Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53

Teufel, Daniel P.; Freund, Stefan M.; Bycroft, Mark; Fersht, Alan R.

doi:10.1073/pnas.0702010104

Cited by 192

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53

Teufel, Daniel P., Freund, Stefan M., Bycroft, Mark, Fersht, Alan R.·2007·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0702010104

Open this paper in CoChat — free account

Abstract

The transcriptional coactivator p300 binds to and mediates the transcriptional functions of the tetrameric tumor suppressor p53. Both proteins consist of independently folded domains linked by intrinsically disordered sequences. A well studied short sequence of the p53 transactivation domain, p53(15–29), binds weakly to four folded domains of p300 [Taz1/cysteine–histidine-rich region 1 (CH1), Kix, Taz2/CH3, IBiD], with dissociation constants ( K D ) in the 100 μM region. However, we found that a longer N-terminal transactivation domain construct p53(1–57) bound tightly to each p300 domain. Taz2/CH3 had the greatest affinity ( K D = 27 nM) and competes with the N-terminal domain of Mdm2 for the p53 N terminus. p300 thus can protect the N terminus of p53 against the binding of other proteins. Mutations of p53 that abrogate transactivation (L22Q/W23S, W53Q/F54S) greatly weakened binding to each p300 domain, linking phenotypic defects to weakened coactivator binding. We propose a complex between tetrameric p53 and p300 in which four domains of p300 wrap around the four transactivation domains of p53.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1073/pnas.0702010104

Cites

8 of 8 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Surfing the p53 network
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
CBP/p300 in cell growth, transformation, and development
Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
DNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
MDMX: a novel p53‐binding protein with some functional properties of MDM2.
Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00919.x · Cited by 648
p300/MDM2 complexes participate in MDM2-mediated p53 degradation
Grossman, S. R., Perez, M., Kung, A. L., Joseph, M., Mansur, C., Xiao, Z.-X., Kumar, S., Howley, P. M., & Livingston, D. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80140-9 · Cited by 414
Core domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
Self-citation

Show all 8 references

Research works printed but not linked: 47

E Reihsaus, M Kohler, S Kraiss, M Oren, M Montenarh Oncogene 5, 137–145 (1990).
10.2174/1568009053332627 · DOI · Paper page
10.1038/42972 · DOI · Paper page
10.1016/S0092-8674(00)80304-9 · DOI · Paper page
10.1038/42981 · DOI · Paper page
10.1128/MCB.16.5.2101 · DOI
10.1074/jbc.274.20.13760 · DOI
10.1074/jbc.274.37.26321 · DOI
10.1074/jbc.M108870200 · DOI
10.1074/jbc.M211460200 · DOI
10.1074/jbc.M405974200 · doi:10.1074/jbc.m405974200
10.1074/jbc.270.42.25014 · DOI
10.1073/pnas.93.26.15335 · DOI · Paper page
10.1074/jbc.273.21.13030 · DOI
10.1038/sj.onc.1201244 · DOI · Paper page
10.1038/sj.onc.1202539 · DOI
10.1074/jbc.M210696200 · DOI
10.1006/jmbi.2000.4141 · DOI
10.1006/abbi.2000.1998 · DOI
10.1016/S0022-2836(02)00852-5 · DOI · Paper page
10.1093/embo-reports/kve025 · DOI
10.1074/jbc.273.49.33048 · DOI · Paper page
10.1128/MCB.23.23.8846-8861.2003 · DOI
10.1074/jbc.M508578200 · DOI
10.1093/nar/gki336 · DOI
10.1074/jbc.M005676200 · DOI
10.1126/science.7809597 · DOI · Paper page
10.1073/pnas.92.11.5154 · DOI · Paper page
10.1073/pnas.0504614102 · DOI · Paper page
10.1016/j.molcel.2006.05.007 · DOI · Paper page
10.1128/mcb.14.10.7013-7024.1994 · doi:10.1128/mcb.14.10.7013-7024.1994
10.1073/pnas.082121399 · DOI · Paper page
10.1073/pnas.082117899 · DOI · Paper page
10.1093/emboj/19.18.4967 · DOI · Paper page
K Roemer, N Mueller-Lantzsch Oncogene 12, 2069–2079 (1996).
10.1038/ng1498 · DOI
10.1038/ng0406-395 · DOI
10.1073/pnas.97.23.12547 · DOI · Paper page
10.1042/BJ20040564 · DOI
10.1042/BJ20041096 · DOI
10.1016/j.jmb.2004.07.042 · DOI · Paper page
10.1074/jbc.M003107200 · DOI · Paper page
TD Goddard, DG Kneller Sparky, NMR Assignment and Integration Software (Univ of California, San Francisco, Version 3.0. (2004).
10.1038/nsb0901-756 · DOI
10.1016/j.jmb.2004.06.071 · DOI · Paper page
10.1016/0014-5793(92)80300-6 · DOI · Paper page
10.1016/S1097-2765(03)00528-8 · DOI · Paper page

Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
Distinct p53 Transcriptional Programs Dictate Acute DNA-Damage Responses and Tumor Suppression
Brady, C. A., Jiang, D., Mello, S. S., Johnson, T. M., Jarvis, L. A., Kozak, M. M., Broz, D. K., Basak, S., Park, E. J., McLaughlin, M. E., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.035 · Cited by 533
Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others
Sabapathy, K., & Lane, D. P. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.151 · Cited by 517
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Self-citation

See all 192

Authors: Teufel, D. P., Freund, S. M., Bycroft, M., & Fersht, A. R.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2007-04-24
Volume: 104
Issue: 17
Pages: 7009-7014
ISSN: 0027-8424
1091-6490
DOI: 10.1073/pnas.0702010104
Cited by: 192
References: 8
Language: en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page: CoChat. (2026). Citation check: Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. https://app.cochat.ai/papers/10.1073/pnas.0702010104
The paper: Teufel, D. P., Freund, S. M., Bycroft, M., & Fersht, A. R. (2007). Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0702010104

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

How to cite

Data sources