Trigger Factor Assists the Refolding of Heterodimeric but Not Monomeric Luciferases

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O. E. Melkina¹, I. I. Goryanin¹, I. V. Manukhov¹, A. V. Baranova², V. A. Kolb³, M. S. Svetlov³, and G. B. Zavilgelsky^1*

¹Research Institute for Genetics and Selection of Industrial Microorganisms (GosNIIGenetika), 1-yi Dorozhnyi Proezd 1, 117545 Moscow, Russia; fax: +7 (495) 315-0501; E-mail: zavilgel@genetika.ru

²School of Systems Biology, College of Science, George Mason University, Fairfax, VA, 22003, USA

³Institute of Protein Research, Russian Academy of Sciences, ul. Institutskaya 4, 142290 Pushchino, Moscow Region, Russia

^* To whom correspondence should be addressed.

Received September 2, 2013; Revision received October 1, 2013

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The refolding of thermally inactivated protein by ATP-independent trigger factor (TF) and ATP-dependent DnaKJE chaperones was comparatively analyzed. Heterodimeric (αβ) bacterial luciferases of Aliivibrio fischeri, Photobacterium leiognathi, and Vibrio harveyi as well as monomeric luciferases of Vibrio harveyi and Luciola mingrelica (firefly) were used as substrates. In the presence of TF, thermally inactivated heterodimeric bacterial luciferases refold, while monomeric luciferases do not refold. These observations were made both in vivo (Escherichia coli ΔdnaKJ containing plasmids with tig gene) and in vitro (purified TF). Unlike TF, the DnaKJE chaperone system refolds both monomeric and heterodimeric luciferases with equal efficiency.

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KEY WORDS: trigger factor, DnaKJE chaperone, luciferase, refolding

DOI: 10.1134/S000629791401009X

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