lectures in university of brawijaya, 2013 biological responses to environmental stress tetsuro...
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Lectures in University of Brawijaya, 2013
Biological Responses to Environmental Stress
Tetsuro Ishii, PhD.
Professor Emeritus, University of Tsukuba, Japan
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Animal
Plant
poisons
Detoxification systemNatural immunityRepair systemApoptosis
Animals have developed defense system against environmental stress agents
Toxic agents
UV, As, Heavy metals
Infection
Bacteria, Virus
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Stress causes upregulation of stress proteins
stressor Detection by sensors
Gene activation
Protein synthesisRepair damages
Cell damages
Acquire tolerance
Activation of transcription factors
Heat shockOxidative stress
HSFsNrf2
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Biological Responses to Environmental Stress
1. Cellular response to heat
2. Cellular response to electrophiles and reactive oxygen species
3. Nrf2 target genes
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Heat was necessary to create life
Adaptation to heat is most important for life.
Yellowstone hot spring
Hydrothermal vent
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Heat shock induces various proteins in cells
37°C 43°C
Temperature shift
Induction of heat shock proteins (HSPs)Has60, Hsp70, Hsp90, etc.
Activation of heat shock factors
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Heat shock protein (HSP) family
HSP110HSP100HSP90HSP70 (DNAK)HSP60 (chaperonin, GroEL)HSP47HSP40 (DNAJ)HSP33HSP27HSP15HSP10
Some of these proteins are constitutively expressed and play their roles under normal temperature.
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Some proteins return to native form following heat denaturation
denature or unfolding
Renature or refolding
But, many proteins became aggregated when denatured
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Denatured/unfolded proteins tend to aggregate
Protein aggregates
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Inhibition of protein aggregation by Dank-ClpB
Heat shock
Aggregation
Native form
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Chaperonin inhibits protein aggregation
Native form
Denatured form
Urea + DTT
± chaperonin
albumin
Enzyme activity
turbidity
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Opitical Scattering
Inhibition of protein aggregate by chaperonin
ATP-dependent folding of GFP-protein by chaperonin
GFP fluorescence
(+) chaperonin
(-) chaperonin
Time (min)
Time (min)
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Without chaperonin
With chaperonin
Chaperonin inhibits protein aggregate by heat treatment
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Double ring structure of chaperonin, GroEL
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GroEL-GroES complex provides space for protein folding
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Discovery of chaperonin
“Molecular chaperon” was found in different systems
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Functions of chaperonin during protein synthesis
chaperonin
hsp
normal folding
aggregates
Protein synthesis
Miss-folding
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Role of chaperons in protein synthesis
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Role of chaperons in protein targeting to mitochondria