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Biotechnology |
Dipartimento di Biologia, Università ’Tor Vergata’, via della Ricerca Scientifica, 00133 La Romanina (Roma), Italy1
Centro Acidi Nucleici del CNR, Roma, Italy2
Author for correspondence: L. Paolozzi. Tel: +39 6 72594674. Fax: +39 6 2023500. e-mail: Paolozzi{at}bio.uniroma2.it
The development of a convenient and promising alternative to the various two-hybrid methods that are used to study protein–protein interactions is described. In this system, a lambdoid chimeric operator is recognized by a hybrid repressor formed by two chimeric monomers whose C-terminal domains are composed of heterologous proteins (or protein domains). Only if these proteins efficiently dimerize in vivo is a functional repressor formed able to bind the chimeric operator and shut off the synthesis of a downstream reporter gene. This new approach was tested with several interacting proteins ranging in size from less than 100 to more than 800 amino acids and, to date, no size or topology limit has been detected.
Keywords: protein–protein interaction, cell division proteins, phage repressor, ß-galactosidase assay
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