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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/5041Full metadata record
| DC Field | Value | Language |
|---|---|---|
| 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 | - |
| Appears in Collections: | Digital Csic | |
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