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EKLF/KLF1 is ubiquitinated in vivo and its stability is regulated by activation domain sequences through the 26S proteasome
Author(s) -
Quadrini Karen J.,
Bieker James J.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.039
Subject(s) - ubiquitin , microbiology and biotechnology , zinc finger , transcription factor , proteasome , chromatin , chemistry , in vivo , biology , gene , biochemistry , genetics
Erythroid Krüppel‐like factor (EKLF/KLF1) is an erythroid specific, C 2 H 2 zinc finger transcription factor that is essential for the proper chromatin structure and expression of the adult β‐globin gene. Herein, we determine that 26S proteasome inhibitors lead to an accumulation of EKLF protein in murine erythroleukemia (MEL) cells. In addition, EKLF half‐life in both MEL cells (<3 h) and fetal liver cells (between 6 and 9 h) is stabilized in the presence of these inhibitors. EKLF is ubiquitinated in vivo, however its modification does not rely on a particular internal lysine. Finally, EKLF contains two PEST sequences within its N‐terminus that have no effect on the ability of EKLF to be ubiquitinated but contribute to its destabilization.