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Molecular and Cellular Biology, September 2005, p. 7803-7811, Vol. 25, No. 17
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.17.7803-7811.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mutational Analysis of an RNA Polymerase II Elongation Factor in Drosophila melanogaster

Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, 1402 South Grand Blvd., St. Louis, Missouri 63104

Received 9 February 2005/ Returned for modification 8 April 2005/ Accepted 18 May 2005

The ELL family of proteins function in vitro as elongation factors for RNA polymerase II. Deletion studies have defined domains in mammalian ELL required for transcription elongation activity and RNA polymerase binding in vitro, for transformation of cultured cells when overexpressed, and for leukemogenesis and cell proliferation as part of a leukemic fusion protein. The goal of this study was to identify domains required for chromosome targeting and viability in the unique Drosophila ELL (dELL) protein. Here, we show that an N-terminal domain of dELL is necessary and sufficient for targeting to transcriptionally active puff sites in chromatin, supporting a role for this domain in recruiting dELL to elongating RNA polymerase II. We demonstrate that a central domain of dELL is required for rapid mobilization of ELL during the heat shock response, suggesting a regulatory function for this domain. Unexpectedly, transgenic dELL in which the N-terminal chromosome binding domain is deleted can complement the recessive lethality of mutations in ELL, suggesting that Drosophila ELL has an essential activity in development distinct from its role as an RNA polymerase II elongation factor.

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• Smith, E. R., Winter, B., Eissenberg, J. C., Shilatifard, A. (2008). Regulation of the transcriptional activity of poised RNA polymerase II by the elongation factor ELL. Proc. Natl. Acad. Sci. USA 105: 8575-8579 [Abstract] [Full Text]