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Prepublished online as a Blood First Edition Paper on November 21, 2002; DOI 10.1182/blood-2002-06-1664. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-06-1664v1 101/6/2355    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Simone, F. Articles by Thirman, M. J. Search for Related Content PubMed PubMed Citation Articles by Simone, F. Articles by Thirman, M. J. Related Collections Neoplasia Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 March 2003, Vol. 101, No. 6, pp. 2355-2362 NEOPLASIA ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties Federico Simone, Roger T. Luo, Paul E. Polak, Joseph J. Kaberlein, and Michael J. Thirman From the University of Chicago Section of Hematology/Oncology, Chicago, IL. The (11;19)(q23;p13.1) translocation in acute leukemia results in the formation of an MLL-ELL fusion protein. ELL is an RNA polymerase II elongation factor that interacts with the recently identified EAF1 protein. To characterize the normal functions of ELL and its aberrant activities when fused to MLL, we isolated a second protein that interacts with ELL named EAF2 for ELL Associated Factor 2. EAF2 is highly homologous to EAF1, with 58% identity and 74% amino acid conservation. Using specific antibodies generated to EAF2, we coimmunoprecipitated ELL and EAF2 from multiple cell lines. Confocal microscopy revealed that endogenous EAF2 and ELL colocalized in a nuclear speckled pattern. Database comparisons with EAF2 identified a region with a high content of serine, aspartic acid, and glutamic acid residues that is conserved with EAF1 and exhibited amino acid similarity with several translocation partner proteins of MLL, including AF4 and ENL. We found that EAF2 and EAF1 both contain transcriptional activation domains within this region. Using retroviral bone marrow transduction, we observed that a heterologous fusion of EAF2 to MLL immortalized hematopoietic progenitor cells. In contrast to EAF1, EAF2 does not bind to the carboxy-terminus of ELL. We identified a protein-protein interaction domain within the amino-terminus of ELL that binds to both EAF1 and EAF2. This amino-terminal interaction domain is disrupted in the formation of the MLL-ELL fusion protein. Thus, MLL-ELL retains an interaction domain for EAF1 but not for EAF2. Taken together, these data suggest that MLL-ELL may disrupt the normal protein-protein interactions of ELL. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. Zhou, X. Feng, B. Ban, J. Liu, Z. Wang, and W. Xiao Elongation Factor ELL (Eleven-Nineteen Lysine-rich Leukemia) Acts as a Transcription Factor for Direct Thrombospondin-1 Regulation J. Biol. Chem., July 10, 2009; 284(28): 19142 - 19152. [Abstract] [Full Text] [PDF] R. K. Slany The molecular biology of mixed lineage leukemia Haematologica, July 1, 2009; 94(7): 984 - 993. [Abstract] [Full Text] [PDF] J.-X. Liu, B. Hu, Y. Wang, J.-F. Gui, and W. Xiao Zebrafish eaf1 and eaf2/u19 Mediate Effective Convergence and Extension Movements through the Maintenance of wnt11 and wnt5 Expression J. Biol. Chem., June 12, 2009; 284(24): 16679 - 16692. [Abstract] [Full Text] [PDF] E. R. Smith, B. Winter, J. C. Eissenberg, and A. Shilatifard Regulation of the transcriptional activity of poised RNA polymerase II by the elongation factor ELL PNAS, June 24, 2008; 105(25): 8575 - 8579. [Abstract] [Full Text] [PDF] C. A. S. Banks, S. E. Kong, H. Spahr, L. Florens, S. Martin-Brown, M. P. Washburn, J. W. Conaway, A. Mushegian, and R. C. Conaway Identification and Characterization of a Schizosaccharomyces pombe RNA Polymerase II Elongation Factor with Similarity to the Metazoan Transcription Factor ELL J. Biol. Chem., February 23, 2007; 282(8): 5761 - 5769. [Abstract] [Full Text] [PDF] S. E. Kong, C. A. S. Banks, A. Shilatifard, J. W. Conaway, and R. C. Conaway ELL-associated factors 1 and 2 are positive regulators of RNA polymerase II elongation factor ELL PNAS, July 19, 2005; 102(29): 10094 - 10098. [Abstract] [Full Text] [PDF] L. Pascual-Le Tallec, F. Simone, S. Viengchareun, G. Meduri, M. J. Thirman, and M. Lombes The Elongation Factor ELL (Eleven-Nineteen Lysine-Rich Leukemia) Is a Selective Coregulator for Steroid Receptor Functions Mol. Endocrinol., May 1, 2005; 19(5): 1158 - 1169. [Abstract] [Full Text] [PDF] W. Xiao, Q. Zhang, F. Jiang, M. Pins, J. M. Kozlowski, and Z. Wang Suppression of Prostate Tumor Growth by U19, a Novel Testosterone-regulated Apoptosis Inducer Cancer Res., August 1, 2003; 63(15): 4698 - 4704. [Abstract] [Full Text] [PDF]

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