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Institut Jacques Monod, 2 Place Jussieu Tour 43, 75251 Paris Cedex 05, France1
Centro de Biologia Molecular e Engenharia Genética, UNICAMP, CP 6109, Campinas SP, Brazil2
Author for correspondence: Silvio Urcuqui-Inchima.Fax +33 1 44 27 35 80. e- mail urcuqui{at}ijm.jussieu.fr (On leave from the Centro Fruticola Andino, Cali, Colombia.)
The first ~60 amino acids of the N-terminal part of the potyvirus helper component-proteinase (HC-Pro) include highly conserved residues comprising a Cys-rich region. In the present study, the domain in Potato virus Y sufficient for self-interaction was mapped using the yeast two-hybrid system to the 83 N-terminal amino acids of HC-Pro. Mutations in the conserved His and two Cys residues within the Cys-rich region have a strong debilitating effect on self-interaction when introduced in the full-length HC-Pro, but not when introduced in the N-terminal fragment.
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