Cited by 315Protein Structure and DynamicsGenomics and Chromatin DynamicsDNA and Nucleic Acid Chemistry

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A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex

Kodandapani, Ramadurgam, Pio, Frédéric, Ni, Chao-Zhou, Piccialli, Gennaro, Klemsz, Michael, McKercher, Scott, Maki, Richard A., Ely, Kathryn R.·1996·Nature

DOI 10.1038/380456a0

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Abstract

The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction
Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., & Pease, L. R. (1989) · Gene · doi:10.1016/0378-1119(89)90358-2 · Cited by 7,354
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,950
Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement
Engh, R., & Huber, R. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767391001071 · Cited by 2,497
Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
Clark, K., Halay, E. D., Lai, E., & Burley, S. K. (1993) · Nature · doi:10.1038/364412a0 · Cited by 1,275
Crystal Structure of a CAP-DNA Complex: the DNA Is Bent by 90°
Schultz, S. C., Shields, G. C., & Steitz, T. A. (1991) · Science · doi:10.1126/science.1653449 · Cited by 1,116
Resolution of phase ambiguity in macromolecular crystallography
Wang, B. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)15009-3 · Cited by 1,033
The macrophage and B cell-specific transcription factor PU.1 is related to the ets oncogene
Klemsz, M. J., McKercher, S. R., Celada, A., Van Beveren, C., & Maki, R. A. (1990) · Cell · doi:10.1016/0092-8674(90)90219-5 · Cited by 954
Self-citation
The Ets family of transcription factors
Wasylyk, B., Hahn, S. L., & Giovane, A. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb19864.x · Cited by 839
Interactive computer graphics: FRODO
Jones, T. A. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)15014-7 · Cited by 825

Flagged first, then by citations

Show all 23 references

Research works printed but not linked: 7

Moreau-Gachelin, F. Biochim. biophys. Acta 1198, 149–163 (1994).
Moreau-Gachelin, F., Mattei, M. G., Tambourin, R. & Tavitian, A. Oncogene 4, 1449–1456 (1989).
Mavrothalassitis, G., Fisher, R. J., Smyth, F., Watson, D. K. & Papas, T. S. Oncogens 9, 425–435 (1994).
Furey, W. & Swaminathan, S. Am. crystallogr. Ass. Meeting 18, 73 (1990).
Jones, T. A., Zhou, J., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1992).
Brünger, A. T. X-PLOR Manual Version 3.1 (Yale Univ. Press, New Haven, CT, 1992).
Parkinson, G., Vojtechovsky, J., Clowney, L., Brünger, A. T. & Berman, H. M. Acta crystallogr. D52, 57–64 (1996).

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Background
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Background
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Self-citation
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Kamath, M. B., Houston, I. B., Janovski, A. J., Zhu, X., Gowrisankar, S., Jegga, A. G., & DeKoter, R. P. (2008) · Leukemia · doi:10.1038/leu.2008.67 · Cited by 41
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Recent advances in the structural molecular biology of Ets transcription factors: interactions, interfaces and inhibition
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Bai, Y., Srinivasan, L., Perkins, L., & Atchison, M. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5160 · Cited by 39
Cooperative interaction between the DNA-binding domains of PU.1 and IRF4
Yee, A. A., Yin, P., Siderovski, D. P., Mak, T. W., Litchfield, D. W., & Arrowsmith, C. H. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1838 · Cited by 38
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Stephens, D. C., Kim, H. M., Kumar, A., Farahat, A. A., Boykin, D. W., & Poon, G. M. K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw229 · Cited by 38
Identification of an ETV6–ABL2 fusion transcript in combination with an ETV6 point mutation in a T‐cell acute lymphoblastic leukaemia cell line
Griesinger, F., Janke, A., Podleschny, M., & Bohlander, S. K. (2002) · British Journal of Haematology · doi:10.1046/j.1365-2141.2002.03850.x · Cited by 38
“The three-dimensional structures of the PU.1 and ETS1 ets domains shows that the homologous arginine residue in these ets domains is one of the two arginine residues making contact with the core ets DNA binding site (Kodandapani et al, 1996; Werner et al, 1997).”
Background
Pax6 and Cdx2/3 form a functional complex on the rat glucagon gene promoter G1‐element
Andersen, F. G., Heller, R. S., Petersen, H. V., Jensen, J. N., Madsen, O. D., & Serup, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00145-3 · Cited by 38
Differential sensitivity to methylated DNA by ETS-family transcription factors is intrinsically encoded in their DNA-binding domains
Stephens, D. C., & Poon, G. M. K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw528 · Cited by 37
Ets1 and Elk1 transcription factors regulatecancerous inhibitor of protein phosphatase 2Aexpression in cervical and endometrial carcinoma cells
Pallai, R., Bhaskar, A., Sodi, V. L., & Rice, L. M. (2012) · Transcription · doi:10.4161/trns.22518 · Cited by 41
Expression Pattern of the Ets-related Transcription Factor Elf-1
Bassuk, A. G., Barton, K., Anandappa, R. T., Lu, M. M., & Leiden, J. M. (1998) · Molecular Medicine · doi:10.1007/bf03401746 · Cited by 36
The Transcription Factor Sp1 Regulates the Myeloid-specific Expression of the Human Hematopoietic Cell Kinase (HCK) Gene through Binding to Two Adjacent GC Boxes within the HCK Promoter-Proximal Region
Hauses, M., Tönjes, R. R., & Grez, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.31844 · Cited by 35
Autoinhibition as a Transcriptional Regulatory MechanismPreprint
Graves, B. J., Cowley, D. O., Goetz, T. L., Petersen, J. M., Jonsen, M. D., & Gillespie, M. E. (1998) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1998.63.621 · Cited by 35
Dynamic and Structural Modeling of the Specificity in Protein–DNA Interactions Guided by Binding Assay and Structure Data
Tan, C., & Takada, S. (2018) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.8b00299 · Cited by 35
The transcription factor PU.1 mediates enhancer-promoter looping that is required for IL-1β eRNA and mRNA transcription in mouse melanoma and macrophage cell lines
Ha, S.-D., Cho, W., DeKoter, R. P., & Kim, S. O. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010149 · Cited by 36
“The residues Arg-230 and Arg-233 have been shown to be crucial for GGAA sequence–specific DNA binding and nuclear localization (65, 66); therefore, it is not surprising that R230A/ R233A mutant failed to induce the looping.”
Background
Identification and characterization of a PU.1/Spi-B binding site in the bovine leukemia virus long terminal repeat
Dekoninck, A., Calomme, C., Nizet, S., de Launoit, Y., Burny, A., Ghysdael, J., & Lint, C. M. V. (2003) · Oncogene · doi:10.1038/sj.onc.1206392 · Cited by 35
“…studies emphasize the importance of the sequences flanking the GGAA core for PU.1 binding by showing that the PU.1 ETS domain forms a series of specific contacts with both the GGAA core sequence and the nucleotides 30 and 50 to this core sequence (Kodandapani et al., 1996; Pio et al., 1996).”
Background
Secretory Interleukin-1 Receptor Antagonist Gene Expression Requires both a PU.1 and a Novel Composite NF-κB/PU.1/ GA-binding Protein Binding Site
Smith, M. F., Carl, V. S., Lodie, T. A., & Fenton, M. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.24272 · Cited by 35
Correlated Motions and Interactions at the Onset of the DNA-Induced Partial Unfolding of Ets-1
Kamberaj, H., & van der Vaart, A. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.019 · Cited by 35
Inner Workings of a Transcription Factor Partnership
Graves, B. J. (1998) · Science · doi:10.1126/science.279.5353.1000 · Cited by 34
Structural insights into the interaction between transcription factors and the nucleosome
Morgunova, E. Y., & Taipale, J. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.06.016 · Cited by 32
Mitf–PU.1 interactions with the tartrate-resistant acid phosphatase gene promoter during osteoclast differentiation
Partington, G. A., Fuller, K., Chambers, T. J., & Pondel, M. D. (2003) · Bone · doi:10.1016/j.bone.2003.11.010 · Cited by 33
“1 is reported to be GAGGAA [48,49].”
Role of Asymmetric Phosphate Neutralization in DNA Bending by PU.1
Strauss-Soukup, J. K., & Maher, L. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31570 · Cited by 31
Pax-5/BSAP: Regulator of Specific Gene Expression and Differentiation in B Lymphocytes
Hagman, J. R., Wheat, W. H., Fitzsimmons, D., Hodsdon, W., Negri, J. A., & Dizon, F. (2000) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-57066-7_5 · Cited by 30
Identification of Residues of the Caenorhabditis elegans LIN-1 ETS Domain That Are Necessary for DNA Binding and Regulation of Vulval Cell Fates
Miley, G. R., Fantz, D., Glossip, D., Lu, X., Saito, R. M., Palmer, R. E., Inoue, T., van den Heuvel, S., Sternberg, P. W., & Kornfeld, K. (2004) · Genetics · doi:10.1534/genetics.104.029017 · Cited by 28
“K.K. is a scholar of the Leukemia and Lymphoma Society.making glycine substitutions (Kodandapani et al. 1996).”
Background
Spi-1/PU.1 Oncoprotein Affects Splicing Decisions in a Promoter Binding-dependent Manner
Guillouf, C., Gallais, I., & Moreau-Gachelin, F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512049200 · Cited by 37
Mechanistic Heterogeneity in Site Recognition by the Structurally Homologous DNA-binding Domains of the ETS Family Transcription Factors Ets-1 and PU.1
Wang, S., Linde, M. H., Munde, M. M., Carvalho, V. D., Wilson, W. D., & Poon, G. M. K. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.575340 · Cited by 29
Analysis of the 2.0 Å Crystal Structure of the Protein−DNA Complex of the Human PDEF Ets Domain Bound to the Prostate Specific Antigen Regulatory Site,
Wang, Y., Feng, L., Said, M., Balderman, S., Fayazi, Z. S., Liu, Y., Ghosh, D., & Gulick, A. M. (2005) · Biochemistry · doi:10.1021/bi047352t · Cited by 29
Base Coupling in Sequence-specific Site Recognition by the ETS Domain of Murine PU.1
Poon, G. M. K., & Macgregor, R. B. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00362-0 · Cited by 29
Ulmoidol, an unusual nortriterpenoid from Eucommia ulmoides Oliv. Leaves prevents neuroinflammation by targeting the PU.1 transcriptional signaling pathway
Han, R., Yuan, T., Yang, Z. H., Zhang, Q., Wang, W., Lin, L., Zhu, M.-Q., & Gao, J. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105345 · Cited by 30
Sequence Discrimination by DNA-binding Domain of ETS Family Transcription Factor PU.1 Is Linked to Specific Hydration of Protein-DNA Interface
Poon, G. M. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342345 · Cited by 28
DNA binding by the ETS domain
Graves, B. J., Gillespie, M. E., & Mclntosh, L. P. (1996) · Nature · doi:10.1038/384322a0 · Cited by 28
Pentaprobe: a comprehensive sequence for the one-step detection of DNA-binding activities
Kwan, A. H. (2003) · Nucleic Acids Research · doi:10.1093/nar/gng124 · Cited by 28
The transcription factor PU.1 does not regulate lineage commitment but has lineage-specific effects
McKercher, S. R., Henkel, G. W., & Maki, R. A. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.5.727 · Cited by 28
Self-citation
Crystal Structure of Mouse Elf3 C-terminal DNA-binding Domain in Complex with Type II TGF-β Receptor Promoter DNA
Agarkar, V. B., Babayeva, N. D., Wilder, P. J., Rizzino, A., & Tahirov, T. H. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.01.017 · Cited by 27
Prf, a novel Ets family protein that binds to the PU.1 binding motif, is specifically expressed in restricted stages of B cell development
Hashimoto, S., Nishizumi, H., Hayashi, R., Tsuboi, A., Nagawa, F., Takemori, T., & Sakano, H. (1999) · International Immunology · doi:10.1093/intimm/11.9.1423 · Cited by 27
The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove.
Clubb, R. T., Wojciak, J. M., & Iwahara, J. (2001) · Nature Structural Biology · doi:10.1038/83103 · Cited by 27
Signatures of DNA target selectivity by ETS transcription factors
Poon, G. M. K., & Kim, H. M. (2017) · Transcription · doi:10.1080/21541264.2017.1302901 · Cited by 27
Upregulation of the pathogenic transcription factor SPI1/PU.1 in tuberous sclerosis complex and focal cortical dysplasia by oxidative stress
Zimmer, T. S., Korotkov, A., Zwakenberg, S., Jansen, F. E., Zwartkruis, F. J. T., Rensing, N. R., Wong, M., Mühlebner, A., van Vliet, E. A., Aronica, E., et al. (2021) · Brain Pathology · doi:10.1111/bpa.12949 · Cited by 27

Authors: Kodandapani, R., Pio, F., Ni, C.-Z., Piccialli, G., Klemsz, M., McKercher, S., Maki, R. A., & Ely, K. R.
Affiliations: Sanford Burnham Prebys Medical Discovery Institute (US)
University of Naples Federico II (IT)
Indiana University School of Medicine (US)
ORCID: Pio, Frédéric
Piccialli, Gennaro
Maki, Richard A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1996-04
Volume: 380
Issue: 6573
Pages: 456-460
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/380456a0
OpenAlex: W1985177466
Cited by: 315
References: 23
Citations by year: 2026: 5 · 2025: 9 · 2024: 2 · 2023: 4 · 2022: 10 · 2021: 6 · 2020: 2 · 2019: 3 · 2018: 6 · 2017: 8 · 2016: 10 · 2015: 7 · 2014: 6 · 2013: 7 · 2012: 7
FWCI: 12.37
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
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 › DNA and Nucleic Acid Chemistry
Keywords: ETS transcription factors, ETS domain, DNA-binding domain, helix-turn-helix motif, winged helix-turn-helix, DNA recognition sequence, protein-DNA complex, crystal structure, major groove, transcriptional regulation
MeSH terms: Amino Acid Sequence, Animals, DNA, DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Retroviridae Proteins, Oncogenic, Sequence Homology, Amino Acid, Crystallography, X-Ray, Helix-Turn-Helix Motifs

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A new pattern for helix–turn–helix recognition revealed by the PU.l ETS–domain–DNA complex

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