Cloning and characterization of ELL-associated proteins EAP45 and EAP20 - A role for yeast EAP-like proteins in regulation of gene expression by glucose

RNA polymerase II elongation factor ELL was recently purified from rat live r as a component of a multiprotein complex containing ELL and three ELL-ass ociated proteins (EAPs) of similar to 45 (EAP45), similar to 30 (EAP30), an d similar to 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 cere visiae SNF8 gene (Schmidt, A E,, Miller, T,, Schmidt, S, L,, Shiekhattar, R ,, and Shilatifard, A. (1999) J, Biol, Chem, 274, 21981-21985), which is re quired for efficient derepression of glucose-repressed genes. Here we repor t the cloning of cDNAs encoding the EAP45 and EAP20 proteins. In addition, we identify the S, cerevisiae VPS36 and YJR102c genes as potential ortholog s of EAP45 and EAP20 and show that they are previously uncharacterized SNF genes with properties very similar to SNF8.