Archaeal-like chaperonins in bacteria

Edited by Arthur L. Horwich, Yale University School of Medicine, New Haven, CT, and approved September 14, 2010 (received for review April 16, 2010)
November 5, 2010
107 (47) 20269-20274

Abstract

Chaperonins (CPN) are ubiquitous oligomeric protein machines that mediate the ATP-dependent folding of polypeptide chains. These chaperones have not only been assigned stress response and normal housekeeping functions but also have a role in certain human disease states. A longstanding convention divides CPNs into two groups that share many conserved sequence motifs but differ in both structure and distribution. Group I complexes are the well known GroEL/ES heat-shock proteins in bacteria, that also occur in some species of mesophilic archaea and in the endosymbiotic organelles of eukaryotes. Group II CPNs are found only in the cytosol of archaea and eukaryotes. Here we report a third, divergent group of CPNs found in several species of bacteria. We propose to name these Group III CPNs because of their distant relatedness to both Group I and II CPNs as well as their unique genomic context, within the hsp70 operon. The prototype Group III CPN, Carboxydothermus hydrogenoformans chaperonin (Ch-CPN), is able to refold denatured proteins in an ATP-dependent manner and is structurally similar to the Group II CPNs, forming a 16-mer with each subunit contributing to a flexible lid domain. The Group III CPN represent a divergent group of bacterial CPNs distinct from the GroEL/ES CPN found in all bacteria. The Group III lineage may represent an ancient horizontal gene transfer from an archaeon into an early Firmicute lineage. An analysis of their functional and structural characteristics may provide important insights into the early history of this ubiquitous family of proteins.

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Acknowledgments.

We thank Dr. Ru-Ching Hsia for assistance with operation of the Tecnai T12 Electron microscope. Dr. Travis Gallagher and Dr. Jane Ladner for assistance with Multiangle light scattering. We also thank Dr. Alberto Marcario and Dr. Everly Conway de Marcario for careful reading of the manuscript. This work was funded by Grants NSF EAR 65132 and AFOSR FA9550-07-1-0022 from the National Science Foundation and the Air Force Office of Scientific Research.

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Information & Authors

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Published in

Go to Proceedings of the National Academy of Sciences
Go to Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences
Vol. 107 | No. 47
November 23, 2010
PubMed: 21057109

Classifications

Submission history

Published online: November 5, 2010
Published in issue: November 23, 2010

Keywords

  1. evolution
  2. protein-folding
  3. thermophilic

Acknowledgments

We thank Dr. Ru-Ching Hsia for assistance with operation of the Tecnai T12 Electron microscope. Dr. Travis Gallagher and Dr. Jane Ladner for assistance with Multiangle light scattering. We also thank Dr. Alberto Marcario and Dr. Everly Conway de Marcario for careful reading of the manuscript. This work was funded by Grants NSF EAR 65132 and AFOSR FA9550-07-1-0022 from the National Science Foundation and the Air Force Office of Scientific Research.

Notes

This article is a PNAS Direct Submission.

Authors

Affiliations

Stephen M. Techtmann
Institute of Marine and Environmental Technology, Program in the Biology of Model Systems, 701 East Pratt Street, Baltimore, MD 21202 and Department of Microbiology and Immunology, University of Maryland School of Medicine, 685 West Baltimore Street, Baltimore, MD 21201
Present address: Department of Biochemistry and Molecular Biology, Uniformed Services University for the Health Science, 4301 Jones Bridge Road, Bethesda, MD 20814.
Frank T. Robb2 [email protected]
Institute of Marine and Environmental Technology, Program in the Biology of Model Systems, 701 East Pratt Street, Baltimore, MD 21202 and Department of Microbiology and Immunology, University of Maryland School of Medicine, 685 West Baltimore Street, Baltimore, MD 21201

Notes

2
To whom correspondence should be addressed. E-mail: [email protected].
Author contributions: S.M.T. and F.T.R. designed research; S.M.T. performed research; S.M.T. and F.T.R. analyzed data; and S.M.T. and F.T.R. wrote the paper.

Competing Interests

The authors declare no conflict of interest.

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    Archaeal-like chaperonins in bacteria
    Proceedings of the National Academy of Sciences
    • Vol. 107
    • No. 47
    • pp. 20145-20592

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