Abstract
The crystal structure of p24, the single-stranded DNA (ssDNA) binding subunit of the plant defense transcription factor PBF-2, has been determined to 2.3 Å resolution. p24 is representative of a novel family of ubiquitous plant-specific proteins that we refer to as the Whirly family because of their quaternary structure. PBF-2 is composed of four p24 molecules that interact through a helix-loop-helix motif. This interaction produces a central pore, with β-strands radiating outwards, resulting in a whirligig appearance to the quaternary structure. The noncrystallographic C4 symmetry arrangement of p24 subunits is novel for ssDNA binding proteins and may explain the binding specificity of PBF-2. This structural arrangement also supports the role of PBF-2 in binding melted promoter regions to modulate gene expression.
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References
Brivanlou, A.H. & Darnell, J.E., Jr Science 295, 813–818 (2002).
Roeder, R.G. Trends Biochem. Sci. 21, 327–335 (1996).
Kornberg, R.D. Trends Cell. Biol. 9, M46–49 (1999).
Woychik, N.A. & Hampsey, M. Cell 108, 453–463 (2002).
Nikolov, D.B. et al. Nature 360, 40–46 (1992).
Rushton, P. & Somssich, E. Curr. Opin. Plant Biol. 1, 311–315 (1998).
Maleck, K. et al. Nature Genet. 26, 403–410 (2000).
Matton, D.P. & Brisson, N. Mol. Plant Microbe Interact. 2, 325–331 (1989).
Matton, D.P., Prescott, G., Bertrand, C., Camirand, A. & Brisson, N. Plant Mol. Biol. 22, 279–291 (1993).
Després, C., Subramaniam, R., Matton, D.P. & Brisson, N. Plant Cell 7, 589–598 (1995).
Desveaux, D, Després, C., Joyeux, A., Subramaniam, R. & Brisson, N. Plant Cell 12, 1477–1489 (2000).
Hendrickson, W. & Ogata, C. Methods Enzymol. 276, 494–523 (1997).
Desveaux, D., Allard, J., Brisson, N. & Sygusch, J. Acta Crystallogr. D 58, 296–298 (2002).
Raghunathan, S., Ricard, C.S., Lohman, T.M. & Waksman, G. Proc. Natl. Acad. Sci. USA 94, 6652–6657 (1997).
Yang, C., Curth, U., Urbanke, C. & Kang, C. Nature Struct. Biol. 4, 153–157 (1997).
Rost, B. & Sander, C. J. Mol. Biol. 232, 584–599 (1993).
Rost, B. & Sander, C. Proteins 19, 55–72 (1994).
Holm, L. & Sander, C. J. Mol. Biol. 233, 123–138 (1993).
Werten, S., Wechselberger, R., Boelens, R., van der Vliet, P.C. & Kaptein, R. J. Biol. Chem. 274, 3693–3699 (1999).
Brandsen, J. et al. Nature Struct. Biol. 4, 900–903 (1997).
Bates, A.D. & Maxwell, A. In DNA Topology (eds Rickwood, D. & Male, D.) 88–95 (IRL Press, Oxford; 1993).
Duncan, R. et al. Genes Dev. 8, 465–480 (1994).
Kowalski, D., Natale, D.A. & Eddy, M.J. Proc. Natl. Acad. Sci. USA 85, 9464–9468 (1988).
Gerber, H.-P. et al. Science 263, 808–811 (1994).
Kahn, J.D., Yun, E. & Crothers, D.M. Nature 368, 163–166 (1994).
Travers, A. & Muskhelishvili, G. J. Mol. Biol. 279, 1027–1043 (1998).
Suck, D. Nature Struct. Biol. 4, 161–165 (1997).
Bochkarev, A., Pfuetzner, R.A., Edwards, A.M. & Frappier, L. Nature 385, 176–181 (1997).
Ruff, M. et al. Science 252, 1682–1689 (1991).
Klinge, C.M. Nucleic Acids Res. 29, 2905–2919 (2001).
Terwilliger, T.C. & Berendzen, J. Acta Crystallogr. D 55, 849–861 (1999).
Brünger, A.T. et al. Acta Crystallogr. D 54, 905–921 (1998).
Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Acta Crystallogr. A 47, 110–119 (1991).
Diamond, R. Protein Sci. 1, 1279–1287 (1992).
Constable, C.P. & Brisson, N. Planta 188, 289–295 (1992).
Thompson, J.D., Higgins, D.G. & Gibson, T.J. Nucleic Acids Res. 22, 4673–4680 (1994).
Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. J. Appl. Crystallogr. 26, 283–291 (1993).
Luzzati, P.V. Acta Crystallogr. 5, 802–810 (1952).
Acknowledgements
The assistance of T.-S. Yoon in data collection and reduction is gratefully acknowledged. Research carried out at the National Synchrotron Light Source, Brookhaven National Laboratory, was supported by the U.S. Department of Energy, Division of Materials Sciences and Division of Chemical Sciences. Assistance by X8-C and X25 beamline personnel is gratefully appreciated. This research was supported by a fellowship from the Natural Sciences and Engineering Research Council of Canada (NSERC) to D.D. and research grants from the Canadian Institutes of Health Research to J.S., from NSERC to both N.B. and J.S. and the Fonds pour la Formation de Chercheurs et l'Aide à la Recherche, Québec to N.B.
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Desveaux, D., Allard, J., Brisson, N. et al. A new family of plant transcription factors displays a novel ssDNA-binding surface. Nat Struct Mol Biol 9, 512–517 (2002). https://doi.org/10.1038/nsb814
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DOI: https://doi.org/10.1038/nsb814
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