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Originally published In Press as doi:10.1074/jbc.M002030200 on March 20, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16597-16601, June 2, 2000
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Co-translational Folding of an Eukaryotic Multidomain Protein in a Prokaryotic Translation System*

Vyacheslav A. Kolb, Eugeny V. Makeyev, and Alexander S. SpirinDagger

From the Institute of Protein Research, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia

Continuous monitoring of the enzymatic activity of newly synthesized firefly luciferase in Escherichia coli cell-free translation system was performed to record folding kinetics of this multidomain eukaryotic protein in the prokaryotic cytosol. Whereas in vitro refolding of denatured luciferase in prokaryotic cytosol occurred with a low yield of active enzyme and took about an hour, the enzyme acquired its native structure immediately upon release from the ribosome, as seen from the immediate halt of active luciferase accumulation upon blocking of translation with inhibitors. The nascent luciferase was also capable of acquiring the active conformation prior to release from the ribosome, when its C terminus was extended with a polypeptide segment. Specific enzymatic activity of the firefly luciferase was found to be equally high irrespective of whether this protein was synthesized in eukaryotic or prokaryotic translation systems. The data presented demonstrate the fundamental ability of prokaryotic cytosol to support effective co-translational protein folding in general and co-translational folding of multidomain proteins in particular.

* This work was supported by Grant 96-15-97999 from the Russian Foundation for Fundamental Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel. and Fax: 7-095-924-0493; E-mail: spirin@vega.protres.ru.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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