Effect 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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ftunswworks:oai:unsworks.library.unsw.edu.au:1959.4/39564 2023-05-15T13:52:09+02:00 Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens Thomas, Torsten Kumar, N Cavicchioli, R 2001 http://hdl.handle.net/1959.4/39564 https://doi.org/10.1128/JB.183.6.1974-1982.2001 EN eng http://hdl.handle.net/1959.4/39564 http://dx.doi.org/10.1128/JB.183.6.1974-1982.2001 metadata only access http://purl.org/coar/access_right/c_14cb CC BY-NC-ND 3.0 https://creativecommons.org/licenses/by-nc-nd/3.0/au/ CC-BY-NC-ND Journal of Bacteriology, 183, 6, 1974-1982 journal article http://purl.org/coar/resource_type/c_6501 2001 ftunswworks https://doi.org/10.1128/JB.183.6.1974-1982.2001 2022-08-09T07:39:35Z 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. Article in Journal/Newspaper Antarc* Antarctic UNSW Sydney (The University of New South Wales): UNSWorks Antarctic The Antarctic Journal of Bacteriology 183 6 1974 1982 |
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Open Polar |
collection |
UNSW Sydney (The University of New South Wales): UNSWorks |
op_collection_id |
ftunswworks |
language |
English |
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 |
Article in Journal/Newspaper |
author |
Thomas, Torsten Kumar, N Cavicchioli, R |
spellingShingle |
Thomas, Torsten Kumar, N Cavicchioli, R Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
author_facet |
Thomas, Torsten Kumar, N Cavicchioli, R |
author_sort |
Thomas, Torsten |
title |
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
title_short |
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
title_full |
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
title_fullStr |
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
title_full_unstemmed |
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
title_sort |
effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens |
publishDate |
2001 |
url |
http://hdl.handle.net/1959.4/39564 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_source |
Journal of Bacteriology, 183, 6, 1974-1982 |
op_relation |
http://hdl.handle.net/1959.4/39564 http://dx.doi.org/10.1128/JB.183.6.1974-1982.2001 |
op_rights |
metadata only access http://purl.org/coar/access_right/c_14cb CC BY-NC-ND 3.0 https://creativecommons.org/licenses/by-nc-nd/3.0/au/ |
op_rightsnorm |
CC-BY-NC-ND |
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_ |
1766256414601248768 |