دورية أكاديمية
أعرض في EDS

A Potential Structural Switch for Regulating DNA-Binding by TEAD Transcription Factors.

التفاصيل البيبلوغرافية
العنوان: A Potential Structural Switch for Regulating DNA-Binding by TEAD Transcription Factors.
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.)
References: Immunity. 2011 Apr 22;34(4):479-91. (PMID: 21458306)
Biochim Biophys Acta. 2012 Jan;1819(1):67-77. (PMID: 22067744)
Dev Genet. 1998;22(1):43-55. (PMID: 9499579)
Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1204-14. (PMID: 23793146)
Curr Opin Struct Biol. 1997 Jun;7(3):416-21. (PMID: 9204285)
J Mol Biol. 2012 Jan 6;415(1):221-35. (PMID: 22079367)
Acta Crystallogr D Biol Crystallogr. 2006 Jan;62(Pt 1):72-82. (PMID: 16369096)
Curr Opin Struct Biol. 2009 Feb;19(1):39-49. (PMID: 19162470)
Proc Natl Acad Sci U S A. 1988 Sep;85(17):6404-8. (PMID: 3413104)
Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1002-11. (PMID: 16929101)
J Biol Chem. 2001 Mar 30;276(13):10413-22. (PMID: 11136726)
Cell. 1988 Sep 23;54(7):931-42. (PMID: 2843293)
Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):2023-30. (PMID: 14573958)
Development. 2001 Sep;128(17):3295-305. (PMID: 11546746)
DNA Cell Biol. 2000 Aug;19(8):507-14. (PMID: 10975468)
Curr Opin Struct Biol. 2002 Feb;12(1):48-53. (PMID: 11839489)
Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):903-9. (PMID: 12777808)
Protein J. 2015 Apr;34(2):111-21. (PMID: 25724387)
Structure. 2013 Apr 2;21(4):638-49. (PMID: 23523426)
Trends Biochem Sci. 1995 Nov;20(11):478-80. (PMID: 8578593)
Mol Cell Biol. 1990 Aug;10(8):4271-83. (PMID: 2370866)
J Biol Chem. 1994 Feb 4;269(5):3147-50. (PMID: 8106348)
Nucleic Acids Res. 2010 Jul;38(Web Server issue):W545-9. (PMID: 20457744)
Proc Natl Acad Sci U S A. 2006 Nov 14;103(46):17225-30. (PMID: 17085591)
Cell Death Differ. 2012 Feb;19(2):220-31. (PMID: 21701496)
Biochem Biophys Res Commun. 2002 Jun 21;294(4):791-7. (PMID: 12061776)
Nucleic Acids Res. 2003 Jul 1;31(13):3784-8. (PMID: 12824418)
Cell. 1991 Jul 12;66(1):11-2. (PMID: 2070413)
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):293-302. (PMID: 21460447)
Proteins. 2006 Dec 1;65(4):1041-5. (PMID: 17044043)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32. (PMID: 20124692)
J Biol Chem. 1997 Apr 18;272(16):10664-8. (PMID: 9099715)
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
الوصف
تدمد:1089-8638
DOI:10.1016/j.jmb.2016.03.008