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A sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.

Although many transcription activators contact the same set of coactivator complexes, the mechanism and specificity of these interactions have been unclear. For example, do intrinsically disordered transcription activation domains (ADs) use sequence-specific motifs, or do ADs of seemingly different... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America August 26, 2014, Vol.111(34), pp.E3506-E3513
Main Author: Warfield, Linda
Other Authors: Tuttle, Lisa M , Pacheco, Derek , Klevit, Rachel E , Hahn, Steven
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1412088111
Link: http://search.proquest.com/docview/1558521864/?pq-origsite=primo
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recordid: proquest1558521864
title: A sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.
format: Article
creator:
  • Warfield, Linda
  • Tuttle, Lisa M
  • Pacheco, Derek
  • Klevit, Rachel E
  • Hahn, Steven
subjects:
  • Amino Acid Sequence–Chemistry
  • Amino Acid Substitution–Genetics
  • Basic-Leucine Zipper Transcription Factors–Metabolism
  • Hydrophobic and Hydrophilic Interactions–Chemistry
  • Kinetics–Genetics
  • Mediator Complex–Metabolism
  • Models, Molecular–Chemistry
  • Molecular Sequence Data–Metabolism
  • Multiprotein Complexes–Chemistry
  • Mutagenesis, Site-Directed–Genetics
  • Nuclear Magnetic Resonance, Biomolecular–Metabolism
  • Protein Binding–Genetics
  • Protein Interaction Domains and Motifs–Metabolism
  • Recombinant Proteins–Chemistry
  • Saccharomyces Cerevisiae–Genetics
  • Saccharomyces Cerevisiae Proteins–Metabolism
  • Transcriptional Activation–Metabolism
  • Basic-Leucine Zipper Transcription Factors
  • Gal11 Protein, S Cerevisiae
  • Gcn4 Protein, S Cerevisiae
ispartof: Proceedings of the National Academy of Sciences of the United States of America, August 26, 2014, Vol.111(34), pp.E3506-E3513
description: Although many transcription activators contact the same set of coactivator complexes, the mechanism and specificity of these interactions have been unclear. For example, do intrinsically disordered transcription activation domains (ADs) use sequence-specific motifs, or do ADs of seemingly different sequence have common properties that encode activation function? We find that the central activation domain (cAD) of the yeast activator Gcn4 functions through a short, conserved sequence-specific motif. Optimizing the residues surrounding this short motif by inserting additional hydrophobic residues creates very powerful ADs that bind the Mediator subunit Gal11/Med15 with high affinity via a "fuzzy" protein interface. In contrast to Gcn4, the activity of these synthetic ADs is not strongly dependent on any one residue of the AD, and this redundancy is similar to that of some natural ADs in which few if any sequence-specific residues have been identified. The additional hydrophobic residues in the synthetic ADs likely allow multiple faces of the AD helix to interact with the Gal11 activator-binding domain, effectively forming a fuzzier interface than that of the wild-type cAD.
language: eng
source:
identifier: E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1412088111
fulltext: fulltext
issn:
  • 10916490
  • 1091-6490
url: Link


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titleA sequence-specific transcription activator motif and powerful synthetic variants that bind Mediator using a fuzzy protein interface.
creatorWarfield, Linda ; Tuttle, Lisa M ; Pacheco, Derek ; Klevit, Rachel E ; Hahn, Steven
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ispartofProceedings of the National Academy of Sciences of the United States of America, August 26, 2014, Vol.111(34), pp.E3506-E3513
identifierE-ISSN: 1091-6490 ; DOI: 10.1073/pnas.1412088111
subjectAmino Acid Sequence–Chemistry ; Amino Acid Substitution–Genetics ; Basic-Leucine Zipper Transcription Factors–Metabolism ; Hydrophobic and Hydrophilic Interactions–Chemistry ; Kinetics–Genetics ; Mediator Complex–Metabolism ; Models, Molecular–Chemistry ; Molecular Sequence Data–Metabolism ; Multiprotein Complexes–Chemistry ; Mutagenesis, Site-Directed–Genetics ; Nuclear Magnetic Resonance, Biomolecular–Metabolism ; Protein Binding–Genetics ; Protein Interaction Domains and Motifs–Metabolism ; Recombinant Proteins–Chemistry ; Saccharomyces Cerevisiae–Genetics ; Saccharomyces Cerevisiae Proteins–Metabolism ; Transcriptional Activation–Metabolism ; Basic-Leucine Zipper Transcription Factors ; Gal11 Protein, S Cerevisiae ; Gcn4 Protein, S Cerevisiae
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descriptionAlthough many transcription activators contact the same set of coactivator complexes, the mechanism and specificity of these interactions have been unclear. For example, do intrinsically disordered transcription activation domains (ADs) use sequence-specific motifs, or do ADs of seemingly different sequence have common properties that encode activation function? We find that the central activation domain (cAD) of the yeast activator Gcn4 functions through a short, conserved sequence-specific motif. Optimizing the residues surrounding this short motif by inserting additional hydrophobic residues creates very powerful ADs that bind the Mediator subunit Gal11/Med15 with high affinity via a "fuzzy" protein interface. In contrast to Gcn4, the activity of these synthetic ADs is not strongly dependent on any one residue of the AD, and this redundancy is similar to that of some natural ADs in which few if any sequence-specific residues have been identified. The additional hydrophobic residues in the synthetic ADs likely allow multiple faces of the AD helix to interact with the Gal11 activator-binding domain, effectively forming a fuzzier interface than that of the wild-type cAD.
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