Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens
Low-temperature-adapted archaea are abundant in the environment, yet little is known about the thermal adaptation of their proteins. We have previously compared elongation factor 2 (EF-2) proteins from Antarctic (Methanococcoides burtonii) and thermophilic (Methanosarcina thermophila) methanogens an...
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ftpubmed:oai:pubmedcentral.nih.gov:95092 2023-05-15T13:55:23+02:00 Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens Thomas, Torsten Kumar, Naresh Cavicchioli, Ricardo 2001-03 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95092 http://www.ncbi.nlm.nih.gov/pubmed/11222595 https://doi.org/10.1128/JB.183.6.1974-1982.2001 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95092 http://www.ncbi.nlm.nih.gov/pubmed/11222595 http://dx.doi.org/10.1128/JB.183.6.1974-1982.2001 Copyright © 2001, American Society for Microbiology Enzymes and Proteins Text 2001 ftpubmed https://doi.org/10.1128/JB.183.6.1974-1982.2001 2013-08-29T09:30:29Z Low-temperature-adapted archaea are abundant in the environment, yet little is known about the thermal adaptation of their proteins. We have previously compared elongation factor 2 (EF-2) proteins from Antarctic (Methanococcoides burtonii) and thermophilic (Methanosarcina thermophila) methanogens and found that the M. burtonii EF-2 had greater intrinsic activity at low temperatures and lower thermal stability at high temperatures (T. Thomas and R. Cavicchioli, J. Bacteriol. 182:1328–1332, 2000). While the gross thermal properties correlated with growth temperature, the activity and stability profiles of the EF-2 proteins did not precisely match the optimal growth temperature of each organism. This indicated that intracellular components may affect the thermal characteristics of the EF-2 proteins, and in this study we examined the effects of ribosomes and intracellular solutes. At a high growth temperature the thermophile produced high levels of potassium glutamate, which, when assayed in vitro with EF-2, retarded thermal unfolding and increased catalytic efficiency. In contrast, for the Antarctic methanogen adaptation to growth at a low temperature did not involve the accumulation of stabilizing organic solutes but appeared to result from an increased affinity of EF-2 for GTP and high levels of EF-2 in the cell relative to its low growth rate. Furthermore, ribosomes greatly stimulated GTPase activity and moderately stabilized both EF-2 proteins. These findings illustrate the different physiological strategies that have evolved in two phylogenetically related but thermally distinct methanogens to enable EF-2 to function satisfactorily. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic Journal of Bacteriology 183 6 1974 1982 |
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English |
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Enzymes and Proteins |
spellingShingle |
Enzymes and Proteins Thomas, Torsten Kumar, Naresh Cavicchioli, Ricardo Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
topic_facet |
Enzymes and Proteins |
description |
Low-temperature-adapted archaea are abundant in the environment, yet little is known about the thermal adaptation of their proteins. We have previously compared elongation factor 2 (EF-2) proteins from Antarctic (Methanococcoides burtonii) and thermophilic (Methanosarcina thermophila) methanogens and found that the M. burtonii EF-2 had greater intrinsic activity at low temperatures and lower thermal stability at high temperatures (T. Thomas and R. Cavicchioli, J. Bacteriol. 182:1328–1332, 2000). While the gross thermal properties correlated with growth temperature, the activity and stability profiles of the EF-2 proteins did not precisely match the optimal growth temperature of each organism. This indicated that intracellular components may affect the thermal characteristics of the EF-2 proteins, and in this study we examined the effects of ribosomes and intracellular solutes. At a high growth temperature the thermophile produced high levels of potassium glutamate, which, when assayed in vitro with EF-2, retarded thermal unfolding and increased catalytic efficiency. In contrast, for the Antarctic methanogen adaptation to growth at a low temperature did not involve the accumulation of stabilizing organic solutes but appeared to result from an increased affinity of EF-2 for GTP and high levels of EF-2 in the cell relative to its low growth rate. Furthermore, ribosomes greatly stimulated GTPase activity and moderately stabilized both EF-2 proteins. These findings illustrate the different physiological strategies that have evolved in two phylogenetically related but thermally distinct methanogens to enable EF-2 to function satisfactorily. |
format |
Text |
author |
Thomas, Torsten Kumar, Naresh Cavicchioli, Ricardo |
author_facet |
Thomas, Torsten Kumar, Naresh Cavicchioli, Ricardo |
author_sort |
Thomas, Torsten |
title |
Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
title_short |
Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
title_full |
Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
title_fullStr |
Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
title_full_unstemmed |
Effects of Ribosomes and Intracellular Solutes on Activities and Stabilities of Elongation Factor 2 Proteins from Psychrotolerant and Thermophilic Methanogens |
title_sort |
effects of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
publisher |
American Society for Microbiology |
publishDate |
2001 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95092 http://www.ncbi.nlm.nih.gov/pubmed/11222595 https://doi.org/10.1128/JB.183.6.1974-1982.2001 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC95092 http://www.ncbi.nlm.nih.gov/pubmed/11222595 http://dx.doi.org/10.1128/JB.183.6.1974-1982.2001 |
op_rights |
Copyright © 2001, American Society for Microbiology |
op_doi |
https://doi.org/10.1128/JB.183.6.1974-1982.2001 |
container_title |
Journal of Bacteriology |
container_volume |
183 |
container_issue |
6 |
container_start_page |
1974 |
op_container_end_page |
1982 |
_version_ |
1766262004330266624 |