TAILIEUCHUNG - Báo cáo khoa học: Mixed lineage leukemia: a structure–function perspective of the MLL1 protein

Several acute lymphoblastic and myelogenous leukemias are correlated with alterations in the human mixed lineage leukemia protein-1 (MLL1) gene. MLL1 is a member of the evolutionarily conserved SET1 family of histone H3 lysine 4 (H3K4) methyltransferases, which are required for the regula-tion of distinct groups of developmentally regulated genes in metazoans. | MINIREVIEW Mixed lineage leukemia a structure-function perspective of the MLL1 protein Michael S. Cosgrove and Anamika Patel Department of Biology Syracuse University NY USA Keywords Asli2L CXXC H3K4 methylation MLL RbBP5 SET TAD WDR5 Win motif Correspondence M. S. Cosgrove Syracuse University 340 Life Sciences Complex 107 College Place Syracuse NY 13244 USA Fax 1 315 443 2012 Tel 1 315 443 2964 E-mail mscosgro@ Several acute lymphoblastic and myelogenous leukemias are correlated with alterations in the human mixed lineage leukemia protein-1 MLL1 gene. MLL1 is a member of the evolutionarily conserved SET1 family of histone H3 lysine 4 H3K4 methyltransferases which are required for the regulation of distinct groups of developmentally regulated genes in metazoans. Despite the important biological role of SET1 family enzymes and their involvement in human leukemias relatively little is understood about how these enzymes work. Here we review several recent structural and biochemical studies that are beginning to shed light on the molecular mechanisms for the regulation of H3K4 methylation by the human MLL1 enzyme. Received 16 November 2009 accepted 3 February 2010 doi Introduction Chromosomal translocations that disrupt the mixed lineage leukemia protein-1 gene MLL1 ALL1 HRX Htrx are associated with a unique subset of acute lymphoblastic or myelogenous leukemias 1-4 . The product of the MLL1 gene is a large protein that functions as a transcriptional co-activator required for the maintenance of Hox gene expression patterns during hematopoiesis and development 5-8 . The transcriptional co-activator activity of MLL1 is mediated in part by its histone H3 lysine 4 H3K4 methyltransferase activity 6 an epigenetic mark correlated with transcriptionally active forms of chromatin 9 10 . MLL1 complexes catalyze mono- di- and trimethylation of H3K4 regulation of which can have distinct functional consequences. MLL1 contains a number of .

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