Comprehensive Physiology Wiley Online Library

Temperature Relationships: From Molecules to Biogeography

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Abstract

The sections in this article are:

1 Temperature Effects on Physiological, Biochemical, and Molecular Systems: Basic Considerations
2 Temperature Effects on Proteins
2.1 Determinants of Thermal Sensitivities of Protein Structure and Function
2.2 Protein Structural Stability and Adaptation Temperature
2.3 Adaptations in Enzyme Kinetic Properties Lead to Conservation of Metabolic Regulation and Rate of Function
2.4 Rate Compensation to Temperature Through Alterations in Enzyme Concentration
3 The Heat Shock Response
3.1 Molecular Chaperones: Assistants in Protein Folding, Compartmentation, and Renaturation
3.2 The Heat Shock Response and Induced Thermal Tolerance
3.3 Acclimatization‐Induced Differences in the Heat Shock Response
3.4 Interindividual and Intertissue Differences in the Heat Shock Response
3.5 Evolutionary, Interspecific Differences in the Heat Shock Response
3.6 Cellular Thermometers and Regulation of HSP Synthesis
3.7 Cold Shock May Induce Stress Proteins
4 Temperature Effects on Lipids and Membrane‐Localized Functions
4.1 Temperature Effects on Membrane Lipids: Changes in Phase and Fluidity
4.2 Membrane Fluidity and Compositional Changes Correlate With Effects on Membrane Functions
4.3 Homeoviscous Adaptation: Occurrence and Efficacy
4.4 Adaptation of Membrane Lipids: Regulation and Biophysical Effects
4.5 Adaptive Regulation of Depot and Membrane Lipid Fluidity in Hibernators
4.6 Membrane Lipids of Thermophilic Archaebacteria
4.7 Membrane Adaptations Involving Extrinsic Factors: pH and Solutes
4.8 Cuticular Waxes: Regulation of Body Temperature and Control of Water Loss
4.9 Evaporative Cooling in Insects
5 Temperature–pH Interactions
5.1 Temperature Dependence of Body Fluid pH Values
5.2 The Imidazole Alphastat Hypothesis
5.3 Functional Manifestations of the Advantages of Alphastat Regulation
5.4 Deviations from Alphastat Regulation in Small Mammalian Hibernators
5.5 Variation in Alpha Imidazole among Species, Tissues, Histidyl Residues, and Methodologies
6 Biogeographical Implications of Temperature Adaptation
Figure 1. Figure 1.

Thermal stabilities of orthologous homologs of four proteins. a: Lens crystallins . Species studied were (1) Pagothenia borchgrevinki (Antarctic fish), (2) Coryphaenoides armatus (deep‐sea fish), (3) Coryphaenoides rupestris (deep‐sea fish), (4) Oncorhynchus mykiss (rainbow trout), (5) Cebidichthys violaceus (tidepool fish), (6) Rana muscosa (frog), (7) Alticus kirkii (Red Sea fish), (8) Rana erythraea (frog), (9) Gekko gecko (lizard), (10) Rattus norwegicus, (11) Tropidurus hispidus (reptile), and (12) Dipsosaurus dorsalis (desert iguana). b: Skeletal muscle (alpha isoform) actin . c: M4 (A4) lactate dehydrogenase. Unfolding of the protein was monitored by quenching of protein fluorescence by acrylamide, which is able to penetrate the protein and quench fluorescing tryptophyl residues when the protein unfolds . d: Cytosolic malate dehydrogenase. Four species of abalone (genus Haliotis) are compared. Habitat ranges in parentheses. The first range is the entire biogeographic range in temperature; the second range encompasses temperatures where each species is commonly found: Haliotis fulgens (green abalone) (14°–27°C; 14°–23°C), H. corregata (pink abalone) (12°–23°C; 12°–20°C), H. cracherodii (black abalone) (12°–25°C; 12°–22°C), H. rufesens (red abalone) (8°–18°C; 8°–16°C), and H. kamtschatkana kamtschatkana (4°–14°C; 4°–9°C) .

Figure 2. Figure 2.

Effects of temperature on apparent Michaelis‐Menten constants for pyruvate (a) and reduced nicotinamide adenine dinucleotide (NADH) (b) for M4 (A4) lactate dehydrogenases of vertebrates adapted to different temperatures. a: Km of pyruvate. Pagothenia borchgrevinki, Cynocion striatus, Cynocion xanthulus, Gillichthys mirabilis, and Gillichthys seta are teleost fishes. Species' temperature ranges are shown in parentheses next to the species name.

Data from references , and G. N. Somero and E. Winter (G. mirabilis and G. seta) (unpublished data). b: Km of NADH. Figure modified after Yancey and Siebenaller . Dark line segments denote Km values at physiological temperatures. Dark vertical bar encompasses Km values for all species at physiological temperatures
Figure 3. Figure 3.

Effect of temperature on homologous dehydrogenases from congeneric species adapted to different temperatures, a: M4 ‐lactate dehydrogenases of four species of barracuda (genus Sphyraena). Dark line segments indicate Km values at physiological temperatures. Dark vertical bar encompasses Km values for all species at physiological temperatures. Figure modified after Graves and Somero . b: Km of NADH for cytosolic malate dehydrogenases of abalone congeners . Dark line segments and vertical bar indicate Km values at physiological temperatures. See legend to Figure for additional information on the thermal conditions of the aba‐lone congeners.

Figure 4. Figure 4.

Temperature effects on the enzyme acetylcholinesterase (AChE) from brain tissue of several fishes and the frequency of release of acetylcholine (ACh) quanta in the Antarctic fish Pagothenia borchgrevinki. Left: Effect of temperature on the rate of spontaneous release of ACh quanta at the neuromuscular junction of the extraocular nerve of P. borchgrevinki. Figure modified after MacDonald et al. . Right: Effect of temperature on the Km of ACh from brains of several teleost fishes.

Data from Baldwin and Baldwin and Hochachka
Figure 5. Figure 5.

Arrhenius plots of liver mitochondrial succinate:cytochrome c reductase activity for the homeothermic guinea pig, the heterothermic brown antechinus, and the heterothermic bent wing bat isolated during winter. Arrhenius activation energies in kilocalories per mole are given above line segments. Temperatures shown near discontinuities in slopes are Arrhenius break temperatures. Figure modified after Geiser and McMurchie .

Figure 6. Figure 6.

Effects of temperature on mitochondrial respiration and membrane fluidity. A: Arrhenius plot of oxygen consumption by mitochondria from the deep‐sea hydrothermal vent tube worm Riftia pachyptila, illustrating the discontinuity (“break”) in slope that occurs at an elevated temperature, the Arrhenius break temperature (ABT). Figure modified after Dahlhoff et al. . B: ABTs for respiration of mitochondria isolated from marine invertebrates adapted to different temperatures. Estimates of maximal habitat temperatures given on the abscissa. Study species included six hydrothermal vent species: R. pachyptila, the crab Bythograea thermydron, two polychaete worms of the genus Alvinella, a mussel (Bathymodiolus thermophilus), and the clam Calyptogena magnifica. Solemya reidi is a protobranch clam, and Mytilus galloprovincialis is a mussel.

Data from Dahlhoff et al. . C. Effect of acclimation temperature on the ABTs of mitochondrial respiration for four species of abalone: Haliotis fulgens (green), H. corregata (pink), H. rufesens (red), and H. kamtschatkana kamtschatkana (pinto). Figure modified after Dahlhoff and Somero . D: Effect of acclimation temperature on fluidity (inversely related to fluorescence polarization of 1,6‐diphenyl‐1,3,5‐hexatriene) of mitochondrial membranes of five species of abalone (H. cracherodii: black abalone). Figure modified after Dahlhoff and Somero . For environmental temperature ranges of the abalone species, see Figure
Figure 7. Figure 7.

Homeoviscous adaptation in synaptosomal membranes from brain tissue of vertebrates adapted to different temperatures. Membrane fluidity is inversely related to magnitude of 1,6‐diphenyl‐1,3,5‐hexatriene polarization. Broad line segments indicate polarization values within range of physiological temperatures of each species. Dark vertical bar at right shows range of polarization values at physiological temperatures for all six species. Figure modified after Cossins and Bowler and Behan‐Martin et al. .

Figure 8. Figure 8.

Changes in head group composition (phospholipid class) of phospholipids of rainbow trout gill during temperature acclimation. Top: Changes in weight percent of phosphatidylethanol‐amine (PE) during acclimation from 5°C to 20°C or from 20°C to 5°C. Middle: Changes in weight percent of phosphatidylcholine (PC). Bottom: Ratio of PC to PE during acclimation. Figure modified after Hazel and Carpenter .

Figure 9. Figure 9.

Effect of buffer composition on temperature dependence of fluorescence anisotropy parameters for plasma membranes from rainbow trout acclimated to 20°C. The anisotropy parameter is inversely related to membrane fluidity. In phosphate buffer, pH was almost independent of temperature, but in the imidazole buffer, pH varied with temperature according to the alphastat relationship. Figure modified from Hazel et al. .

Figure 10. Figure 10.

Effects of pH on binding of phosphofructokinase (PFK) to myofibrils (open symbols, dashed line) and interacting effects of pH and temperature on PFK self‐assembly, as indexed by residual PFK activity (closed symbols, solid lines). PFK binding to myofibrils measured using PFK‐containing supernatants and myofibrillar preparations from white skeletal muscle of the fish Paralabrax nebulifer . Incubations were at 20°C for 15 min. PFK self‐assembly was studied using enzyme purified from the ground squirrel Spermophilus beecheyi . Residual activity after incubation for 60 min at different combinations of temperature and pH reflects fraction of PFK remaining as catalytically active tetramers or aggregations of tetramers.



Figure 1.

Thermal stabilities of orthologous homologs of four proteins. a: Lens crystallins . Species studied were (1) Pagothenia borchgrevinki (Antarctic fish), (2) Coryphaenoides armatus (deep‐sea fish), (3) Coryphaenoides rupestris (deep‐sea fish), (4) Oncorhynchus mykiss (rainbow trout), (5) Cebidichthys violaceus (tidepool fish), (6) Rana muscosa (frog), (7) Alticus kirkii (Red Sea fish), (8) Rana erythraea (frog), (9) Gekko gecko (lizard), (10) Rattus norwegicus, (11) Tropidurus hispidus (reptile), and (12) Dipsosaurus dorsalis (desert iguana). b: Skeletal muscle (alpha isoform) actin . c: M4 (A4) lactate dehydrogenase. Unfolding of the protein was monitored by quenching of protein fluorescence by acrylamide, which is able to penetrate the protein and quench fluorescing tryptophyl residues when the protein unfolds . d: Cytosolic malate dehydrogenase. Four species of abalone (genus Haliotis) are compared. Habitat ranges in parentheses. The first range is the entire biogeographic range in temperature; the second range encompasses temperatures where each species is commonly found: Haliotis fulgens (green abalone) (14°–27°C; 14°–23°C), H. corregata (pink abalone) (12°–23°C; 12°–20°C), H. cracherodii (black abalone) (12°–25°C; 12°–22°C), H. rufesens (red abalone) (8°–18°C; 8°–16°C), and H. kamtschatkana kamtschatkana (4°–14°C; 4°–9°C) .



Figure 2.

Effects of temperature on apparent Michaelis‐Menten constants for pyruvate (a) and reduced nicotinamide adenine dinucleotide (NADH) (b) for M4 (A4) lactate dehydrogenases of vertebrates adapted to different temperatures. a: Km of pyruvate. Pagothenia borchgrevinki, Cynocion striatus, Cynocion xanthulus, Gillichthys mirabilis, and Gillichthys seta are teleost fishes. Species' temperature ranges are shown in parentheses next to the species name.

Data from references , and G. N. Somero and E. Winter (G. mirabilis and G. seta) (unpublished data). b: Km of NADH. Figure modified after Yancey and Siebenaller . Dark line segments denote Km values at physiological temperatures. Dark vertical bar encompasses Km values for all species at physiological temperatures


Figure 3.

Effect of temperature on homologous dehydrogenases from congeneric species adapted to different temperatures, a: M4 ‐lactate dehydrogenases of four species of barracuda (genus Sphyraena). Dark line segments indicate Km values at physiological temperatures. Dark vertical bar encompasses Km values for all species at physiological temperatures. Figure modified after Graves and Somero . b: Km of NADH for cytosolic malate dehydrogenases of abalone congeners . Dark line segments and vertical bar indicate Km values at physiological temperatures. See legend to Figure for additional information on the thermal conditions of the aba‐lone congeners.



Figure 4.

Temperature effects on the enzyme acetylcholinesterase (AChE) from brain tissue of several fishes and the frequency of release of acetylcholine (ACh) quanta in the Antarctic fish Pagothenia borchgrevinki. Left: Effect of temperature on the rate of spontaneous release of ACh quanta at the neuromuscular junction of the extraocular nerve of P. borchgrevinki. Figure modified after MacDonald et al. . Right: Effect of temperature on the Km of ACh from brains of several teleost fishes.

Data from Baldwin and Baldwin and Hochachka


Figure 5.

Arrhenius plots of liver mitochondrial succinate:cytochrome c reductase activity for the homeothermic guinea pig, the heterothermic brown antechinus, and the heterothermic bent wing bat isolated during winter. Arrhenius activation energies in kilocalories per mole are given above line segments. Temperatures shown near discontinuities in slopes are Arrhenius break temperatures. Figure modified after Geiser and McMurchie .



Figure 6.

Effects of temperature on mitochondrial respiration and membrane fluidity. A: Arrhenius plot of oxygen consumption by mitochondria from the deep‐sea hydrothermal vent tube worm Riftia pachyptila, illustrating the discontinuity (“break”) in slope that occurs at an elevated temperature, the Arrhenius break temperature (ABT). Figure modified after Dahlhoff et al. . B: ABTs for respiration of mitochondria isolated from marine invertebrates adapted to different temperatures. Estimates of maximal habitat temperatures given on the abscissa. Study species included six hydrothermal vent species: R. pachyptila, the crab Bythograea thermydron, two polychaete worms of the genus Alvinella, a mussel (Bathymodiolus thermophilus), and the clam Calyptogena magnifica. Solemya reidi is a protobranch clam, and Mytilus galloprovincialis is a mussel.

Data from Dahlhoff et al. . C. Effect of acclimation temperature on the ABTs of mitochondrial respiration for four species of abalone: Haliotis fulgens (green), H. corregata (pink), H. rufesens (red), and H. kamtschatkana kamtschatkana (pinto). Figure modified after Dahlhoff and Somero . D: Effect of acclimation temperature on fluidity (inversely related to fluorescence polarization of 1,6‐diphenyl‐1,3,5‐hexatriene) of mitochondrial membranes of five species of abalone (H. cracherodii: black abalone). Figure modified after Dahlhoff and Somero . For environmental temperature ranges of the abalone species, see Figure


Figure 7.

Homeoviscous adaptation in synaptosomal membranes from brain tissue of vertebrates adapted to different temperatures. Membrane fluidity is inversely related to magnitude of 1,6‐diphenyl‐1,3,5‐hexatriene polarization. Broad line segments indicate polarization values within range of physiological temperatures of each species. Dark vertical bar at right shows range of polarization values at physiological temperatures for all six species. Figure modified after Cossins and Bowler and Behan‐Martin et al. .



Figure 8.

Changes in head group composition (phospholipid class) of phospholipids of rainbow trout gill during temperature acclimation. Top: Changes in weight percent of phosphatidylethanol‐amine (PE) during acclimation from 5°C to 20°C or from 20°C to 5°C. Middle: Changes in weight percent of phosphatidylcholine (PC). Bottom: Ratio of PC to PE during acclimation. Figure modified after Hazel and Carpenter .



Figure 9.

Effect of buffer composition on temperature dependence of fluorescence anisotropy parameters for plasma membranes from rainbow trout acclimated to 20°C. The anisotropy parameter is inversely related to membrane fluidity. In phosphate buffer, pH was almost independent of temperature, but in the imidazole buffer, pH varied with temperature according to the alphastat relationship. Figure modified from Hazel et al. .



Figure 10.

Effects of pH on binding of phosphofructokinase (PFK) to myofibrils (open symbols, dashed line) and interacting effects of pH and temperature on PFK self‐assembly, as indexed by residual PFK activity (closed symbols, solid lines). PFK binding to myofibrils measured using PFK‐containing supernatants and myofibrillar preparations from white skeletal muscle of the fish Paralabrax nebulifer . Incubations were at 20°C for 15 min. PFK self‐assembly was studied using enzyme purified from the ground squirrel Spermophilus beecheyi . Residual activity after incubation for 60 min at different combinations of temperature and pH reflects fraction of PFK remaining as catalytically active tetramers or aggregations of tetramers.

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George N. Somero. Temperature Relationships: From Molecules to Biogeography. Compr Physiol 2011, Supplement 30: Handbook of Physiology, Comparative Physiology: 1391-1444. First published in print 1997. doi: 10.1002/cphy.cp130219