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- W1994496212 abstract "PCAF and GCN5 are histone acetyltransferase (HAT) paralogs which play roles in the remodeling of chromatin in health and disease. Previously, a conformationally flexible loop in the catalytic domain had been observed in the X-ray structures of GCN5 in different liganded states. Here, the conformation and dynamics of this PCAF/GCN5 α5−β6 loop was investigated in solution using tryptophan fluorescence. A mutant human PCAF HAT domain (PCAFWloop) was created in which the natural tryptophan (Trp-514) remote from the α5−β6 loop was replaced with tyrosine and a glutamate within the loop (Glu-641) was substituted with tryptophan. This PCAFWloop protein exhibited catalytic parameters within 3-fold of those of the wild-type PCAF catalytic domain, suggesting that the loop mutation was not deleterious for HAT activity. While saturating CoASH induced a 30% quenching of Trp fluorescence in PCAFWloop, binding of the high-affinity bisubstrate analogue H3-CoA-20 led to a 2-fold fluorescence increase. These different effects correlate with the different α5−β6 loop conformations seen previously in X-ray structures. On the basis of stopped-flow fluorescence studies, binding of H3-CoA-20 to PCAFWloop proceeds via a rapid association step followed by a slower conformational change involving loop movement. Time-resolved fluorescence measurements support a model in which the α5−β6 loop in the H3-CoA-20−PCAFWloop complex exists in a narrower ensemble of conformations compared to free PCAFWloop. The relevance of loop dynamics to PCAF/GCN5 catalysis and substrate specificity are discussed." @default.
- W1994496212 created "2016-06-24" @default.
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- W1994496212 date "2005-07-15" @default.
- W1994496212 modified "2023-10-16" @default.
- W1994496212 title "Fluorescence Analysis of a Dynamic Loop in the PCAF/GCN5 Histone Acetyltransferase" @default.
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- W1994496212 doi "https://doi.org/10.1021/bi050776i" @default.
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