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Gene activation by histone and factor acetyltransferases.
1Molecular Genetics Program, The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA. berger@wistar.upenn.edu.
Current Opinion in Cell Biology
|July 8, 1999
Summary
Histone acetyltransferases (HATs) acetylate histones and transcription factors to activate genes. Their structures reveal conserved mechanisms, and HAT activity is regulated by phosphorylation and protein interactions.
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- Acetyltransferases are crucial enzymes involved in gene regulation.
- These enzymes function as components of large macromolecular assemblies.
- Evidence suggests their role in acetylating histones and transcription factors.
Purpose of the Study:
- To summarize the emerging evidence on the function and regulation of acetyltransferases.
- To highlight the structural insights into the GNAT superfamily.
- To discuss the regulatory mechanisms of enzymatic acetyltransferase activity.
Main Methods:
- Review of existing literature and experimental evidence.
- Analysis of structural data for HATs and GNATs.
- Integration of findings on protein-protein interactions and phosphorylation.
Main Results:
- Acetyltransferases acetylate histones and transcription factors in vivo, leading to gene activation.
- HATs are part of large, conserved macromolecular complexes.
- Atomic resolution structures reveal conserved acetyl-CoA binding mechanisms in GNATs.
- Enzymatic activity is modulated by phosphorylation and protein interactions.
Conclusions:
- Acetyltransferases play a vital role in gene activation through acetylation.
- The structure and assembly of HATs suggest complex regulatory functions.
- Understanding HAT regulation is key to deciphering gene expression control.