Investigation of the acetylation mechanism by GCN5 histone acetyltransferase.

PloS One
Junfeng JiangCheng Luo

Abstract

The histone acetylation of post-translational modification can be highly dynamic and play a crucial role in regulating cellular proliferation, survival, differentiation and motility. Of the enzymes that mediate post-translation modifications, the GCN5 of the histone acetyltransferase (HAT) proteins family that add acetyl groups to target lysine residues within histones, has been most extensively studied. According to the mechanism studies of GCN5 related proteins, two key processes, deprotonation and acetylation, must be involved. However, as a fundamental issue, the structure of hGCN5/AcCoA/pH3 remains elusive. Although biological experiments have proved that GCN5 mediates the acetylation process through the sequential mechanism pathway, a dynamic view of the catalytic process and the molecular basis for hGCN5/AcCoA/pH3 are still not available and none of theoretical studies has been reported to other related enzymes in HAT family. To explore the molecular basis for the catalytic mechanism, computational approaches including molecular modeling, molecular dynamic (MD) simulation and quantum mechanics/molecular mechanics (QM/MM) simulation were carried out. The initial hGCN5/AcCoA/pH3 complex structure was modeled and a reasonab...Continue Reading

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Feb 14, 2014·The Journal of Physical Chemistry. B·Xinlei ZhangCheng Luo
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Methods Mentioned

BETA
histone acetylation
acetylation
acetylating

Software Mentioned

Sybyl
InsightII
Gaussian
ONIOM
LIGPLOT
hbonds
INTMED
AMBER

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