Journal
BIOCHEMISTRY AND CELL BIOLOGY
Volume 87, Issue 1, Pages 151-161Publisher
CANADIAN SCIENCE PUBLISHING
DOI: 10.1139/O08-131
Keywords
chromatin; epigenetics; histone; posttranslational modification; mass spectrometry
Categories
Funding
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0821893] Funding Source: National Science Foundation
Ask authors/readers for more resources
Antisera raised against individual sites of histone post-translational modification (PTM) have provided critical insights into the biology of many of these PTMs. However, limitations inherent to immunochemical approaches can skew results obtained with these reagents, possibly leading investigators to misjudge the role of a specific histone PTM in a given process. We have used mass spectrometry in Conjunction with cell synchronization, metabolic labeling, RNA interference, and other approaches to show that the SET domain proteins PR-Set7 and Suv4-20 mediate progressive global mono-, di-, and trimethylation of lysine 20 (K20) in newly synthesized histone H4, beginning approximately at the G(2)/M transition, well after new H4 is deposited in replicating chromatin during S phase. Immunochemical and other approaches have implicated H4-K20 methylation in multiple processes, including gene activation, gene repression, chromatin condensation, S phase progression, mitosis, and DNA-damage checkpoint signaling. Here, we review recent data on the regulation and significance of K20 methylation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available