Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 19, Pages 16528-16533Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M010142200
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- NIGMS NIH HHS [R37-GM41628] Funding Source: Medline
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RNA polymerase II elongation factor ELL was recently purified from rat liver as a component of a multiprotein complex containing ELL and three ELL-associated proteins (EAPs) of similar to 45 (EAP45), similar to 30 (EAP30), and 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 cerevisiae SNF8 gene (Schmidt, A E,, Miller, T,, Schmidt, S, L,, Shiekhattar, R,, and Shilatifard, A. (1999) J, Biol, Chem, 274, 21981-21985), which is required for efficient derepression of glucose-repressed genes. Here we report the cloning of cDNAs encoding the EAP45 and EAP20 proteins. In addition, we identify the S, cerevisiae VPS36 and YJR102c genes as potential orthologs of EAP45 and EAP20 and show that they are previously uncharacterized SNF genes with properties very similar to SNF8.
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