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J. Biol. Chem., Vol. 280, Issue 11, 10189-10195, March 18, 2005

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Resurrecting the Ancestral Enzymatic Role of a Modulatory Subunit^*

Miguel A. Ballicora, Jennifer R. Dubay, Claire H. Devillers, and Jack Preiss

From the Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824

In the post-genomic era, functional prediction of genes is largely based on sequence similarity searches, but sometimes the homologues bear different roles because of evolutionary adaptations. For instance, the existence of enzyme and non-enzyme homologues poses a difficult case for function prediction and the extent of this phenomenon is just starting to be surveyed. Different evolutionary paths are theoretically possible for the loss or acquisition of enzyme function. Here we studied the ancestral role of a model non-catalytic modulatory subunit. With a rational approach, we "resurrected" enzymatic activity from that subunit to experimentally prove that it derived from a catalytic ancestor. We show that this protein (L subunit ADP-glucose pyrophosphorylase) evolved to have a regulatory role, losing catalytic residues more than 130 million years ago, but preserving, possibly as a by-product, the substrate site architecture. Inactivation of catalytic subunits could be the consequence of a general evolutionary strategy to explore new regulatory roles in hetero-oligomers.

Received for publication, December 1, 2004 , and in revised form, January 3, 2005.

^* This work was supported by a Department of Energy Research grant and a Northern Regional United States Department of Agriculture grant. 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 supplemental Fig. 1 and Table I.

This article was selected as a Paper of the Week.

Present address: Alcimed Co., 84 boulevard Vivier Merle, 69485 Lyon cedex 03, France.

To whom correspondence should be addressed. Tel.: 517-353-3137; Fax: 517-353-9334; E-mail: preiss{at}msu.edu.

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