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Volume 272, Number 5, Issue of January 31, 1997 pp. 3016-3021
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Quaternary Associations of Acetylcholinesterase
II. THE POLYPROLINE ATTACHMENT DOMAIN OF THE COLLAGEN TAIL

(Received for publication, July 3, 1996, and in revised form, October 23, 1996)

From the Laboratoire de Neurobiologie Moléculaire et Cellulaire, Unité CNRS 1857, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France

In transfected COS cells, we analyzed the formation of heteromeric associations between rat acetylcholinesterase of type T (AChE_T) and various constructions derived from the NH₂-terminal region of the collagen tail of asymmetric forms, Q_N. Using a series of deletions and point mutations in Q_N, we showed that the binding of AChE_T to Q_N does not require the cysteines that normally establish intersubunit disulfide bonds with catalytic subunits and that it essentially relies on the presence of stretches of successive prolines, although adjacent residues also contribute to the interaction. We thus defined a roline-ich ttachment omain or PRAD, which recruits AChE_T subunits to form heteromeric associations. Such molecules, consisting of one PRAD associated with a tetramer of AChE_T, are exported efficiently by the cells. Using the proportion of AChE_T subunits engaged in heteromeric tetramers, we ranked the interaction efficiency of various constructions. From these experiments we evaluated the contribution of different elements of the PRAD to the quaternary assembly of AChE_T subunits in the secretory pathway. The PRAD remained functional when reduced to six residues followed by a string of 10 prolines (Glu-Ser-Thr-Gly₃-Pro₁₀). We then showed that synthetic polyproline itself can associate with AChE_T subunits, producing well defined tetramers, when added to live transfected cells or even to cell extracts. This is the first example of an in vitro assembly of AChE tetramers from monomers and dimers. These results open the way to a chemical-physical exploration of the formation of these quaternary associations, both in the secretory pathway and in vitro.

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