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Brian K. Davis

Publications and source records attributed to Brian K. Davis.

5 recordsLinked to original sources

The Biosynthetic Order of Amino Acid Addition to the Genetic Code

The previously formulated model for the evolution of the genetic code was shown to clarify why base triplets of some precursor amino acids differ by a single base from product amino acid codons, while others show less homology. First, the model indicated that the direction of code evolution changed on expansion from the N-fixers code (stage 2). Growth of the code from 16 codons in the NAN column (N, any standard nucleotide) proceeded by assignment of codons in the GNN, ANN, CNN and UNN rows. Expansion phase (stage 4 to 7) precursor/product pairs that spanned this shift included aspartate/threonine, aspartate/methionine and glutamate/proline. Both 5' and mid-base differ in the codons of each of these pairs. Second, post-expansion additions (stage 9 to 14) required codon reassignment, eliminating initial correlations. Codons for the post-expansion pair, aspartate (glutamate)/arginine, also differ at both 5' and mid-base sites. Third, the distribution of core structure groups among acceptors indicated that variant tRNA specific for a sibling, rather than precursor, commonly participated as cofactors in early amino acid synthesis. Sibling pairs, rather than precursor/product pairs, then exhibit codon correlations. On removing these sources of variation, highly significant correlations emerged between codons assigned to biosynthetically related amino acids.

physics.bio-ph

Residue profile in predivergence sequences as a guide to the origin of DNA replication

DNA dependent RNA polymerase core subunits abb' conserved residues at frequencies most closely matched with codons at stage 10.4-11.1 in code evolution. An excess of acidic residues (stage 2 additions) lowered this estimate, but not by more than 2.3 stages. With 1 tryptophan (stage 14 addition) in 529 conserved residues, abb' significantly under-represented this amino acid, consistent with a cut-off in its residue profile before completion of the genetic code. Residue profiles in FEN-1 homologs and DNA topoisomerase I-5' placed their origin at stage 11-13. Prokaryote septation protein, FtsZ, arose earlier, between stage 8-11. Proteolipid in an ATP-driven proton pump served as a marker for cell membrane formation. It indicated this event took place near stage 7. Cell division, DNA replication and transcription were inferred to have originated in a protocell antecedent of the last common ancestor. Late-forming residue profiles characterized RNA dependent RNA replicase, DNA polymerase, reverse transcriptase and ribonucleotide reductase. This suggests some early processes, including RNA replication and deoxynucleotide synthesis, once depended on catalysts not found in extant residue sequences. Early formation of topoisomerase I, and enzymes that synthesize and trim RNA-DNA hybrids was viewed as evidence for a mixed duplex, with linear RNA and DNA strands, in the transition from an RNA to DNA genome.

physics.bio-ph

Darwinian Aspects of Molecular Evolution at Sublinear Propagation Rates

The symmetric distribution and all other states in the symmetry sector of the frequency trajectory increase mean fitness during competitive replication at sublinear propagation rates (parabolic time course). States in the non-symmetry sector, by contrast, produce negative time variations in mean fitness. The polymorphic steady state attained in sublinear systems is destabilised by formation of a variant with above threshold fitness. Evolution in the post-steady state interval increases threshold fitness. Contrary to the proposition that 'parabolic growth invariably results in the survival of all competing species,' only species with sufficient fitness to avoid subthreshold frequencies survive.

physics.bio-ph

Transition to the Most Probable Kinetic State in a Pre-Steady State System

A system containing a pre-steady state standard (non-autocatalytic) reaction, with multiple paths, evolves toward a kinetic state with the minimum attainable activation free energy. Displacement of the path frequency distribution in this transition was shown to minimise the affinity linked to this change in activation free energy. In damping this scalar force, a standard system is driven along a path of least action, as previously established for a system of competing autocatalytic reactions. A kinetic source of time asymmetry arises within the system, as the activation affinity moves the system toward the most probable distribution of reaction paths. As the functions of state are not changed by path displacement, a change of kinetic state cannot produce chemical work. This generalises the notion of force to a scalar quantity responsible for a displacement that does not yield work or heat. Spectrophotometric observations reported on the transition to steady state kinetics during dinitrophenyl phosphate phosphorolysis confirmed that time variations in the activation affinity are non-positive.

physics.chem-ph