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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2015: 2.710
Rank 142 out of 289 in category Biochemistry & Molecular Biology in the 2015 Thomson Reuters Journal Citation Report/Science Edition

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Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

Online
ISSN
1437-4315
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Volume 380, Issue 1 (Jan 1999)

Issues

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
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.1999.007

Abstract

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.

About the article

Published Online: 2005-06-01

Published in Print: 1999-01-04


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.1999.007. Export Citation

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