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J. Biol. Chem., Vol. 275, Issue 41, 32052-32056, October 13, 2000
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From the The human ELL gene, which is a
frequent target for translocation in acute myeloid leukemia, was
initially isolated from rat liver nuclei and found to be an RNA
polymerase II elongation factor. Based on homology to ELL, we later
cloned ELL2 and demonstrated that it can also increase the catalytic
rate of transcription elongation by RNA polymerase II. To better
understand the role of ELL proteins in the regulation of transcription
by RNA polymerase II, we have initiated a search for proteins related
to ELLs. In this report, we describe the molecular cloning, expression,
and characterization of ELL3, a novel RNA polymerase II elongation factor approximately 50% similar to both ELL and ELL2. Our
transcriptional studies have demonstrated that ELL3 can also increase
the catalytic rate of transcription elongation by RNA polymerase II.
The C-terminal domain of ELL, which we recently demonstrated to be
required and sufficient for the immortalization of myeloid progenitor
cells, shares strong similarities to the C-terminal domain of ELL3.
ELL3 was localized by immunofluorescence to the nucleus of cells, and Northern analysis indicated that ELL3 is a testis-specific RNA polymerase II elongation factor.
Identification, Cloning, Expression, and Biochemical
Characterization of the Testis-specific RNA Polymerase II Elongation
Factor ELL3*
,
,
¶
Edward A. Doisy Department of Biochemistry,
St. Louis University School of Medicine, St. Louis, Missouri 63104 and § Cancer Immunology Division, the Peter MacCallum Cancer
Institute, East Melbourne 3002, Victoria, Australia
*
This work was supported in part by American Cancer Society
Grant RPG-99-218-01-MGO (to A. S.).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.
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