| First Author | Mujtaba S | Year | 2002 |
| Journal | Mol Cell | Volume | 9 |
| Issue | 3 | Pages | 575-86 |
| PubMed ID | 11931765 | Mgi Jnum | J:75809 |
| Mgi Id | MGI:2177881 | Doi | 10.1016/s1097-2765(02)00483-5 |
| Citation | Mujtaba S, et al. (2002) Structural Basis of Lysine-Acetylated HIV-1 Tat Recognition by PCAF Bromodomain. Mol Cell 9(3):575-86 |
| abstractText | The human immunodeficiency virus type 1 (HIV-1) trans-activator protein Tat stimulates transcription of the integrated HIV-1 genome and promotes viral replication in infected cells. Tat transactivation activity is dependent on lysine acetylation and its association with nuclear histone acetyltransferases p300/CBP (CREB binding protein) and p300/CBP-associated factor (PCAF). Here, we show that the bromodomain of PCAF binds specifically to HIV-1 Tat acetylated at lysine 50 and that this interaction competes effectively against HIV-1 TAR RNA binding to the lysine-acetylated Tat. The three-dimensional solution structure of the PCAF bromodomain in complex with a lysine 50-acetylated Tat peptide together with biochemical analyses provides the structural basis for the specificity of this molecular recognition and reveals insights into the differences in ligand selectivity of bromodomains. |
