Electrophoretic and Functional Enzymic Evolution in Four Species of Eastern Pacific Barracudas From Different Thermal Environments

Graves, John E.; Somero, George N.

doi:10.1111/j.1558-5646.1982.tb05014.x

Cited by 74 publications

(11 citation statements)

References 30 publications

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“…Nevertheless, at a minimum our comparative approach was successful in identifying structural changes that modify sHsp function in a predictable way. Our findings are also consistent with a history of studies that have identified strong adaptive effects of single or relatively few amino acid changes in proteins as diverse as hemoglobin [42], [43], sodium channels [44], lactate dehydrogenase [45], [46] and malate dehdrogenase [47].…”

Section: Discussionsupporting

confidence: 91%

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

et al. 2012

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Small heat shock proteins (sHsps) maintain cellular homeostasis by preventing stress and disease-induced protein aggregation. While it is known that hydrophobicity impacts the ability of sHsps to bind aggregation-prone denaturing proteins, the complex quaternary structure of globular sHsps has made understanding the significance of specific changes in hydrophobicity difficult. Here we used recombinant protein of the lenticular sHsp α A-crystallin from six teleost fishes environmentally adapted to temperatures ranging from -2°C to 40°C to identify correlations between physiological temperature, protein stability and chaperone-like activity. Using sequence and structural modeling analysis we identified specific amino acid differences between the warm adapted zebrafish and cold adapted Antarctic toothfish that could contribute to these correlations and validated the functional consequences of three specific hydrophobicity-altering amino acid substitutions in αA-crystallin. Site directed mutagenesis of three residues in the zebrafish (V62T, C143S, T147V) confirmed that each impacts either protein stability or chaperone-like activity or both, with the V62T substitution having the greatest impact. Our results indicate a role for changing hydrophobicity in the thermal adaptation of α A-crystallin and suggest ways to produce sHsp variants with altered chaperone-like activity. These data also demonstrate that a comparative approach can provide new information about sHsp function and evolution.

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Section: Discussionsupporting

confidence: 91%

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

et al. 2012

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“…The A1 receptors in vertebrates with widely different (Yancey and Somero, 1978;Graves and Somero, 1982;Hochachka and Somero, 1984;Yancey and Siebenaller, 1987). Conservation of Km, values, coupled with the similar in vivo substrate levels among species, results in the preservation of the regulatory and catalytic properties of the enzymes, and the sparing of cellular solvent capacity (e.g., discussion in Hochachka and Somero, 1984).…”

Section: Discussionmentioning

confidence: 99%

“…For example, in studies of homologs of M4-lactate dehydrogenase from species with cell temperatures of-2 to 47?C, the Km values of substrate and coenzyme are highly similar among species when measured at the Tb of the species, despite variation in Km values with measurement temperature (Yancey and Somero, 1978;Graves and Somero, 1982;Hochachka and Somero, 1984;Yancey and Siebenaller, 1987). Do these receptors retain a high affinity for agonists at the average body temperature (Tb) of the species?…”

Section: Introductionmentioning

confidence: 99%

Evolutionary Temperature Adaptation of Agonist Binding to the A₁Adenosine Receptor

Siebenaller

Murray

1988

The Biological Bulletin

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“…The outcome of evolutionary temperature adaptation is thus to render key aspects of organismal physiology moderately independent of cellular enthalpy: evolution has worked to overcome the tyranny of Boltzmann. (For the classic work in this area see Graves & Somero 1982; and Holland, McFall‐Ngai & Somero 1997; for a review of the field see Hochachka & Somero 2002.) These arguments are presented in more detail in Clarke (2004).…”

Section: Does Temperature Determine Resting Metabolic Rate Directly?mentioning

confidence: 99%

Why does metabolism scale with temperature?

2004

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Electrophoretic and Functional Enzymic Evolution in Four Species of Eastern Pacific Barracudas From Different Thermal Environments

Cited by 74 publications

References 30 publications

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

Evolutionary Temperature Adaptation of Agonist Binding to the A₁Adenosine Receptor

Why does metabolism scale with temperature?

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Electrophoretic and Functional Enzymic Evolution in Four Species of Eastern Pacific Barracudas From Different Thermal Environments

Cited by 74 publications

References 30 publications

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin

Evolutionary Temperature Adaptation of Agonist Binding to the A1Adenosine Receptor

Why does metabolism scale with temperature?

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Evolutionary Temperature Adaptation of Agonist Binding to the A₁Adenosine Receptor