Molecular mechanisms of temperature adaptation in fish myofibrillar adenosine triphosphatases

1977 ◽  
Vol 119 (2) ◽  
pp. 195-206 ◽  
Author(s):  
Ian A. Johnston ◽  
N. J. Walesby
Keyword(s):  
Molecular Mechanisms ◽  
Temperature Adaptation ◽  
Adenosine Triphosphatases

Parallel molecular mechanisms for enzyme temperature adaptation

Science ◽  
2021 ◽  
Vol 371 (6533) ◽  
pp. eaay2784
Author(s):  
Margaux M. Pinney ◽  
Daniel A. Mokhtari ◽  
Eyal Akiva ◽  
Filip Yabukarski ◽  
David M. Sanchez ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Interaction Networks ◽  
Temperature Adaptation ◽  
Mechanistic Studies ◽  
Sequence Analyses ◽  
Evolutionary Mechanisms ◽  
Ketosteroid Isomerase ◽  
Physical Mechanisms ◽  
Bacterial Enzyme ◽  
Enzyme Families

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.

scholarly journals The advantage of channeling nucleotides for very processive functions

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 724 ◽  
Author(s):  
Diana Zala ◽  
Uwe Schlattner ◽  
Thomas Desvignes ◽  
Julien Bobe ◽  
Aurélien Roux ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Molecular Mechanisms ◽  
Nucleoside Triphosphate ◽  
High Turnover ◽  
Physiological Importance ◽  
Adenosine Triphosphatases ◽  
Close Proximity ◽  
Nucleoside Diphosphate Kinases ◽  
Very High

Nucleoside triphosphate (NTP)s, like ATP (adenosine 5’-triphosphate) and GTP (guanosine 5’-triphosphate), have long been considered sufficiently concentrated and diffusible to fuel all cellular ATPases (adenosine triphosphatases) and GTPases (guanosine triphosphatases) in an energetically healthy cell without becoming limiting for function. However, increasing evidence for the importance of local ATP and GTP pools, synthesised in close proximity to ATP- or GTP-consuming reactions, has fundamentally challenged our view of energy metabolism. It has become evident that cellular energy metabolism occurs in many specialised ‘microcompartments’, where energy in the form of NTPs is transferred preferentially from NTP-generating modules directly to NTP-consuming modules. Such energy channeling occurs when diffusion through the cytosol is limited, where these modules are physically close and, in particular, if the NTP-consuming reaction has a very high turnover, i.e. is very processive. Here, we summarise the evidence for these conclusions and describe new insights into the physiological importance and molecular mechanisms of energy channeling gained from recent studies. In particular, we describe the role of glycolytic enzymes for axonal vesicle transport and nucleoside diphosphate kinases for the functions of dynamins and dynamin-related GTPases.

scholarly journals Fungal Dimorphism and Virulence: Molecular Mechanisms for Temperature Adaptation, Immune Evasion, and In Vivo Survival

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Gregory M. Gauthier
Keyword(s):  
Phase Transition ◽  
Immune Evasion ◽  
Molecular Mechanisms ◽  
Temperature Adaptation ◽  
Dimorphic Fungi ◽  
Fungal Dimorphism ◽  
Recent Advances ◽  
Immune Defenses ◽  
Yeast Phase

The thermally dimorphic fungi are a unique group of fungi within the Ascomycota phylum that respond to shifts in temperature by converting between hyphae (22–25°C) and yeast (37°C). This morphologic switch, known as the phase transition, defines the biology and lifestyle of these fungi. The conversion to yeast within healthy and immunocompromised mammalian hosts is essential for virulence. In the yeast phase, the thermally dimorphic fungi upregulate genes involved with subverting host immune defenses. This review highlights the molecular mechanisms governing the phase transition and recent advances in how the phase transition promotes infection.

scholarly journals Molecular mechanisms of temperature adaptation

2015 ◽  
Vol 593 (16) ◽  
pp. 3483-3491 ◽  
Author(s):  
Sviatoslav N. Bagriantsev ◽  
Elena O. Gracheva
Keyword(s):  
Molecular Mechanisms ◽  
Temperature Adaptation

scholarly journals The advantage of channeling nucleotides for very processive functions

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 724 ◽  
Author(s):  
Diana Zala ◽  
Uwe Schlattner ◽  
Thomas Desvignes ◽  
Julien Bobe ◽  
Aurélien Roux ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Molecular Mechanisms ◽  
Nucleoside Triphosphate ◽  
High Turnover ◽  
Physiological Importance ◽  
Adenosine Triphosphatases ◽  
Close Proximity ◽  
Nucleoside Diphosphate Kinases ◽  
Very High

Nucleoside triphosphate (NTP)s, like ATP (adenosine 5’-triphosphate) and GTP (guanosine 5’-triphosphate), have long been considered sufficiently concentrated and diffusible to fuel all cellular ATPases (adenosine triphosphatases) and GTPases (guanosine triphosphatases) in an energetically healthy cell without becoming limiting for function. However, increasing evidence for the importance of local ATP and GTP pools, synthesised in close proximity to ATP- or GTP-consuming reactions, has fundamentally challenged our view of energy metabolism. It has become evident that cellular energy metabolism occurs in many specialised ‘microcompartments’, where energy in the form of NTPs is transferred preferentially from NTP-generating modules directly to NTP-consuming modules. Such energy channeling occurs when diffusion through the cytosol is limited, where these modules are physically close and, in particular, if the NTP-consuming reaction has a very high turnover,i.e. is very processive. Here, we summarise the evidence for these conclusions and describe new insights into the physiological importance and molecular mechanisms of energy channeling gained from recent studies. In particular, we describe the role of glycolytic enzymes for axonal vesicle transport and nucleoside diphosphate kinases for the functions of dynamins and dynamin-related GTPases.

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