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J. Biol. Chem., Vol. 279, Issue 31, 32087-32092, July 30, 2004

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Molecular Architecture, Structure-Function Relationship, and Importance of the Elp3 Subunit for the RNA Binding of Holo-Elongator^*

Thodoris G. Petrakis, Birgitte Ø. Wittschieben, and Jesper Q. Svejstrup

From the Cancer Research UK, London Research Institute, Clare Hall Laboratories, Blanche Lane, South Mimms, Hertfordshire EN6 3LD, United Kingdom

The molecular architecture of six-subunit yeast holo-Elongator complex was investigated by the use of immunoprecipitation, two-hybrid interaction mapping, and in vitro studies of binary interactions between individual subunits. Surprisingly, Elp2 is dispensable for the integrity of the holo-Elongator complex, and a purified five-subunit elp2 Elongator complex retains histone acetyltransferase activity in vitro. These results indicate that the WD40 repeats in Elp2 are required neither for subunit-subunit interactions within Elongator nor for Elongator interaction with histones during catalysis. Elp2 and Elp4 were largely dispensable for the association of Elongator with nascent RNA transcript in vivo.In contrast, Elongator-RNA interaction requires the Elp3 protein. Together, these data shed light on the structure-function relationship of the Elongator complex.

Received for publication, March 25, 2004 , and in revised form, May 6, 2004.

^* This work was supported by a grant for Cancer Research UK (to J. Q. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: University of Pittsburgh Cancer Institute, Hillman Cancer Center Research Pavilion, 5117 Centre Ave., Suite 264, Pittsburgh, PA 15213.

To whom correspondence should be addressed. Fax: 44-207-269-3801; E-mail: j.svejstrup{at}cancer.org.uk.

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