Group II Chaperonin in a Thermophilic Methanogen,Methanococcus thermolithotrophicus
نویسندگان
چکیده
منابع مشابه
Crystal structure of group II chaperonin in the open state.
Thermosomes are group II chaperonins responsible for protein refolding in an ATP-dependent manner. Little is known regarding the conformational changes of thermosomes during their functional cycle due to a lack of high-resolution structure in the open state. Here, we report the first complete crystal structure of thermosome (rATcpnβ) in the open state from Acidianus tengchongensis. There is a ∼...
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Elevated hydrostatic pressure has been shown to affect the growth rate of the thermophilic methanobacterium Methanococcus thermolithotrophicus without extending its temperature range of viability. Analysis of the cell inventory after approximately 10 h of incubation at 65 degrees C and 50 MPa (applying high-pressure liquid chromatography and two-dimensional gel electrophoresis) proved that pres...
متن کاملIntracellular localization of a group II chaperonin indicates a membrane-related function.
Chaperonins are protein complexes that are believed to function as part of a protein folding system in the cytoplasm of the cell. We observed, however, that the group II chaperonins known as rosettasomes in the hyperthermophilic archaeon Sulfolobus shibatae, are not cytoplasmic but membrane associated. This association was observed in cultures grown at 60 degrees C and 76 degrees C or heat-shoc...
متن کاملSingle-Molecule Fluorescence Polarization Study of Conformational Change in Archaeal Group II Chaperonin
Group II chaperonins found in archaea and in eukaryotic cytosol mediate protein folding without a GroES-like cofactor. The function of the cofactor is substituted by the helical protrusion at the tip of the apical domain, which forms a built-in lid on the central cavity. Although many studies on the change in lid conformation coupled to the binding and hydrolysis of nucleotides have been conduc...
متن کاملReplacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis
UNLABELLED Chaperonins are required for correct folding of many proteins. They exist in two phylogenetic groups: group I, found in bacteria and eukaryotic organelles, and group II, found in archaea and eukaryotic cytoplasm. The two groups, while homologous, differ significantly in structure and mechanism. The evolution of group II chaperonins has been proposed to have been crucial in enabling t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1998
ISSN: 0021-9258
DOI: 10.1074/jbc.273.43.28399