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Journal of General Virology (2001), 82, 121-128.
© 2001 Society for General Microbiology

Animal: RNA Viruses

Zinc-binding properties of Junín virus nucleocapsid protein

M. Alejandra Tortorici1, P. Daniel Ghiringhelli2, Mario E. Lozano2, César G. Albariñoa,1 and Víctor Romanowski1,2

Instituto de Bioquímica y Biología Molecular, Depto de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Calles 47 y 115, 1900 La Plata, Buenos Aires, Argentina1
Laboratorio de Ingeniería Genética y Biología Celular y Molecular, Departamento de Ciencia y Tecnología, Centro de Estudios e Investigaciones, Universidad Nacional de Quilmes, Roque Saenz Peña 180, 1876 Bernal, Buenos Aires, Argentina2

Author for correspondence: Victor Romanowski (at address 1). Fax +54 221 4259223. e-mail victor{at}biol.unlp.edu.ar

The arenavirus nucleocapsid protein (N) is a highly basic 63 kDa protein with a dual function during the virus life-cycle. First, it is involved in essential steps of genome replication, promoting the synthesis of the full-length antigenomic copy of S RNA, and second it associates with the genomic RNA to form the nucleocapsid. We have expressed the N protein of Junín virus in E. coli and shown that it binds zinc in vitro. This property is in agreement with the presence in the carboxy-terminal region of the N protein of the CX2HX23CX4C sequence, which resembles a classical zinc-finger motif. The specificity for zinc binding was demonstrated by competition with other divalent metal ions. The ability of the predicted motif to bind zinc was established by analysis of a series of N mutants, including truncated variants and amino acid substitutions. In addition, alternative zinc-binding sites were found.




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