Argentina
| Articulo
Zinc-binding properties of Junín virus nucleocapsid protein
| dc.creator | Tortorici, María Alejandra | |
| dc.creator | Ghiringhelli, P. D. | |
| dc.creator | Lozano, Mario E. | |
| dc.creator | Albariño, César G. | |
| dc.creator | Romanowski, Víctor | |
| dc.date | 2001 | |
| dc.date | 2019-10-25T17:33:03Z | |
| dc.identifier | http://sedici.unlp.edu.ar/handle/10915/84101 | |
| dc.identifier | issn:0022-1317 | |
| dc.description | 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. | |
| dc.description | Instituto de Biotecnologia y Biologia Molecular | |
| dc.format | application/pdf | |
| dc.format | 121-128 | |
| dc.language | en | |
| dc.rights | http://creativecommons.org/licenses/by-nc-sa/4.0/ | |
| dc.rights | Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) | |
| dc.subject | Biología | |
| dc.subject | Virus Junin | |
| dc.title | Zinc-binding properties of Junín virus nucleocapsid protein | |
| dc.type | Articulo | |
| dc.type | Articulo |