2024-03-28T23:51:04Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1590382019-03-13T11:24:19Zcom_10261_79com_10261_1col_10261_332
2018-01-12T12:07:55Z
urn:hdl:10261/159038
The N-terminal Arg-rich region of human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus Nef is involved in RNA binding
Echarri, Asier
González, María Eugenia
Carrasco, Luís
Fundación Ramón Areces
Eusko Jaurlaritza
Dirección General de Investigación Científica y Técnica, DGICT (España)
Human immunodeficiency virus 1: Human immunodeficiency virus 2
Simian immunodeficiency virus
Nef
RNA-binding protein
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.
2018-01-12T12:07:55Z
2018-01-12T12:07:55Z
1997
2018-01-12T12:07:55Z
artículo
European Journal of Biochemistry 246: 38- 44 (1997)
0014-2956
http://hdl.handle.net/10261/159038
10.1111/j.1432-1033.1997.00038.x
http://dx.doi.org/10.13039/100008054
http://dx.doi.org/10.13039/501100008737
http://dx.doi.org/10.13039/501100003086
eng
Publisher's version
Sí
openAccess