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Proteins, the chaperone function and heredity

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Abstract

In this paper I use a case study—the discovery of the chaperon function exerted by proteins in the various steps of the hereditary process—to re-discuss the question whether the nucleic acids are the sole repositories of relevant information as assumed in the information theory of heredity. The evidence I here present of a crucial role for molecular chaperones in the folding of nascent proteins, as well as in DNA duplication, RNA folding and gene control, suggests that the family of proteins acting as molecular chaperones provides information that is complementary to that stored in the nucleic acids, and equally important. A re-evaluation of the role of proteins in the hereditary process is in order away from the gene-centric approach of the information theory of heredity, to which neo-Darwinian evolutionists adhere.

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Notes

  1. The information theory of heredity stemmed from the discovery of the double helix structure of DNA (Watson and Crick 1953a), which provided an explanation for earlier findings (Avery et al. Avery et al. 1944) pointing to DNA being the repository of biological specificity: “It has not escaped our notice that the specific pairing we have postulated immediately suggests a possible copying mechanism of the genetic material” (Watson and Crick 1953b, p. 737).

  2. The term ‘neo-Darwinian’ was coined by Romanes (1905) to denote those among Darwin’s followers whose thinking was, in his view, closer to Wallace’s and Weismann’s than to Darwin’s own one.

  3. Such tension, and the refusal to face it, have brought about an unhealthy state of affairs, one that allowed “Mechanistic developmental biology and evolutionary genetics [to] largely proceed independently from each other throughout most of the twentieth century” (Landry and Rifkin 2010, p. 434).

  4. It has recently emerged that the percentage of the human genome ‘responsible’ for protein synthesis is less than 1.5 percent (Baltimore 2001).

  5. For an excellent first-hand account of the gathering of early evidence in favour of the information theory of heredity, see Kornberg (1960).

  6. A recent assessment based on sophisticated computational techniques, in fact, revealed the match between data on actual conformations and tertiary structures predicted from amino acid sequences to be rather modest (Ramsey 2007).

  7. Conversely, it was shown that enzymes involved in the same process, for instance in redox reactions, often do not show primary structure homology (Jörnvall 1973).

  8. The main difference between in vitro and in vivo experiments is that protein concentration in the former is usually very low, and this reduces the number of off-pathways leading to non-functional proteins.

  9. In which case, thermodynamic and kinetic control coincide.

  10. Regrettably, even recent textbooks fail to give adequate recognition of the role of molecular chaperones in protein folding: “Proteins fold up into…conformations largely determined by their primary structure…In the 1950s Cristian Anfinsen…and his colleagues demonstrated that tertiary structure is a consequence of primary structure” (Sheehan 2009, pp. 199–200).

  11. The human genome has been found to contain only twice as many structural genes as a worm or fly; the much larger number of proteins it generates is the result of much more extensive protein-induced alternative splicing (Lander et al. 2001).

  12. Histones are the principal protein components of chromatin, the other component being DNA; the two are present in the ratio of 2:1.

  13. The discovery of the role of ATP synthase (Boyer et al. 1973) earned the scientists behind it the Nobel Prize for chemistry in 1997.

  14. The quip relates to Dobzhanski claim that “nothing in biology makes sense except in the light of evolution” (1973, p. 125).

  15. Recall that the view in question was based on extrapolating to metabolizing cells data collected from growing cells and, consequently, analysing mutation rates as if these were constant through the various stages of cellular development (see Hall 1988 for discussion).

  16. Because of their assistance in ensuring the stability of genotypes, stress proteins, histones, and other proteins acting as molecular chaperones have been attributed to highly conserved families believed to have been present in the very first living organisms (Morimoto et al. 1990; Macario and Conway de Macario 1999).

  17. The first insight into the phenomenon of plasticity may be traced back to Schmalhausen’s (1949) identifying a ‘reserve of hereditary variability’ in each one species that could be used for adaptive purposes when environmental conditions changed.

  18. Discussion of epigenetics was revived in the late 1980 s, when phenotypic change attributable to modifications of extranucleic, epinucleic, or nucleic type (the latter relating to loss of non-essential DNA/RNA) appeared to be hereditable for multicellular organisms at degrees that vary widely from species to species, while decreasing sharply in higher animals (Buss 1987; Jablonka et al. 1992). Since then, the inheritance of acquired characters appeared to be, at least for some organisms, “a well-established phenomenon” (Landman 1991, p. 16).

  19. For an overview of the Conference, organised in November 2001 at the University of Ghent, see Van Speybroeck (2002).

  20. “Function cannot be understood without information about shape and form” (Lewontin 1998, pp. 113–114).

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Mosini, V. Proteins, the chaperone function and heredity. Biol Philos 28, 53–74 (2013). https://doi.org/10.1007/s10539-012-9332-4

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