Publication:
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens
dc.contributor.author | Thomas, Torsten | en_US |
dc.contributor.author | Kumar, N | en_US |
dc.contributor.author | Cavicchioli, R | en_US |
dc.date.accessioned | 2021-11-25T13:24:21Z | |
dc.date.available | 2021-11-25T13:24:21Z | |
dc.date.issued | 2001 | en_US |
dc.description.abstract | 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. | en_US |
dc.identifier.uri | http://hdl.handle.net/1959.4/39564 | |
dc.language | English | |
dc.language.iso | EN | en_US |
dc.rights | CC BY-NC-ND 3.0 | en_US |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/3.0/au/ | en_US |
dc.source | Legacy MARC | en_US |
dc.title | Effect of ribosomes and intracellular solutes on activities and stabilities of elongation factor 2 proteins from psychrotolerant and thermophilic methanogens | en_US |
dc.type | Journal Article | en |
dcterms.accessRights | metadata only access | |
dspace.entity.type | Publication | en_US |
unsw.accessRights.uri | http://purl.org/coar/access_right/c_14cb | |
unsw.identifier.doiPublisher | http://dx.doi.org/10.1128/JB.183.6.1974-1982.2001 | en_US |
unsw.relation.faculty | Science | |
unsw.relation.ispartofissue | 6 | en_US |
unsw.relation.ispartofjournal | Journal of Bacteriology | en_US |
unsw.relation.ispartofpagefrompageto | 1974-1982 | en_US |
unsw.relation.ispartofvolume | 183 | en_US |
unsw.relation.originalPublicationAffiliation | Thomas, Torsten, Biotechnology & Biomolecular Sciences, Faculty of Science, UNSW | en_US |
unsw.relation.originalPublicationAffiliation | Kumar, N | en_US |
unsw.relation.originalPublicationAffiliation | Cavicchioli, R | en_US |
unsw.relation.school | School of Biotechnology & Biomolecular Sciences | * |