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Título: | The N-terminal Arg-rich region of human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus Nef is involved in RNA binding |
Autor: | Echarri, Asier CSIC ORCID; González, María Eugenia; Carrasco, Luís | Palabras clave: | Human immunodeficiency virus 1: Human immunodeficiency virus 2 Simian immunodeficiency virus Nef RNA-binding protein |
Fecha de publicación: | 1997 | Citación: | European Journal of Biochemistry 246: 38- 44 (1997) | Resumen: | Comparison of the amino acid sequences of human immunodeficiency virus (HIV) Nef protein and several RNA-binding proteins shows similarities in some regions of these proteins. Thus, poliovirus protein 2C, an RNA-binding protein, shares with Nef the sequence YXQQ...MDD...DXXD. In addition, both proteins contain an Arg-rich motif that, in the case of poliovirus 2C, is involved in RNA-binding activity. Moreover, the RNA-binding, anti-terminator N proteins of λ,φ21 and P22 phages show sequence similarities with HIV Nef at the Arg-rich motif. To assess the significance of this motif, native and deletion variants of Nef protein were assayed for RNA-binding activity. The N-terminal 35 amino acids of HIV-1 Nef that comprise the Arg-rich motif are sufficient for RNA binding. Point mutations engineered at the Arg-rich motif of HIV-1 Nef revealed that basic amino acid residues are essential for RNA-binding activity. The Nef proteins from HIV-2 and SIV can also interact with RNA, while the same proteins with the N-terminal Arg-rich domain truncated fail to interact with RNA. These findings indicate that all three Nef proteins from HIV-1, HIV-2 and simian immunodeficiency virus belong to the RNA-binding family of proteins. The three proteins contain an Arg-rich region at the N-terminus which is necessary to interact with RNA. | URI: | http://hdl.handle.net/10261/159038 | DOI: | 10.1111/j.1432-1033.1997.00038.x | ISSN: | 0014-2956 |
Aparece en las colecciones: | (CBM) Artículos |
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1997 Eur J Biochem.pdf | 769,56 kB | Adobe PDF | Visualizar/Abrir |
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