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HIV protease cleaves poly(A)-binding protein

AutorÁlvarez, Enrique; Castelló, Alfredo; Menéndez-Arias, Luis ; Carrasco Llamas, Luis
Palabras claveEukaryotic initiation factor (eIF),
Poly(A)-binding protein (PABP),
Fecha de publicación15-may-2006
EditorPortland Press
CitaciónBiochem J. 2006 June 1; 396(Pt 2): 219–226
ResumenThe PABP [poly(A)-binding protein] is able to interact with the 3′ poly(A) tail of eukaryotic mRNA, promoting its translation. Cleavage of PABP by viral proteases encoded by several picornaviruses and caliciviruses plays a role in the abrogation of cellular protein synthesis. We report that infection of MT-2 cells with HIV-1 leads to efficient proteolysis of PABP. Analysis of PABP integrity was carried out in BHK-21 (baby-hamster kidney) and COS-7 cells upon individual expression of the protease from several members of the Retroviridae family, e.g. MoMLV (Moloney murine leukaemia virus), MMTV (mouse mammary tumour virus), HTLV-I (human T-cell leukaemia virus type I), SIV (simian immunodeficiency virus), HIV-1 and HIV-2. Moreover, protease activity against PABP was tested in a HeLa-cell-free system. Only MMTV, HIV-1 and HIV-2 proteases were able to cleave PABP in the absence of other viral proteins. Purified HIV-1 and HIV-2 proteases cleave PABP1 directly at positions 237 and 477, separating the two first RNA-recognition motifs from the C-terminal domain of PABP. An additional cleavage site located at position 410 was detected for HIV-2 protease. These findings indicate that some retroviruses may share with picornaviruses and caliciviruses the capacity to proteolyse PABP
DescripciónArticle available at http://dx.doi.org/10.1042/BJ20060108
ISSN0264-6021 (Print)
1470-8728 (Online)
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