Structural Basis of DNA Recognition by p53 Tetramers

Kitayner, Malka; Rozenberg, Haim; Kessler, Naama; Rabinovich, Dov; Shaulov, Lihi; Haran, Tali E.; Shakked, Zippora

doi:10.1016/j.molcel.2006.05.015

Cited by 408Cancer-related Molecular PathwaysProtein Structure and DynamicsDNA and Nucleic Acid Chemistry

Structural Basis of DNA Recognition by p53 Tetramers

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Kitayner, Malka, Rozenberg, Haim, Kessler, Naama, Rabinovich, Dov, Shaulov, Lihi, Haran, Tali E., Shakked, Zippora·2006·Molecular Cell

DOI 10.1016/j.molcel.2006.05.015

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Abstract

The tumor-suppressor protein p53 is among the most effective of the cell's natural defenses against cancer. In response to cellular stress, p53 binds as a tetramer to diverse DNA targets containing two decameric half-sites, thereby activating the expression of genes involved in cell-cycle arrest or apoptosis. Here we present high-resolution crystal structures of sequence-specific complexes between the core domain of human p53 and different DNA half-sites. In all structures, four p53 molecules self-assemble on two DNA half-sites to form a tetramer that is a dimer of dimers, stabilized by protein-protein and base-stacking interactions. The protein-DNA interface varies as a function of the specific base sequence in correlation with the measured binding affinities of the complexes. The new data establish a structural framework for understanding the mechanisms of specificity, affinity, and cooperativity of DNA binding by p53 and suggest a model for its regulation by regions outside the sequence-specific DNA binding domain.

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Typically, p53 binds to target genes as a tetramer comprising two dimers, each binding a decameric half-site with the consensus sequence RRRCWWGYYY.
“Typically, p53 binds to the target genes as a tetramer, which comprises two dimers that each binds a decameric half-site with the consensus sequence RRRCWWGYYY (R = A/G, W = A/T, Y = C/T).7, 8, 9, 10”
From Census and evaluation of p53 target genes (2017) · cites this paper as [9]

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Authors: Kitayner, M., Rozenberg, H., Kessler, N., Rabinovich, D., Shaulov, L., Haran, T. E., & Shakked, Z.
Affiliations: Weizmann Institute of Science (IL)
Technion – Israel Institute of Technology (IL)
Corresponding author: Haran, Tali E.
Shakked, Zippora
ORCID: Rozenberg, Haim
Kessler, Naama
Haran, Tali E.
Shakked, Zippora
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2006-06
Volume: 22
Issue: 6
Pages: 741-753
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2006.05.015
OpenAlex: W2168497623
Cited by: 408
References: 68
Citations by year: 2026: 18 · 2025: 17 · 2024: 15 · 2023: 17 · 2022: 28 · 2021: 26 · 2020: 27 · 2019: 27 · 2018: 17 · 2017: 18 · 2016: 19 · 2015: 13 · 2014: 9 · 2013: 22 · 2012: 22
FWCI: 12.14
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2639 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: p53, DNA binding, protein-DNA complex, tetramer, crystal structure, base stacking, protein-protein interaction, binding affinity, sequence specificity, cooperativity, tumor suppressor
MeSH terms: Binding Sites, Cell Cycle, DNA, Models, Molecular, Neoplasms, Protein Binding, Structure-Activity Relationship, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Apoptosis, Protein Structure, Tertiary, Crystallography, X-Ray, Protein Structure, Quaternary

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Structural Basis of DNA Recognition by p53 Tetramers

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