Temperature adaptation

AccessScience ◽  
2015 ◽  
2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Changi Wong ◽  
Yee Soon Ling ◽  
Julia Lih Suan Wee ◽  
Aazani Mujahid ◽  
Moritz Müller

AbstractNepenthes, as the largest family of carnivorous plants, is found with an extensive geographical distribution throughout the Malay Archipelago, specifically in Borneo, Philippines, and Sumatra. Highland species are able to tolerate cold stress and lowland species heat stress. Our current understanding on the adaptation or survival mechanisms acquired by the different Nepenthes species to their climatic conditions at the phytochemical level is, however, limited. In this study, we applied an eco-metabolomics approach to identify temperature stressed individual metabolic fingerprints of four Nepenthes species: the lowlanders N. ampullaria, N. rafflesiana and N. northiana, and the highlander N. minima. We hypothesized that distinct metabolite regulation patterns exist between the Nepenthes species due to their adaptation towards different geographical and altitudinal distribution. Our results revealed not only distinct temperature stress induced metabolite fingerprints for each Nepenthes species, but also shared metabolic response and adaptation strategies. The interspecific responses and adaptation of N. rafflesiana and N. northiana likely reflected their natural habitat niches. Moreover, our study also indicates the potential of lowlanders, especially N. ampullaria and N. rafflesiana, to produce metabolites needed to deal with increased temperatures, offering hope for the plant genus and future adaption in times of changing climate.


Author(s):  
Kevin M. Johnson ◽  
Hollis R. Jones ◽  
Sandra M. Casas ◽  
Jerome F. La Peyre ◽  
Morgan W. Kelly

Aquaculture ◽  
1998 ◽  
Vol 167 (1-2) ◽  
pp. 85-94 ◽  
Author(s):  
M Emri ◽  
T Márián ◽  
L Trón ◽  
L Balkay ◽  
Z Krasznai

1991 ◽  
Vol 159 (1) ◽  
pp. 473-487 ◽  
Author(s):  
ELIZABETH DAHLHOFF ◽  
GEORGE N. SOMERO

Effects of temperature and hydrostatic pressure were measured on cytosolic malate dehydrogenases (cMDHs) from muscle tissue of a variety of shallow- and deep-living benthic marine invertebrates, including seven species endemic to the deep-sea hydrothermal vents. The apparent Michaelis-Menten constant (Km) of coenzyme (nicotinamide adenine dinucleotide, NADH), used to index temperature and pressure effects, was conserved within a narrow range (approximately 15–25 μmoll−1) at physiological temperatures and pressures for all species. However, at elevated pressures, the Km of NADH rose sharply for cMDHs of shallow species (depths of occurrence >Approximately 500 m), but not for the cMDHs of deep-sea species. Cytosolic MDHs of invertebrates from the deep-sea hydrothermal vents generally were not perturbed by elevated temperatures (15–25°C) at in situ pressures, but cMDHs of cold-adapted deep-sea species were. At a single measurement temperature, the Km of NADH for cMDHs from invertebrates from habitats with well-characterized temperatures was inversely related to maximal sustained body temperature. This correlation was used to predict the maximal sustained body temperatures of vent invertebrates for which maximal habitat and body temperatures are difficult to estimate. Species occurring on the ‘smoker chimneys’, which emit waters with temperatures up to 380°C, are predicted to have sustained body temperatures that are approximately 20–25°C higher than vent species living in cooler vent microhabitats. We conclude that, just as adaptation of enzymes to elevated pressures is important in establishing species’ depth distribution patterns, adaptation of pressure-adapted enzymes to temperature is critical in enabling certain vent species to exploit warm-water microhabitats in the vent environment.


Science ◽  
2021 ◽  
Vol 371 (6533) ◽  
pp. eaay2784
Author(s):  
Margaux M. Pinney ◽  
Daniel A. Mokhtari ◽  
Eyal Akiva ◽  
Filip Yabukarski ◽  
David M. Sanchez ◽  
...  

The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.


1972 ◽  
Vol 45 (3) ◽  
pp. 223-228 ◽  
Author(s):  
Ian A. McLaren ◽  
John M. Cooley

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