NDLI: Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo

Content Provider	PubMed Central
Author	Winkler, G. Sebastiaan Arnold, Kristjuhan Erdjument-bromage, Hediye Paul, Tempst Svejstrup, Jesper Q.
Copyright Year	2002
Abstract	The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits—Elp4, Elp5, and Elp6—are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3.
Related Links	http://dx.doi.org/10.1073/pnas.022042899
Ending Page	3522
Page Count	6
Starting Page	3517
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	99
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2002-03-19
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
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Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo