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

Erythroid Kruppel-like factor (EKLF) plays an important role in erythroid development by stimulating [beta]-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 th... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America June 28, 2011, Vol.108(26), pp.10484-10489
Main Author: Mas, Caroline
Other Authors: Lussier-Price, Mathieu , Soni, Shefali , Morse, Thomas , Arseneault, Geneviève , Di Lello, Paola , Lafrance-Vanasse, Julien , Bieker, James J , Omichinski, James G
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1017029108
Link: http://search.proquest.com/docview/874297579/?pq-origsite=primo
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title: Structural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF).
format: Article
creator:
  • Mas, Caroline
  • Lussier-Price, Mathieu
  • Soni, Shefali
  • Morse, Thomas
  • Arseneault, Geneviève
  • Di Lello, Paola
  • Lafrance-Vanasse, Julien
  • Bieker, James J
  • Omichinski, James G
subjects:
  • Amino Acid Sequence–Chemistry
  • Binding Sites–Genetics
  • Calorimetry–Metabolism
  • Cloning, Molecular–Metabolism
  • Humans–Metabolism
  • K562 Cells–Metabolism
  • Kruppel-Like Transcription Factors–Metabolism
  • Models, Molecular–Metabolism
  • Molecular Sequence Data–Metabolism
  • Mutagenesis, Site-Directed–Metabolism
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Protein Binding–Metabolism
  • Protein Conformation–Metabolism
  • Sequence Homology, Amino Acid–Metabolism
  • Transcription Factors–Metabolism
  • Kruppel-Like Transcription Factors
  • Transcription Factors
  • Erythroid Kruppel-Like Factor
ispartof: Proceedings of the National Academy of Sciences of the United States of America, June 28, 2011, Vol.108(26), pp.10484-10489
description: Erythroid Kruppel-like factor (EKLF) plays an important role in erythroid development by stimulating [beta]-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 [alpha]-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. hematopoiesis | NMR spectroscopy | transcriptional activators | intrinsically unstructured domain | transcription factor lie doi/ 10.1073/pnas.1017029108
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1017029108
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleStructural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF).
creatorMas, Caroline ; Lussier-Price, Mathieu ; Soni, Shefali ; Morse, Thomas ; Arseneault, Geneviève ; Di Lello, Paola ; Lafrance-Vanasse, Julien ; Bieker, James J ; Omichinski, James G
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identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1017029108
subjectAmino Acid Sequence–Chemistry ; Binding Sites–Genetics ; Calorimetry–Metabolism ; Cloning, Molecular–Metabolism ; Humans–Metabolism ; K562 Cells–Metabolism ; Kruppel-Like Transcription Factors–Metabolism ; Models, Molecular–Metabolism ; Molecular Sequence Data–Metabolism ; Mutagenesis, Site-Directed–Metabolism ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Protein Binding–Metabolism ; Protein Conformation–Metabolism ; Sequence Homology, Amino Acid–Metabolism ; Transcription Factors–Metabolism ; Kruppel-Like Transcription Factors ; Transcription Factors ; Erythroid Kruppel-Like Factor
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descriptionErythroid Kruppel-like factor (EKLF) plays an important role in erythroid development by stimulating [beta]-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 [alpha]-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. hematopoiesis | NMR spectroscopy | transcriptional activators | intrinsically unstructured domain | transcription factor lie doi/ 10.1073/pnas.1017029108
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titleStructural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF).
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titleStructural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF).
authorMas, Caroline ; Lussier-Price, Mathieu ; Soni, Shefali ; Morse, Thomas ; Arseneault, Geneviève ; Di Lello, Paola ; Lafrance-Vanasse, Julien ; Bieker, James J ; Omichinski, James G
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