamines putrescine and spermidine, which stabilize both
ribosomes and nucleic acids at high temperature, help maintain key
cellular macromolecules in hyperthermophiles in their active forms.
DNA Stability at High Temperatures:
Reverse Gyrase:
• All hyperthermophiles produce a special DNA
topoisomerase called reverse DNA gyrase.
• This enzyme introduces positive supercoils into
the DNA of hyperthermophiles
• Positive supercoiling stabilizes DNA to heat and
thereby prevents the DNA helix from
spontaneously unwinding.
• The noticeable absence of reverse DNA gyrase
in prokaryotes whose growth temperature
optima lie below 80°C strongly suggests a
specific role for this enzyme in DNA stability at
high temperatures.
 H2 as an Energy Source:
 The oxidation of H2 linked to the
reduction of Fe3+, S0, NO3 or,
rarely, O2 is a widespread form of
energy metabolism in
hyperthermophiles.

 Hydrogen metabolism may have

evolved in primitive organisms
because of the ready availability of
H2 and suitable inorganic electron
acceptors in their primordial
environments, but also because a H2-
based energy economy requires
relatively few proteins.