Purification and structural characterization of the thermosome from the 
hyperthermophilic archaeum methanopyrus kandleri

Andrä, S.; Frey, G.; Nitsch, M.; Baumeister, W.; Stetter, K. O.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Purification and structural characterization of the thermosome from the hyperthermophilic archaeum methanopyrus kandleri

MPS-Authors

There are no MPG-Authors in the publication available

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Andrä, S., Frey, G., Nitsch, M., Baumeister, W., & Stetter, K. O. (1996). Purification and structural characterization of the thermosome from the hyperthermophilic archaeum methanopyrus kandleri. FEBS Letters, 379(2), 127-131.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-72FB-A

Abstract

From Methanopyras kandleri, the most thermophilic methanogen known so far, we have purified to homogeneity a protein complex of high molecular mass. Image analysis of transmission electron micrographs revealed a barrel-shaped particle composed of two rings with 8-fold symmetry. Only one type of subunit could be detected, The corresponding gene has been cloned and sequenced. The deduced amino acid sequence shows high homology with the members of group II chaperonins. The structure of the projection and the sequence homology suggest that this particle is the first thermosome isolated from a methanogen. [References: 29]