| Autor: |
Li, Ming-Shi, Garcia-Asua, Guillermo, Bhattacharyya, Uma, Mascagni, Paolo, Austen, Brian M., Roberts, Michael M. |
| Zdroj: |
Biochemical and Biophysical Research Communications; January 1996, Vol. 218 Issue: 1 p352-355, 4p |
| Abstrakt: |
The Vpr protein of human immunodeficiency virus type 1 (HIV-1) is incorporated into the virion by the Gag polyprotein precursor Pr55gag. The importance of the p6gagsequence at the C-terminal end of Pr55gaghas a crucial role in Vpr incorporation. To identify the Gag sequences directly involved in Vpr binding, we compared the Vpr binding affinities of the 71 amino acid nucleocapsid protein p7, the C-terminal peptide (35–71) p7C and p6gagby affinity chromatography. p7 and p7C have the strongest Vpr binding activities compared to p6gag. These results suggest that the nucleocapsid protein and its C-terminal domain may be important for the incorporation of Vpr into the mature HIV-1 virion and the subsequent localisation of viral nucleic acid to the cell nucleus by Vpr. |
| Databáze: |
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