The LEF-1 High-Mobility Group Domain Undergoes a Disorder-to-Order Transition upon Formation of a Complex with Cognate DNA

Love, John J.; Li, Xiang; Chung, John; Dyson, H. Jane; Wright, Peter E.

doi:10.1021/bi049591m

Cited by 66Protein Structure and DynamicsGenomics and Chromatin DynamicsDiffusion and Search Dynamics

The LEF-1 High-Mobility Group Domain Undergoes a Disorder-to-Order Transition upon Formation of a Complex with Cognate DNA

Love, John J., Li, Xiang, Chung, John, Dyson, H. Jane, Wright, Peter E.·2004·Biochemistry

DOI 10.1021/bi049591m

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Abstract

Lymphoid enhancer-binding factor-1 (LEF-1), a member of the high-mobility group (HMG) family of proteins, functions as an architectural transcription factor. In complex with its cognate DNA, the LEF-1 domain is highly ordered, and its NMR spectra are characteristic of a folded globular protein. In contrast, the uncomplexed protein exhibits NMR evidence of substantial conformational heterogeneity, although circular dichroism spectra indicate that much of the alpha-helical secondary structure of the DNA-bound state is retained in the free protein. Heteronuclear NMR experiments performed on the free LEF-1 domain reveal that helix II and helix III of the HMG domain are folded, although helix III is truncated at its C-terminal end relative to the DNA-bound protein. The major hydrophobic core between helices II and III appears to be formed, but the minor core near the C-terminus of helix III is unstructured in the free protein. Backbone resonances of helix I are undetectable, probably as a result of exchange broadening due to fluctuations between two or more conformations on a microsecond-to-millisecond time scale. On the basis of the circular dichroism spectrum, this region of the polypeptide appears to adopt helical structure but the helix is not fully stabilized in the absence of DNA. These findings argue that, prior to binding, bending, and distorting DNA, the HMG domain of LEF-1 exists in a segmentally disordered or partially folded state. Upon complex formation, the protein domain undergoes a cooperative folding transition with DNA to a highly ordered and well-folded state.

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In the absence of DNA and β-catenin, helix I and the C-terminal end of Helix III of the LEF-1 HMG domain are unstable, fluctuating on the millisecond to microsecond timescale.
“In the absence of DNA and β-catenin, the helix I and the C-terminal end of Helix III of the LEF-1 HMG domain are unstable, fluctuating on the millisecond to microsecond timescale.”
From Intrinsically disordered proteins play diverse roles in cell signaling (2022) · cites this paper as [271]

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The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. Biochemistry 43:8725–8734
Love, J. J., Li, X., Chung, J., Dyson, H. J., & Wright, P. (2004)
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Authors: Love, J. J., Li, X., Chung, J., Dyson, H. J., & Wright, P. E.
Affiliations: Scripps Research Institute (US)
Corresponding author: Wright, Peter E.
ORCID: Love, John J.
Li, Xiang
Dyson, H. Jane
Wright, Peter E.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2004-06-15
Volume: 43
Issue: 27
Pages: 8725-8734
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi049591m
OpenAlex: W1989539099
Cited by: 66
References: 65
Citations by year: 2025: 4 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 5 · 2013: 4 · 2012: 1
FWCI: 1.78
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM-36643, R01GM036643)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Diffusion and Search Dynamics
Keywords: LEF1, high mobility group domain, disorder-to-order transition, protein-DNA complex, DNA-binding proteins, conformational heterogeneity, hydrophobic core, alpha-helical secondary structure, protein folding, transcription factors, Wnt signaling
MeSH terms: Binding Sites, Circular Dichroism, DNA, DNA-Binding Proteins, High Mobility Group Proteins, Isomerism, Models, Molecular, Peptide Fragments, Proline, Solutions, Transcription Factors, Protein Folding, Nuclear Magnetic Resonance, Biomolecular, HMG-Box Domains, Lymphoid Enhancer-Binding Factor 1

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The LEF-1 High-Mobility Group Domain Undergoes a Disorder-to-Order Transition upon Formation of a Complex with Cognate DNA

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