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| VERA,JORGE; VALENZUELA,BEATRIZ; ROTH,MÓNICA J; LEÓN,ÓSCAR. |
| Processing of viral DNA by retroviral integrase leaves a dinucleotide single-strand overhang in the unprocessed strand. Previous studies have stressed the importance of the 5' single-stranded (ss) tail in the integration process. To characterize the ss-tail binding site on M-MuLV integrase, we carried out crosslinking studies utilizing a disintegration substrate that mimics the covalent intermediate formed during integration. This substrate carried reactive groups at the 5' ss tail. A bromoacetyl derivative with a side chain of 6 A was crosslinked to the mutant IN 106-404, which lacks the N-terminal domain, yielding a crosslinked complex of 50 kDa. Treatment of IN 106-404 with N-ethylmaleimide (NEM) prevented crosslinking, suggesting that Cys209 was... |
| Tipo: Journal article |
Palavras-chave: Integrase; Retrovirus; Crosslinking. |
| Ano: 2008 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602008000100009 |
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