Abstract
Prions and other misfolded proteins can impart their structure and functions to normal molecules. Based upon a thorough structural assessment of RNA, prions and misfolded proteins, especially from the perspective of conformational diversity, we propose a case for co-existence of these in the pre-biotic world. Analyzing the evolution of physical aspects of biochemical structures, we put forward a case for an RNA–prion pre-biotic world, instead of, merely, the “RNA World”.
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References
Aguzzi, A.: Beyond the prion principle. Nature 459, 924–925 (2009)
Gilbert, W.: The RNA world. Nature 319, 618 (1986)
Lindahl, T.: Instability and decay of the primary structure of DNA. Nature 362(6422), 709–715 (1993)
Shorter, J., Lindquist, S.: Prions as adaptive conduits of memory and inheritance. Nat. Rev. Gen. 6, 435–450 (2005)
Uversky, V.N.: Natively unfolded proteins: a point where biology waits for physics. Prot. Sci. 11, 739–756 (2002)
Ma, B., Shatsky, M., Wolfson, H.J., Nussinov, R.: Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations. Prot. Sci. 11, 184–197 (2002)
Wright, P.E., Dyson, H.J.: Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321–331 (1999)
James, L.C., Tawfik, D.S.: Conformational diversity and protein evolution—a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28(7), 361–368 (2003)
Banerji, A.: A mathematical model to describe “context-dependence” in biology. arXiv:0902.0664v1 [q-bio.OT] (2009)
Li, J., Browning, S., Mahal, S.P., Oelschlegel, A.M., Weissmann, C.: Darwinian evolution of prions in cell culture. Science 327(5967), 869–872 (2010)
Chien, P., Weissman, J.S.: Conformational diversity in a yeast prion dictates its seeding specificity. Nature 410, 223–227 (2001)
Derreumaux, P.: Evidence that the 127–164 region of prion proteins has two equi-energetic conformations with b or a features. Biophys. J. 81, 1657–1665 (2001)
Jensen, R.A.: Enzyme recruitment in evolution of new function. Ann. Rev. Microbiol. 30, 409–425 (1976)
Prusiner, S.B.: Prions. Proc. Natl. Acad. Sci. U. S. A. 95, 13363–13383 (1998)
Chesebro, B.: BSE and prions: uncertainties about the agent. Science 279(5347), 42–43 (1998)
Rubenstein, R., Carp, R.I., Callahan, S.M.: In vitro replication of scrapie agent in a neuronal model: infection of PC12 cells. J. Gen. Virol. 65(Pt 12), 2191–2198 (1984)
Weiss, S., Proske, D., Neumann, M., Groschup, M.H., Kretzschmar, H.A., Famulok, M., Winnacker, E.L.: RNA aptamers specifically interact with the prion protein PrP. J. Virol. 71(11), 8790–8797 (1997)
Deleault, N.R., Lucassen, R.W., Supattapone, S.: RNA molecules stimulate prion protein conversion. Nature 425(6959), 717–720 (2003)
Tompa, P., Friedrich, P.: Prion proteins as memory molecules: an hypothesis. Neuroscience 86(4), 1037–1043 (1998)
Tompa, P., Tusnady, G.E., Cserzo, M., Simon, I.: Prion protein: evolution caught en route. Proc. Natl. Acad. Sci. U. S. A. 98(8), 4431–4436 (2001)
Acknowledgements
One of the authors, Anirban, acknowledges the support from COE-DBT scheme (Government of India).
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Singh, P.P., Banerji, A. Case for an RNA–prion world: a hypothesis based on conformational diversity. J Biol Phys 37, 185–188 (2011). https://doi.org/10.1007/s10867-011-9219-7
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DOI: https://doi.org/10.1007/s10867-011-9219-7