Skip to main navigation Skip to search Skip to main content

Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function

  • Ling Wang
  • , Yong Tang
  • , Philip A. Cole
  • , Ronen Marmorstein

Research output: Contribution to journalReview articlepeer-review

Abstract

The recent structure and associated biochemical studies of the metazoan-specific p300/CBP and fungal-specific Rtt109 histone acetyltransferases (HATs) have provided new insights into the ancestral relationship between HATs and their functions. These studies point to a common HAT ancester that has evolved around a common structural framework to form HATs with divergent catalytic and substrate-binding properties. These studies also point to the importance of regulatory loops within HATs and autoacetylation in HAT function. Implications for future studies are discussed.

Original languageEnglish (US)
Pages (from-to)741-747
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume18
Issue number6
DOIs
StatePublished - Dec 2008
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function'. Together they form a unique fingerprint.

Cite this