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Originally published In Press as doi:10.1074/jbc.M105303200 on July 2, 2001

J. Biol. Chem., Vol. 276, Issue 35, 32743-32749, August 31, 2001
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RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes*

G. Sebastiaan WinklerDagger , Thodoris G. PetrakisDagger , Steen EthelbergDagger , Masao Tokunaga§, Hediye Erdjument-Bromage, Paul Tempst, and Jesper Q. SvejstrupDagger ||

From the Dagger  Mechanisms of Gene Transcription Laboratory, Imperial Cancer Research Fund, Clare Hall Laboratories, Blanche Lane, South Mimms, Herts, EN6 3LD, United Kingdom, § Applied and Molecular Microbiology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan, and the  Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021

Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the previously identified Elp1, Elp2, and Elp3 proteins and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.

* This project was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Project (to J. Q. S.), by an EMBO Long Term Fellowship (to G. S. W.), by a Carlsberg Foundation Fellowship, by a grant from The Danish Medical Research Council (to S. E.), and by NCI Core Grant P30 CA08748 (to P. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed. Fax: 44 207 269 3801; E-mail: j.svejstrup@icrf.icnet.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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