Structural and functional characterization of an atypical activation domain in erythroid Krüppel-like factor (EKLF)

DOI Web Site 被引用文献6件
  • Caroline Mas
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • Mathieu Lussier-Price
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • Shefali Soni
    Department of Developmental and Regenerative Biology, Mount Sinai School of Medicine, Box 1020, One Gustave Levy Place, New York, NY 10029
  • Thomas Morse
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • Geneviève Arseneault
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • Paola Di Lello
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • Julien Lafrance-Vanasse
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and
  • James J. Bieker
    Department of Developmental and Regenerative Biology, Mount Sinai School of Medicine, Box 1020, One Gustave Levy Place, New York, NY 10029
  • James G. Omichinski
    Département de Biochimie, Université de Montréal, C.P. 6128 Succursale Centre-Ville, Montréal, Canada QC H3C 3J7; and

説明

<jats:p>Erythroid Krüppel-like factor (EKLF) plays an important role in erythroid development by stimulating β-globin gene expression. We have examined the details by which the minimal transactivation domain (TAD) of EKLF (EKLFTAD) interacts with several transcriptional regulatory factors. We report that EKLFTAD displays homology to the p53TAD and, like the p53TAD, can be divided into two functional subdomains (EKLFTAD1 and EKLFTAD2). Based on sequence analysis, we found that EKLFTAD2 is conserved in KLF2, KLF4, KLF5, and KLF15. In addition, we demonstrate that EKLFTAD2 binds the amino-terminal PH domain of the Tfb1/p62 subunit of TFIIH (Tfb1PH/p62PH) and four domains of CREB-binding protein/p300. The solution structure of the EKLFTAD2/Tfb1PH complex indicates that EKLFTAD2 binds Tfb1PH in an extended conformation, which is in contrast to the α-helical conformation seen for p53TAD2 in complex with Tfb1PH. These studies provide detailed mechanistic information into EKLFTAD functions as well as insights into potential interactions of the TADs of other KLF proteins. In addition, they suggest that not only have acidic TADs evolved so that they bind using different conformations on a common target, but that transitioning from a disordered to a more ordered state is not a requirement for their ability to bind multiple partners.</jats:p>

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