Recognition of AT-Rich DNA Binding Sites by the MogR Repressor
Open accessAbstract
The MogR transcriptional repressor of the intracellular pathogen Listeria monocytogenes recognizes AT-rich binding sites in promoters of flagellar genes to downregulate flagellar gene expression during infection. We describe here the 1.8 A resolution crystal structure of MogR bound to the recognition sequence 5' ATTTTTTAAAAAAAT 3' present within the flaA promoter region. Our structure shows that MogR binds as a dimer. Each half-site is recognized in the major groove by a helix-turn-helix motif and in the minor groove by a loop from the symmetry-related molecule, resulting in a "crossover" binding mode. This oversampling through minor groove interactions is important for specificity. The MogR binding site has structural features of A-tract DNA and is bent by approximately 52 degrees away from the dimer. The structure explains how MogR achieves binding specificity in the AT-rich genome of L. monocytogenes and explains the evolutionary conservation of A-tract sequence elements within promoter regions of MogR-regulated flagellar genes.
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MogR binds dsDNA as a dimer with the central AAAA tetranucleotide contacting both protomers.
“MogR binds to dsDNA as a dimer with the central AAAA tetranucleotide contacting both protomers.”
From Structural studies of SALL family protein zinc finger cluster domains in complex with DNA reveal preferential binding to an AATA tetranucleotide motif (2022) · cites this paper as [24]
The Results section, “Structure of MogR bound to its DNA target site,” describes two MogR molecules bound to a DNA duplex, with both molecules contributing contacts to each half-site. But it identifies the central A:T base pair as a spacer that does not directly contribute to sequence specificity; the AAAA tract is at a flank of the reported binding motif, not its center. (LLM, conf=0.90)
Experimental — accuracy not yet measuredMogR protomer B makes base-specific interactions with A6′, A5′, T4, T3 and T4 via Asn118B, Ser114B, Gln117B, Val94B, and Tyr121B.
“Asn118B of protomer B forms one hydrogen bond with A6′; Ser114B and Gln117B form water-mediated hydrogen bonds with A5′ and T4, respectively; Val94B and Tyr121B make hydrophobic interactions with T3 and T4 (24).”
From Structural studies of SALL family protein zinc finger cluster domains in complex with DNA reveal preferential binding to an AATA tetranucleotide motif (2022) · cites this paper as [24]
The Results section on major-groove contacts reports base contacts by Asn118, Ser114, Gln117, and Tyr121, and the structure section says the two MogR domains have identical protein–DNA interactions. But the copy lists different nucleotide positions, does not identify a Val94–T3 contact, and mentions water-mediated contacts without assigning the claimed pairs. Page numbers are unavailable in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredArg140 of MogR protomer A inserts into the narrow minor groove of the AAAA tetranucleotide by forming two hydrogen bonds with the T6-A6′ base pair.
“Arg140 of protomer A (Arg140A) inserts into the narrow minor groove of AAAA tetranucleotide by forming two hydrogen bonds with the T6-A6′ base pair.”
From Structural studies of SALL family protein zinc finger cluster domains in complex with DNA reveal preferential binding to an AATA tetranucleotide motif (2022) · cites this paper as [24]
The Results section on loop L3 reports two hydrogen bonds from Arg140 to adenine 11 and its paired thymine 11′. The Discussion section on A-tracts says Arg140 inserts where the minor groove is very narrow. Our copy does not identify those contacts as being with the T6–A6′ base pair, so the claim’s specific base-pair assignment is not supported. (LLM, conf=0.84)
Experimental — accuracy not yet measuredMogR specifically recognizes AT-rich DNAs.
“It has been reported that transcriptional repressor MogR specifically recognizes AT-rich DNAs (24), which prompts us to compare it with the SALL4ZFC4 complex.”
From Structural studies of SALL family protein zinc finger cluster domains in complex with DNA reveal preferential binding to an AATA tetranucleotide motif (2022) · cites this paper as [24]
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Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works
Self-citation[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works
<i>Coot</i> : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5
Hayashi, F., Smith, K. D., Ozinsky, A., Hawn, T. R., Yi, E. C., Goodlett, D. R., Eng, J. K., Akira, S., Underhill, D. M., & Aderem, A. A. (2001) · Nature · doi:10.1038/35074106 · Cited by 3,605 · see citing works
Classical Electrostatics in Biology and Chemistry
Honig, B. H., & Nicholls, A. O. (1995) · Science · doi:10.1126/science.7761829 · Cited by 2,883 · see citing works
Automated protein model building combined with iterative structure refinement.
Perrakis, A., Morris, R. J., & Lamzin, V. S. (1999) · Nature Structural Biology · doi:10.1038/8263 · Cited by 2,423 · see citing works
Lu, X. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg680 · Cited by 1,669 · see citing works
Gouet, P. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg556 · Cited by 1,505 · see citing works
Holm, L., & Sander, C. (1996) · Science · doi:10.1126/science.273.5275.595 · Cited by 1,504 · see citing works
Atomic Structures of the Human Immunophilin FKBP-12 Complexes with FK506 and Rapamycin
Duyne, G. D. V., Standaert, R. F., Karplus, P. A., Schreiber, S. L., & Clardy, J. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1012 · Cited by 1,190 · see citing works
Kissinger, C. R., Liu, B., Martı́n-Blanco, E., Kornberg, T. B., & Pabo, C. O. (1990) · Cell · doi:10.1016/0092-8674(90)90453-l · Cited by 986 · see citing works
Crystal structure of trp represser/operator complex at atomic resolution
Otwinowski, Z., Schevitz, R. W., Zhang, R.-G., Lawson, C. L., Joachimiak, A., Marmorstein, R. Q., Luisi, B. F., & Sigler, P. B. (1988) · Nature · doi:10.1038/335321a0 · Cited by 908 · see citing works
HKL2MAP: a graphical user interface for macromolecular phasing withSHELXprograms
Pape, T., & Schneider, T. R. (2004) · Journal of Applied Crystallography · doi:10.1107/s0021889804018047 · Cited by 743 · see citing works
Evasion of Toll-like receptor 5 by flagellated bacteria
Andersen‐Nissen, E., Smith, K. D., Strobe, K. L., Barrett, S. L. R., Cookson, B. T., Logan, S. M., & Aderem, A. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502040102 · Cited by 657 · see citing works
(2008) · Springer eBooks · doi:10.1007/978-1-4020-6754-9_6709 · Cited by 575 · see citing works
Wolberger, C., Vershon, A. K., Liu, B., Johnson, A. D., & Pabo, C. O. (1991) · Cell · doi:10.1016/0092-8674(91)90526-5 · Cited by 524 · see citing works
Bacterial flagellins: mediators of pathogenicity and host immune responses in mucosa
Ramos, H. C., Rumbo, M., & Sirard, J. (2004) · Trends in Microbiology · doi:10.1016/j.tim.2004.09.002 · Cited by 485 · see citing works
Role of bacterial cell surface structures in Escherichia coli biofilm formation
Houdt, R. V., & Michiels, C. W. (2005) · Research in Microbiology · doi:10.1016/j.resmic.2005.02.005 · Cited by 445 · see citing works
Structure of the represser–operator complex of bacteriophage 434
Anderson, J. E., Ptashne, M., & Harrison, S. C. (1987) · Nature · doi:10.1038/326846a0 · Cited by 366 · see citing works
Functional Specificity of a Hox Protein Mediated by the Recognition of Minor Groove Structure
Joshi, R., Passner, J. M., Rohs, R., Jain, R., Sosinsky, A., Crickmore, M. A., Jacob, V., Aggarwal, A. K., Honig, B. H., & Mann, R. S. (2007) · Cell · doi:10.1016/j.cell.2007.09.024 · Cited by 338 · see citing works
Involvement of Toll-like receptor 5 in the recognition of flagellated bacteria
Feuillet, V., Medjane, S., Mondor, I., Demaria, O., Pagni, P. P., Galán, J. E., Flavell, R. A., & Alexopoulou, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605200103 · Cited by 337 · see citing works
Type III flagellar protein export and flagellar assembly
Macnab, R. M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.04.005 · Cited by 312 · see citing works
Xu, H. E., Rould, M. A., Xu, W., Epstein, J. A., Maas, R. L., & Pabo, C. O. (1999) · Genes & Development · doi:10.1101/gad.13.10.1263 · Cited by 311 · see citing works
Gründling, A., Burrack, L. S., Bouwer, H. G. A., & Higgins, D. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404924101 · Cited by 240 · see citing works
Self-citationNUCPLOT: a program to generate schematic diagrams of protein-nucleic acid interactions
Luscombe, N. M. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4940 · Cited by 239 · see citing works
Man, T. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.12.2471 · Cited by 191 · see citing works
Crystal structure of ATF‐2/c‐Jun and IRF‐3 bound to the interferon‐β enhancer
Panne, D., Maniatis, T., & Harrison, S. (2004) · EMBO Journal · doi:10.1038/sj.emboj.7600453 · Cited by 182 · see citing works
Self-citationDNA A-tract bending in three dimensions: Solving the dA 4 T 4 vs. dT 4 A 4 conundrum
Štefl, R., Wu, H., Ravindranathan, S., Sklenář, V., & Feigon, J. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308143100 · Cited by 147 · see citing works
A-tract bending: insights into experimental structures by computational models
Strahs, D., & Tamar Schlick, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3863 · Cited by 140 · see citing works
DNA bending by an adenine–thymine tract and its role in gene regulation
Hizver, J., Rozenberg, H., Frolow, F., Rabinovich, D., & Shakked, Z. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151247298 · Cited by 138 · see citing works
A unified model for the origin of DNA sequence‐directed curvature
Hud, N. V., & Plavec, J. (2003) · Biopolymers · doi:10.1002/bip.10364 · Cited by 130 · see citing works
Shen, A., & Higgins, D. E. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020030 · Cited by 124 · see citing works
Self-citationCrystal structure of the λ repressor and a model for pairwise cooperative operator binding
Stayrook, S. E., Jaru-Ampornpan, P., Ni, J., Hochschild, A., & Lewis, M. (2008) · Nature · doi:10.1038/nature06831 · Cited by 103 · see citing works
DNA bending by adenine-thymine tracts
Crothers, D. M., & Shakked, Z. (1999) · doi:10.1093/oso/9780198500384.003.0014 · Cited by 34 · see citing works
Three-dimensional intricacies in protein-DNA recognition and transcriptional control
Harrison, S. C. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1207-1118 · Cited by 4 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- Pape T Schneider TR 2004 HKL2MAP: a graphical user interface for phasing with SHELX programs Journal of Applied Crystallography 37 843 844
- Stefl R Wu H Ravindranathan S Sklenar V Feigon J 2004 DNA A-tract bending in three dimensions: solving the dA4T4 vs. dT4A4 conundrum Proc Natl Acad Sci U S A 101 1177 1182 14739342 PMC337026
Cited by
Sorted by citations
The role of DNA shape in protein–DNA recognition
Rohs, R., West, S. M., Sosinsky, A., Liu, P., Mann, R. S., & Honig, B. (2009) · Nature · doi:10.1038/nature08473 · Cited by 1,096 · see citing works
Origins of Specificity in Protein-DNA Recognition
Rohs, R., Jin, X., West, S. M., Joshi, R., Honig, B. H., & Mann, R. S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-091030 · Cited by 902 · see citing works
Kamp, H. D., & Higgins, D. E. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002153 · Cited by 112 · see citing works
Self-citationBacillus cereus cytotoxins Hbl, Nhe and CytK are secreted via the Sec translocation pathway
Fagerlund, A., Lindbäck, T., & Granum, P. E. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-304 · Cited by 91 · see citing works
Chiu, T.-P., Rao, S., Mann, R. S., Honig, B. H., & Rohs, R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx915 · Cited by 80 · see citing works
Cheng, C., Dong, Z., Han, X., Wang, H., Jiang, L., Sun, J., Yang, Y., Ma, T., Shao, C., Wang, X., et al. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00287 · Cited by 72 · see citing works
Molecular basis of CENP-C association with the CENP-A nucleosome at yeast centromeresPreprint
Xiao, H., Wang, F., Wiśniewski, J., Shaytan, A. К., Ghirlando, R., FitzGerald, P. C., Huang, Y., Wei, D., Li, S., Landsman, D., et al. (2017) · Genes & Development · doi:10.1101/gad.304782.117 · Cited by 57 · see citing works
Kamp, H. D., & Higgins, D. E. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06874.x · Cited by 52 · see citing works
Self-citationPryor, E. E., Waligora, E. A., Xu, B., Dellos-Nolan, S., Wozniak, D. J., & Hollis, T. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002648 · Cited by 47 · see citing works
Agriesti, F., Roncarati, D., Musiani, F., Campo, C. D., Iurlaro, M., Sparla, F., Ciurli, S., Danielli, A., & Scarlato, V. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1258 · Cited by 36 · see citing works
The structural basis for recognition of base J containing DNA by a novel DNA binding domain in JBP1
Heidebrecht, T., Christodoulou, E., Chalmers, M. J., Jan, S. Z., ter Riet, B., Grover, R. K., Joosten, R. P., Littler, D. R., van Luenen, H. G. A. M., Griffin, P. R., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr125 · Cited by 36 · see citing works
Tian, W., Yan, P., Xu, N., Chakravorty, A., Liefke, R., Xi, Q., & Wang, Z. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz294 · Cited by 31 · see citing works
Azad, R. N., Zafiropoulos, D., Ober, D., Jiang, Y., Chiu, T.-P., Sagendorf, J. M., Rohs, R., & Tullius, T. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky033 · Cited by 29 · see citing works
Yang, S., Gao, Z., Li, T., Yang, M., Zhang, T., Dong, Y., & He, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.468694 · Cited by 25 · see citing works
Cho, S. Y., Na, H.-W., Oh, H. B., Kwak, Y. M., Song, W. S., Park, S. C., Jeon, W.-J., Cho, H., Oh, B., Park, J., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac815 · Cited by 22 · see citing works
Ru, W., Koga, T., Wang, X., Guo, Q., Gearhart, M. D., Zhao, S., Murphy, M., Kawakami, H., Corcoran, D., Zhang, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102607 · Cited by 20 · see citing works
“Given that SALL4ZFC1 binds to AT-rich DNAs weaker than SALL4ZFC4, it might be insufficient to maintain the occupancy of SALL4 after the deletion of ZFC4, consistent with previous report that mutation or deletion of SALL4ZFC4 impairs the targeting of SALL4 at genome sites (14).”
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Feng, L., Chen, Z., Wang, Z., Hu, Y., & Chen, S. (2016) · Microbiology · doi:10.1099/mic.0.000257 · Cited by 20 · see citing works
Smith, V., Josefsen, M., Lindbäck, T., Hegna, I. K., Finke, S., Tourasse, N. J., Nielsen‐LeRoux, C., Økstad, O. A., & Fagerlund, A. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.610650 · Cited by 17 · see citing works
A DNA minor groove electronegative potential genome map based on photo-chemical probing
Lindemose, S., Nielsen, P. E., Hansen, M., & Møllegaard, N. E. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr204 · Cited by 14 · see citing works
Käppel, S., Eggeling, R., Rümpler, F., Groth, M., Melzer, R., & Theißen, G. (2021) · Plant Molecular Biology · doi:10.1007/s11103-020-01108-6 · Cited by 14 · see citing works
Zhang, T., Bae, D., & Wang, C. (2016) · Applied and Environmental Microbiology · doi:10.1128/aem.00719-16 · Cited by 13 · see citing works
Huber, E. M., Hortschansky, P., Scheven, M. T., Misslinger, M., Haas, H., Brakhage, A. A., & Groll, M. (2022) · Structure · doi:10.1016/j.str.2022.04.001 · Cited by 12 · see citing works
Liu, C., Xun, M., Jia, B., Qian, R., Gao, S., Liu, L., Qi, Y., Yin, Z., Hu, G., & Wang, J. (2025) · Virulence · doi:10.1080/21505594.2025.2543144 · Cited by 8 · see citing works
Re-visiting protein-centric two-tier classification of existing DNA-protein complexes
Malhotra, S., & Sowdhamini, R. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-165 · Cited by 8 · see citing works
Transcription Regulation of Flagellins: A Structural Perspective
Sheenu, & Jain, D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00791 · Cited by 7 · see citing works
Kotzamanidis, C., Malousi, A., Dushku, E., Dobly, A., Keersmaecker, S. C. J. D., Roosens, N. H. C., Karathodorou, A., Staikou, A. E., Zdragas, A. G., & Yiangou, M. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.03.028 · Cited by 7 · see citing works
Adamopoulos, A., Heidebrecht, T., Roosendaal, J., Touw, W. G., Phan, I. Q., Beijnen, J. H., & Anastassis Perrakis, A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007393 · Cited by 6 · see citing works
Oh, H. B., Lee, S., & Yoon, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-14459-5 · Cited by 4 · see citing works
Some novel features of strong promoters discovered in Cytophaga hutchinsonii
Fan, G., Song, W., Guan, Z., Zhang, W., & Lu, X. (2022) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-022-11869-3 · Cited by 3 · see citing works
Patient satisfaction with hospital services: development and testing of a measuring instrument.
Mokhtar, S. A., Guirguis, W. W., al-Torkey, M. M., & Khalaf, A. A. (1991) · PubMed · Cited by 1 · see citing works
Scalable and interpretable secretion system annotation with SismisPreprint
Larralde, M. F., Albrecht, F., Blom, J., Henriksson, J., & Carroll, L. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.09.675188 · Cited by 1 · see citing works
Characterization of an unusual phage repressor encoded by mycobacteriophage BPs
Villanueva, V. M. (2015)
MogR regulates flagellar synthesis, cell motility and biofilm formation in the Bacillus cereus group
Josefsen, M. (2012) · NORA - Norwegian Open Research Archives
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Ru, W., Koga, T., Wang, X., Guo, Q., Gearhart, M., Zhao, S., Murphy, M. W., Kawakami, H., Corcoran, D., Zhang, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.13.496009
- Authors
- Shen, A., Higgins, D. E., & Panne, D.
- Affiliations
- Harvard University (US)
- European Molecular Biology Laboratory (FR)
- Corresponding author
- Higgins, Darren E.
- Panne, Daniel
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 17
- Issue
- 5
- Pages
- 769-777
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC2712671
- OpenAlex
- W2170567325
- Cited by
- 35
- References
- 38
- Citations by year
- 2025: 3 · 2022: 7 · 2021: 1 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 1 · 2013: 2 · 2012: 4
- FWCI
- 2.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Structure (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Allergy and Infectious Diseases (AI-53669, R01AI053669)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- transcriptional repressor, AT-rich DNA binding, Listeria monocytogenes, flagellar gene expression, DNA bending, helix-turn-helix motif, minor groove recognition, protein-DNA complex crystal structure, DNA binding specificity, intracellular pathogens
- MeSH terms
- Bacterial Proteins, Base Sequence, Binding Sites, DNA, DNA, Bacterial, Flagellin, Listeria monocytogenes, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Promoter Regions, Genetic, Protein Conformation, Repressor Proteins, Helix-Turn-Helix Motifs, AT Rich Sequence
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