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Plant Cell, Vol. 12, 211-224, February 2000, Copyright © 2000, American Society of Plant Physiologists
A Highly Conserved Domain of the Maize Activator Transposase Is Involved in Dimerization
Lutz Essersa,
Ruth H. Adolphsa, and
Reinhard Kunzea
a Institut für Genetik und Mikrobiologie, Universität München, Maria-Ward-Strasse 1a, 80638 Munich, Germany
Correspondence to:
Reinhard Kunze, at Botanisches Institut, Universität zu Köln, Gyrhofstrasse 15, 50931 Cologne, Germany., reinhard.kunze{at}uni-koeln.de (E-mail), 49-221-470-5039 (fax)
Previous studies have presented indirect evidence that the transposase of the maize transposable element Activator (TPase) is active as an oligomer and forms inactive macromolecular complexes expressed in large amounts. Here, we have identified and characterized a dimerization domain at the C terminus of the protein. This domain is the most highly conserved region in the transposases of elements belonging to the Activator superfamily (hAT element superfamily) and contains a characteristic signature motif. The isolated dimerization domain forms extremely stable dimers in vitro. Interestingly, mutations in five of the six conserved residues of the signature motif do not affect in vitro dimerization, whereas mutations in other, less strictly conserved residues of the signature motif do. Loss of dimerization in vitro correlates with loss of TPase activity in vivo. As revealed by in situ immunofluorescence staining of mutant TPase proteins, the dimerization domain also is involved in forming inactive macromolecular aggregates when overexpressed, and the TPase contains one or more additional interaction functions.
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