The evolution of plants and animals under domestication: the contribution of studies at the molecular level
- 27 July 1976
- journal article
- research article
- Published by The Royal Society in Philosophical Transactions of the Royal Society of London. B, Biological Sciences
- Vol. 275 (936) , 99-116
- https://doi.org/10.1098/rstb.1976.0073
Abstract
Protein molecules are essential catalysts in life processes and also form much of the substance of living material. Their three dimensional structures determine their biological function. Their biosynthesis is primarily determined by arrays of nucleic acid macromolecules (DNA and RNA), and the amino acid sequences that constitute their long spatially organized peptide-chain molecules reflect at one remove this DNA coding system, and thus record a step-by-step history of some of the viable genetic events (natural or man-controlled) that have created the organism and the breed. Amino acid sequences can be used to trace the progress of controlled breeding in two ways: by extrapolation back from living breeds, and by analysis of ancient protein material. O f the latter, bone or tendon or skin collagens and hair keratins are the most perfectly preserved as molecular structures through 20000 years and indeed much longer. Amino acid sequences are expensive to determine (collagen has 1052 amino acid residues), and the potential of this palaeobiological information has been as yet little exploited. The first approach has, however, been more explored, in both plants and animals. Several protein systems must be studied in conjunction to reveal the phylogenetic threads in any one breed. As the three dimensional quaternary structure of protein molecules becomes more appreciated in relation to biological function, and as new techniques and procedures are developed, amino acid sequence data can become more informative in our ultimate understanding of early selective breeding.This publication has 11 references indexed in Scilit:
- Slow evolutionary loss of the potential for interspecific hybridization in birds: a manifestation of slow regulatory evolution.Proceedings of the National Academy of Sciences, 1975
- Axially projected collagen structuresProceedings of the Royal Society of London. B. Biological Sciences, 1974
- Analysis of the primary structure of collagen for the origins of molecular packingJournal of Molecular Biology, 1973
- SEED PROTEIN PROFILES AND THE ORIGIN OF THE HEXAPLOID WHEATSAmerican Journal of Botany, 1972
- Protein Electrophoretic Profiles and the Origin of the B Genome of WheatProceedings of the National Academy of Sciences, 1972
- The comparative biochemistry of collagen: The structure of rabbit skin collagen and its relevance to immunochemical studies of collagenArchives of Biochemistry and Biophysics, 1970
- Transferrin and albumin loci in chickens Gallus gallus L.Comparative Biochemistry and Physiology, 1968
- Molecular genetics of avian proteins—VIII. Egg white proteins of the migratory quail, coturnix coturnix—New concepts of “hybrid vigour”Comparative Biochemistry and Physiology, 1967
- A comparison of amino acid sequences in the β-chains of adult bovine hemoglobins A and BArchives of Biochemistry and Biophysics, 1967
- Hemoglobins in Sheep: Multiple Differences in Amino Acid Sequences of Three Beta-Chains and Possible OriginsScience, 1966