Living lungfish (Osteichthyes: Dipnoi) are known to have a very large cell size and unusually large quantitites of DNA per cell (up to 40 times the mammalian content). The pattern of evolution of cell size in fossil Dipnoi has been examined in order to see what light i t might possibly shed on the q
Evolutionary changes in the information content of polypeptides
β Scribed by Koichiro Matsuno
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 744 KB
- Volume
- 105
- Category
- Article
- ISSN
- 0022-5193
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β¦ Synopsis
Thermal proteins arising from the self-sequencing of amino acids satisfy the necessary conditions required for them to become a candidate of the evolutionary precursors of contemporary proteins. The source matrix of information or, equivalently, the statistical ensemble of polypeptides, in reference to which the information content of each amino acid residue can be defined and determined, changes with time endogenously through the production of and the change in the mechanism of production of polypeptides. The change proceeds in the direction along which the order of autocatalysis, the number of autocatalytic polymers needed for synthesizing one such polymer, increases. The underlying dynamics is material flow equilibration working in any material aggregate open to material flow, saying that any open system changes its interaction with the exterior endogenously and successively so as to maintain the continuity of material flow there. The self-sequencing and the autocatalytic polymerization of amino acids are the forms of producing polypeptides. The change in the mechanism of producing polypeptides results from the incorporation of polynucleotides into the polypeptide synthesis. The earlier polymeric information translation proceeds from polypeptide to polynucleotide. The direction of translation is.reversed at a later stage of evolution. All these evolutionary events are consistent with viewing thermal proteins produced by self-sequencing of amino acids as an evolutionary precursor of contemporary proteins.
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