| dc.contributor |
Ministerio de Economía y Competitividad (España) |
|
| dc.contributor |
Ministerio de Educación y Ciencia (España) |
|
| dc.contributor |
Fundación Ramón Areces |
|
| dc.creator |
Álvarez, Enrique |
|
| dc.creator |
Castelló, Alfredo |
|
| dc.creator |
Menéndez-Arias, Luis |
|
| dc.creator |
Carrasco Llamas, Luis |
|
| dc.date |
2008-06-12T12:50:35Z |
|
| dc.date |
2008-06-12T12:50:35Z |
|
| dc.date |
2006-05-15 |
|
| dc.date.accessioned |
2017-01-31T01:39:35Z |
|
| dc.date.available |
2017-01-31T01:39:35Z |
|
| dc.identifier |
Biochem J. 2006 June 1; 396(Pt 2): 219–226 |
|
| dc.identifier |
0264-6021 (Print) |
|
| dc.identifier |
1470-8728 (Online) |
|
| dc.identifier |
http://hdl.handle.net/10261/5041 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/5041 |
|
| dc.description |
Article available at http://dx.doi.org/10.1042/BJ20060108 |
|
| dc.description |
The 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 |
|
| dc.description |
Financial support from Grant BMC2003-00494 from the Dirección General de Investigación Científica y Técnica and an Institutional Grant to the Centro de Biología Molecular “Severo Ochoa” from the Fundación Ramón Areces, are acknowledged. E.A. and A.C. hold fellowships from the Ministerio de Educación y Ciencia |
|
| dc.description |
Peer reviewed |
|
| dc.format |
134559 bytes |
|
| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
Portland Press |
|
| dc.rights |
openAccess |
|
| dc.subject |
Eukaryotic initiation factor (eIF), |
|
| dc.subject |
HIV |
|
| dc.subject |
Poly(A)-binding protein (PABP), |
|
| dc.subject |
Protease |
|
| dc.subject |
Translation |
|
| dc.title |
HIV protease cleaves poly(A)-binding protein |
|
| dc.type |
Artículo |
|