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

Takumi Kamura, Dennis Burian, Hamed Khalili, Susan L. Schmidt, Shigeo Sato, Wen Jun Liu, Michael N. Conrad, Ronald C. Conaway, Joan Weliky Conaway, Ali Shilatifard*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

Abstract

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 ∼45 (EAP45), ∼30 (EAP30), and ∼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.

Original languageEnglish (US)
Pages (from-to)16528-16533
Number of pages6
JournalJournal of Biological Chemistry
Volume276
Issue number19
DOIs
StatePublished - May 11 2001

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Cloning and Characterization of ELL-associated Proteins EAP45 and EAP20: A role for yeast EAP-like proteins in regulation of gene expression by glucose'. Together they form a unique fingerprint.

Cite this