Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 18, Issue 6, Pages 741-747Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2008.09.004
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Funding
- NCRR NIH HHS [U54 RR020839-056891, U54 RR020839] Funding Source: Medline
- NIGMS NIH HHS [R01 GM060293, R01 GM062437-08, R01 GM062437] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [U54RR020839] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM060293, R01GM062437] Funding Source: NIH RePORTER
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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.
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