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Originally published In Press as doi:10.1074/jbc.M010142200 on February 5, 2001

J. Biol. Chem., Vol. 276, Issue 19, 16528-16533, May 11, 2001
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Cloning and Characterization of ELL-associated Proteins EAP45 and EAP20
A ROLE FOR YEAST EAP-LIKE PROTEINS IN REGULATION OF GENE EXPRESSION BY GLUCOSE*

Takumi KamuraDagger §, Dennis BurianDagger §, Hamed KhaliliDagger , Susan L. Schmidt||, Shigeo SatoDagger , Wen-Jun LiuDagger , Michael N. ConradDagger , Ronald C. ConawayDagger , Joan Weliky ConawayDagger **Dagger Dagger , and Ali Shilatifard||§§

From the Dagger  Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City, Oklahoma 73104, the  Howard Hughes Medical Institute, Oklahoma City, Oklahoma 73104, the ** Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190, and the || Edward A. Doisy Department of Biochemistry, St. Louis University School of Medicine, Saint Louis, Missouri 63104

RNA polymerase II elongation factor ELL was recently purified from rat liver as a component of a multiprotein complex containing ELL and three ELL-associated proteins (EAPs) of ~45 (EAP45), ~30 (EAP30), and ~20 (EAP20) kDa (Shilatifard, A. (1998) J. Biol. Chem. 273, 11212-11217). Cloning of cDNA encoding the EAP30 protein revealed that it shares significant sequence similarity with the product of the Saccharomyces cerevisiae SNF8 gene (Schmidt, A. E., Miller, T., Schmidt, S. L., Shiekhattar, R., and Shilatifard, A. (1999) J. Biol. Chem. 274, 21981-21985), which is required for efficient derepression of glucose-repressed genes. Here we report the cloning of cDNAs encoding the EAP45 and EAP20 proteins. In addition, we identify the S. cerevisiae VPS36 and YJR102c genes as potential orthologs of EAP45 and EAP20 and show that they are previously uncharacterized SNF genes with properties very similar to SNF8.


* This work was supported in part by American Cancer Society Grant RP69921801 (to A. S.) and by National Institutes of Health Grant R37-GM41628 and a grant to the Oklahoma Medical Research Foundation by the H. A. and Mary K. Chapman Charitable Trust (to R. C. C. and J. W. C.).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.

§ These authors contributed equally to this work.

Dagger Dagger Associate investigator of the Howard Hughes Medical Institute.

§§ An Edward Mallinckrodt, Jr., Young Investigator. To whom correspondence should be addressed. Tel.: 314-577-8137; Fax: 314-268-5737; E-mail: shilatia@slu.edu.


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