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Thermostable chaperonin from Clostridium thermocellum

Cross, S.J., Ciruela, Antonio, Poomputsa, K., Romaniec, Marek P.M., Freedman, Robert B. (1996) Thermostable chaperonin from Clostridium thermocellum. Biochemical Journal, 316 . pp. 615-622. ISSN 0264-6021. (doi:10.1042/bj3160615) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:18900)

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Homologues of the chaperonins Cpn60 and Cpn10 have been purified from the Gram-positive cellulolytic thermophile Clostridium thermocellum. The Cpn60 protein was purified by ATP-affinity chromatography and the Cpn10 protein was purified by gel-filtration, ion-exchange and hydrophobic interaction chromatographies. The identities of the proteins were confirmed by N-terminal sequence analysis and antigenic cross-reactivity. The Cpn60 homologue is a weak, thermostable ATPase (t(1/2) at 70 degrees C more than 90 min) with optimum activity (k(cat) 0.07 s(-1)) between 60 degrees C and 70 degrees C. The ATPase activity of the authentic Cpn60 was inhibited by Escherichia coli GroES. The catalytic properties of a recombinant C. thermocellum Cpn60 purified from a GST-Cpn60 fusion protein expressed in E. coli [Ciruela (1995) Ph.D. Thesis, University of Kent] were identical with those of the authentic C. thermocellum Cpn60. Gel-filtration studies show that at room temperature the Cpn60 migrates mainly as a heptamer. Electron microscopy confirms the presence of complexes showing 7-fold rotational symmetry and also reveals a small number of particles that seem to be tetradecamers with a similar structure to E. coli GroEL complexes.

Item Type: Article
DOI/Identification number: 10.1042/bj3160615
Additional information: Part: Part 2
Subjects: Q Science
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: M.A. Ziai
Date Deposited: 14 May 2009 19:44 UTC
Last Modified: 09 Mar 2023 11:31 UTC
Resource URI: (The current URI for this page, for reference purposes)

University of Kent Author Information

Freedman, Robert B..

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