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Mechanisms of P/CAF auto-acetylation
Helena Santos-Rosa1, Ester Valls, Tony Kouzarides
1Instituto de Biología Molecular de Barcelona, CID, Consejo Superior de Investigaciones Científicas (CSIC), Jordi Girona 18-26, E-08034 Barcelona, Spain.
Nucleic Acids Research
|July 31, 2003
Summary
Human P/CAF (p300/CBP-associated factor) is acetylated in vivo by itself and p300, enhancing its histone acetyltransferase activity. This post-translational modification may regulate P/CAF function.
Area of Science:
- Biochemistry
- Molecular Biology
- Epigenetics
Background:
- P/CAF (p300/CBP-associated factor) is a histone acetyltransferase.
- It was initially identified as a protein that binds to CBP and p300.
Purpose of the Study:
- To investigate the post-translational modification of human P/CAF.
- To determine the functional consequences of P/CAF acetylation.
Main Methods:
- In vivo acetylation assays.
- Identification of acetylation sites and domains involved.
- Assays to measure histone acetyltransferase (HAT) activity.
Main Results:
- Human P/CAF undergoes acetylation in vivo.
- P/CAF is acetylated by itself and by p300, but not by CBP.
- Acetylation can occur intramolecularly, targeting lysines in the C-terminal nuclear localization signal (NLS), or intermolecularly, requiring the N-terminal domain.
- Acetylation increases P/CAF's HAT activity.
Conclusions:
- P/CAF acetylation is a novel post-translational modification.
- This modification, particularly on the NLS, may regulate P/CAF's function and HAT activity.