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J. Biol. Chem., Vol. 279, Issue 16, 16223-16228, April 16, 2004

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T-complex Polypeptide-1 Interacts with the Erythrocyte Cytoskeleton in Response to Elevated Temperatures^*

Christopher T. Wagner, Irene Y. Lu, Michael H. Hoffman, Wendell Q. Sun, Jonathan D. Trent¶, and Jerome Connor

From the LifeCell Corporation, Branchburg, New Jersey 08876 and the ^¶Astrobiology and Technology Branch, NASA Ames Research Center, Moffett Field, California 94035

Chaperonins are double ring complexes composed of highly conserved 60-kDa protein subunits that are divided into two subgroups. Group II chaperonins are found in archaea and the cytoplasm of eukarya and are believed to function like other chaperonins as part of a protein folding system. We report here that human erythrocytes contain the group II chaperonin T-complex polypeptide 1 (TCP-1) and that this complex translocates from the cytoplasm to the cytoskeleton in response to heat treatment in the absence of overt cell damage. Identification as TCP-1 was determined by immunodetection for TCP-1 and corroborated by mass spectroscopy peptide sequencing. Direct visualization by immunofluorescence confirmed peripherally localized TCP-1 in response to heat treatment. Temperatures ranging from 37–50 °C were demonstrated to have distinct kinetic profiles of induced translocation. Heat-induced binding was shown by Triton shell analysis to be specifically associated with the cytoskeletal proteins. Furthermore, the binding was reversible following removal of the stimulatory condition. A stabilizing process is hypothesized based on the known interactions of chaperonins.

Received for publication, September 29, 2003 , and in revised form, January 6, 2004.

^* This work was supported by a grant from the Defense Advanced Research Project Agency, Defense Sciences Office-Metabolic Engineering Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains two-dimensional analysis and additional information.

To whom correspondence should be addressed: LifeCell Corp., One Millennium Way, Branchburg, NJ 08876. Tel.: 908-947-1100; Fax: 908-947-1085; E-mail: cwagner{at}lifecell.com.

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