دورية أكاديمية
A Potential Structural Switch for Regulating DNA-Binding by TEAD Transcription Factors.
العنوان: | A Potential Structural Switch for Regulating DNA-Binding by TEAD Transcription Factors. |
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المؤلفون: | Lee DS; Jeju National University, 102 Jejudaehak-ro, Jeju-si, Jeju Special Self-Governing Province, 690-756, South Korea., Vonrhein C; Global Phasing Limited, Sheraton House, Castle Park, Cambridge CB3 0AX, UK., Albarado D; Pennington Biomedical Research Center, 6400 Perkins Rd, Baton Rouge, LA 70808, USA., Raman CS; University of Maryland School of Pharmacy, 20 N. Pine St., Baltimore, MD 21201, USA., Veeraraghavan S; University of Maryland School of Pharmacy, 20 N. Pine St., Baltimore, MD 21201, USA. Electronic address: sudha.veeraraghavan@gmail.com. |
المصدر: | Journal of molecular biology [J Mol Biol] 2016 Jun 19; Vol. 428 (12), pp. 2557-2568. Date of Electronic Publication: 2016 Mar 22. |
نوع المنشور: | Journal Article |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE |
أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: 1959- : London : Academic Press |
مواضيع طبية MeSH: | DNA/*metabolism , DNA-Binding Proteins/*metabolism , Transcription Factors/*metabolism, Amino Acid Sequence ; Dimerization ; Escherichia coli/metabolism ; Protein Binding/physiology ; Protein Structure, Tertiary |
مستخلص: | TEA domain (TEAD) transcription factors are essential for the normal development of eukaryotes and are the downstream effectors of the Hippo tumor suppressor pathway. Whereas our earlier work established the three-dimensional structure of the highly conserved DNA-binding domain using solution NMR spectroscopy, the structural basis for regulating the DNA-binding activity remains unknown. Here, we present the X-ray crystallographic structure and activity of a TEAD mutant containing a truncated L1 loop, ΔL1 TEAD DBD. Unexpectedly, the three-dimensional structure of the ΔL1 TEAD DBD reveals a helix-swapped homodimer wherein helix 1 is swapped between monomers. Furthermore, each three-helix bundle in the domain-swapped dimer is a structural homolog of MYB-like domains. Our investigations of the DNA-binding activity reveal that although the formation of the three-helix bundle by the ΔL1 TEAD DBD is sufficient for binding to an isolated M-CAT-like DNA element, multimeric forms are deficient for cooperative binding to tandemly duplicated elements, indicating that the L1 loop contributes to the DNA-binding activity of TEAD. These results suggest that switching between monomeric and domain-swapped forms may regulate DNA selectivity of TEAD proteins. (Copyright © 2016 Elsevier Ltd. All rights reserved.) |
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معلومات مُعتمدة: | R01 GM084700 United States GM NIGMS NIH HHS |
فهرسة مساهمة: | Keywords: Hippo pathway; TEAD; X-ray crystallography; domain swapping; transcription factor |
المشرفين على المادة: | 0 (DNA-Binding Proteins) 0 (Transcription Factors) 9007-49-2 (DNA) |
تواريخ الأحداث: | Date Created: 20160327 Date Completed: 20170612 Latest Revision: 20201209 |
رمز التحديث: | 20221213 |
مُعرف محوري في PubMed: | PMC4893915 |
DOI: | 10.1016/j.jmb.2016.03.008 |
PMID: | 27016204 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1089-8638 |
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DOI: | 10.1016/j.jmb.2016.03.008 |