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J. Biol. Chem., Vol. 280, Issue 14, 13315-13320, April 8, 2005

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Dimeric Trigger Factor Stably Binds Folding-competent Intermediates and Cooperates with the DnaK-DnaJ-GrpE Chaperone System to Allow Refolding^*

Chuan-Peng Liu, Sarah Perrett, and Jun-Mei Zhou

From the National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China

Trigger factor (TF) is the first chaperone encountered by the nascent chain in bacteria and forms a stoichiometric complex with the ribosome. However, the functional significance of the high cytosolic concentration of uncomplexed TF, the majority of which is dimeric, is unknown. To gain insight into TF function, we investigated the TF concentration dependence of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH) reactivation yield in the presence and absence of the DnaK-DnaJ-GrpE chaperone system in vitro. Cross-linking results indicate that the observed decrease in the reactivation yield of GAPDH at high concentrations of TF is due to the formation of a stable complex between TF dimer and GAPDH intermediates. In the absence of TF, or at low TF concentrations, the DnaK-DnaJ-GrpE chaperone system had negligible effect on the GAPDH refolding yield. However, GAPDH intermediates bound and held by dimeric TF could be specifically rescued by the DnaK-DnaJ-GrpE chaperone system in an ATP-dependent manner. This indicates the potential of TF, in its dimeric form, to act as a binding chaperone, maintaining non-native proteins in a refolding competent conformation and cooperating with downstream molecular chaperones to facilitate post-translational or post-stress protein folding.

Received for publication, December 16, 2004 , and in revised form, December 29, 2004.

^* This work was supported in part by the 973 Project of the Chinese Ministry of Science and Technology (G1999075608), the Chinese National Natural Science Foundation (30070163, 30470363), and a CAS Knowledge Innovation Grant (KSCX2-SW214-3). 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.

To whom correspondence should be addressed. Tel.: 86-10-64889859; Fax: 86-10-64840672; E-mail: zhoujm{at}sun5.ibp.ac.cn.

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