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PCAF, SIRT1 and the regulation of substrate acetylation

Abstract:

Levels of lysine acetylation (KAc) in cells are regulated by epigenetic enzymes with opposing roles; histone acetyl transferases (HATs) and histone deacetylases (HDACs). The HAT p300 CBP associating factor (PCAF) and the sirtuin HDAC SIRT1 have protein substrates in common, including histone 3 (H3) at lysine residues 9 and 14 (H3K9 and H3K14) and non histone protein hypoxia inducible factor 1α (HIF1α). Studying PCAF and SIRT1 in parallel helps understand how levels of acetylation are maint...

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Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Oxford college:
Brasenose College
Role:
Author

Contributors

Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Role:
Supervisor
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry
Research group:
Brennan group
Role:
Supervisor
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Role:
Examiner
Institution:
University of Leicester
Department:
Chemistry
Role:
Examiner


More from this funder
Funder identifier:
http://dx.doi.org/10.13039/501100000266
Funding agency for:
Serrano, L
Grant:
EP/L015838/1
Programme:
Synthesis for Biology and Medicine CDT


DOI:
Type of award:
DPhil
Level of award:
Doctoral
Awarding institution:
University of Oxford

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