Jump to ContentJump to Main Navigation
Show Summary Details

Buchner, Johannes

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

See all formats and pricing



Select Volume and Issue


The Recombinant Thermosome from the Hyperthermophilic Archaeon Methanopyrus kandleri: In Vitro Analysis of Its Chaperone Activity

T. Minuth / M. Henn / K. Rutkat / S. Andrä / G. Frey / R. Rachel / K.O. Stetter / R. Jaenicke

Citation Information: Biological Chemistry. Volume 380, Issue 1, Pages 55–62, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.1999.007, June 2005

Publication History

Published Online:


The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains a chaperonin (thermosome) which represents a 951 kDa homo-hexadecameric protein complex with NH4 +-dependent ATPase activity. Since its synthesis is not increased upon heat shock, we set out to test its chaperone function.

In order to obtain the chaperonin in amounts sufficient for functional investigations, the gene encoding the 60 kDa subunit was expressed in E. coli BL21(DE3) cells. Purification yielded soluble, high-molecularmass double-ring complexes, indistinguishable from the natural thermosome. In order to study the functional properties of the recombinant protein complex, pig citrate synthase, yeast alcohol dehydrogenase, yeast α-glucosidase, bovine insulin, and Thermotoga phosphoglycerate kinase were used as model substrates.

The results demonstrate that the recombinant M. kandleri thermosome possesses a chaperone-like activity in vitro, inhibiting aggregation as the major off-pathway-reaction during thermal unfolding and refolding of proteins after chemical denaturation. However, the chaperonin only forms dead-end complexes with its non-native substrates, no release is detectable at temperatures between 25 and 60 °C.

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Irina Gutsche, Lars-Oliver Essen, and Wolfgang Baumeister
Journal of Molecular Biology, 1999, Volume 293, Number 2, Page 295
Irina Gutsche, Oana Mihalache, and Wolfgang Baumeister
Journal of Molecular Biology, 2000, Volume 300, Number 1, Page 187
Jiro Kohda, Tadanori Yamada, Takao Yoshida, Tadashi Maruyama, Masafumi Yohda, Hideki Fukuda, and Akihiko Kondo
Biochemical Engineering Journal, 2004, Volume 18, Number 1, Page 73
Lisa M. Bergeron, Cecilia Lee, Talar Tokatlian, Volker Höllrigl, and Douglas S. Clark
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2008, Volume 1784, Number 2, Page 368
Li Wang, Zhong-jun Hu, Yuan-ming Luo, Yan-wu Huo, Qing Ma, Yong-zhi He, Yu-ying Zhang, Fei Sun, and Zhi-yang Dong
Biochemical and Biophysical Research Communications, 2010, Volume 393, Number 2, Page 228
Rainer Jaenicke
Journal of Biotechnology, 2000, Volume 79, Number 3, Page 193
Stefan Steinbacher and Lars Ditzel
Journal of Structural Biology, 2001, Volume 135, Number 2, Page 147
Eun-Jung Shin, Jin-Woo Lee, Jeong-Hwan Kim, Jae Hyung Lee, Young-Tae Kim, Sung-Jong Jeon, Yeon-Hee Kim, and Soo-Wan Nam
Biotechnology and Bioprocess Engineering, 2009, Volume 14, Number 6, Page 702
Tillmann Burghardt, Manfred Saller, Sonja Gürster, Daniel Müller, Carolin Meyer, Ulrike Jahn, Eduard Hochmuth, Rainer Deutzmann, Frank Siedler, Patrick Babinger, Reinhard Wirth, Harald Huber, and Reinhard Rachel
Archives of Microbiology, 2008, Volume 190, Number 3, Page 379

Comments (0)

Please log in or register to comment.