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J. Biol. Chem., Vol. 282, Issue 9, 6372-6379, March 2, 2007

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Electrostatic Association of Glutathione Transferase to the Nuclear Membrane

EVIDENCE OF AN ENZYME DEFENSE BARRIER AT THE NUCLEAR ENVELOPE^*

Lorenzo Stella, Valentina Pallottini, Sandra Moreno, Silvia Leoni^¶, Francesca De Maria, Paola Turella, Giorgio Federici^||, Raffaele Fabrini, Kutayba F. Dawood, Mario Lo Bello^**, Jens Z. Pedersen^**, and Giorgio Ricci¹

From the Departments of Chemical Sciences and Technologies and ^**Biology, University of Rome "Tor Vergata," 00133 Rome, the Department of Biology, University of Rome "Roma Tre," 00146 Rome, ^¶Department of Cellular and Developmental Biology, University of Rome "La Sapienza," 00185 Rome, ^||Children's Hospital "Bambin Gesù," 00165 Rome, and Department of Internal Medicine, University of Rome "Tor Vergata", 00133 Rome, Italy

The possible nuclear compartmentalization of glutathione S-transferase (GST) isoenzymes has been the subject of contradictory reports. The discovery that the dinitrosyl-diglutathionyl-iron complex binds tightly to Alpha class GSTs in rat hepatocytes and that a significant part of the bound complex is also associated with the nuclear fraction (Pedersen, J. Z., De Maria, F., Turella, P., Federici, G., Mattei, M., Fabrini, R., Dawood, K. F., Massimi, M., Caccuri, A. M., and Ricci, G. (2007) J. Biol. Chem. 282, 6364–6371) prompted us to reconsider the nuclear localization of GSTs in these cells. Surprisingly, we found that a considerable amount of GSTs corresponding to 10% of the cytosolic pool is electrostatically associated with the outer nuclear membrane, and a similar quantity is compartmentalized inside the nucleus. Mainly Alpha class GSTs, in particular GSTA1-1, GSTA2-2, and GSTA3-3, are involved in this double modality of interaction. Confocal microscopy, immunofluorescence experiments, and molecular modeling have been used to detail the electrostatic association in hepatocytes and liposomes. A quantitative analysis of the membrane-bound Alpha GSTs suggests the existence of a multilayer assembly of these enzymes at the outer nuclear envelope that could represent an amazing novelty in cell physiology. The interception of potentially noxious compounds to prevent DNA damage could be the possible physiological role of the perinuclear and intranuclear localization of Alpha GSTs.

Received for publication, October 23, 2006 , and in revised form, December 29, 2006.

^* 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.

¹ To whom correspondence should be addressed: Dept. of Chemical Sciences and Technologies, University of Rome "Tor Vergata," Via della Ricerca Scientifica, 00133 Rome, Italy. Tel.: 39-0672594379; E-mail: riccig{at}uniroma2.it.

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