Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.

Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Abstract Text:

    xiaoping wangXiaoping Wang,dagmar m trucksesDagmar M Truckses,shinako takadaShinako Takada,tatsushi matsumuraTatsushi Matsumura,naoko taneseNaoko Tanese,raymond h jacobsonRaymond H Jacobson,

    TBP-associated factor 4 (TAF4), an essential subunit of the TFIID complex acts as a coactivator for multiple transcriptional regulators, including Sp1 and CREB. However, little is known regarding the structural properties of the TAF4 subunit that lead to the coactivator function. Here, we report the crystal structure at 2.0-A resolution of the human TAF4-TAFH domain, a conserved domain among all metazoan TAF4, TAF4b, and ETO family members. The hTAF4-TAFH structure adopts a completely helical fold with a large hydrophobic groove that forms a binding surface for TAF4 interacting factors. Using peptide phage display, we have characterized the binding preference of the hTAF4-TAFH domain for a hydrophobic motif, DPsiPsizetazetaPsiPhi, that is present in a number of nuclear factors, including several important transcriptional regulators with roles in activating, repressing, and modulating posttranslational modifications. A comparison of the hTAF4-TAFH structure with the homologous ETO-TAFH domain reveals several critical residues important for hTAF4-TAFH target specificity and suggests that TAF4 has evolved in response to the increased transcriptional complexity of metazoans.

    Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Publishing Authors By Initials

    x wangX Wang,dm trucksesDM Truckses,s takadaS Takada,t matsumuraT Matsumura,n taneseN Tanese,rh jacobsonRH Jacobson,

    For similar proteins: dna-binding proteins: transcription factors, general: transcription factors, tfii: transcription factor tfiid research abstracts see: proteins: dna-binding proteins: transcription factors, general: transcription factors, tfii: transcription factor tfiid research

    PUBMED ID PMID:

    MEDLINE DATE:

    Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Proceedings of the National Academy of Sciences of

    VOLUME: 104

    Page Numbers: 7839-44

    Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

    ISSN: 0027-8424

    DAY: 1

    MONTH: 05

    YEAR: 2007

    Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7505876

    Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Keywords Mesh Terms:

    KEYWORDS: Transcription Factor TFIID

    MESH TERMS: physiology

    Chemical & Substance for Abstract: Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators. Information

    Substance Name: Transcription Factor TFIID

    Registry Number: 0

    Grant and Affiliation Information for Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators.

    AFFILIATION: Department of Biochemistry and Molecular Biology, Graduate School in Biomedical Sciences Program in Genes and Development, University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: GM069769

    ACRONYM: GM

    MEDLINETA: Proc Natl Acad Sci U S A

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Conserved region I of human coactivator TAF4 binds to a short hydrophobic motif present in transcriptional regulators Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News