The Quiet Revolution: A New Synthesis of Biological Knowledge

Dyer, K. F.

doi:10.1080/00219266.1971.9653663

Cited by 34 publications

(31 citation statements)

References 33 publications

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“…Lower panel: (left) the average α-amino acid composition in all proteins, with green indicating the prebiotic amino acids, Red bars indicate biotic amino acids (King and Jukes, 1969; Dyer, 1971); (right) the average α-amino acid composition in halophile proteins, with green indicating the prebiotic amino acids, Red bars indicate biotic amino acids (Fukuchi et al, 2003). …”

mentioning

confidence: 99%

Prebiotic protein design supports a halophile origin of foldable proteins

Longo

Blaber

2014

Front. Microbiol.

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confidence: 99%

Prebiotic protein design supports a halophile origin of foldable proteins

Longo

Blaber

2014

Front. Microbiol.

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“…It has been previously reported that overall amino acid composition of the protein have an important role in evolution (King and Jukes 1969). Further, the quality and structure of protein is also found to be dependent upon amino acid composition (Dyer 1971). Osmotin protein is reported to be rich in cysteine residues scattered all over the sequence.…”

Section: Resultsmentioning

confidence: 99%

Cloning and characterization of Osmotin (OsmSt) alleles from potato cultivar ‘Kufri Chipsona 1’

Kaur

Kumar

2020

Preprint

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The present study was focussed to clone and sequence characterise alleles of osmotin from cDNA of Solanum tuberosum L. cultivar 'Kufri Chipsona 1'. The genes vary in sizes as well as were found to have eleven point mutations throughout the coding sequence. One deletion of 7 bp was also found in smaller form of the gene having molecular weight of 19.91 KDa.Osmotin gene is known to impart resistance/tolerance to various fungal diseases in addition to its role as an osmoprotectant, thus, cloned osmotin alleles from important processing grade potato cultivar could become potential candidates for molecular breeding of potato.

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“…). A comparison of 3xY and 3xW mini‐core mutant stability with 3xF shows that the Y mutation is more stable, while W is essentially isoenergetic with F. Thus, with incorporation of just a single aromatic amino acid (that is, at 0.8% of positions–an ∼11‐fold reduction in the typical percentage of aromatic residues found in extant, mesophile proteins), involving either F, Y, or W, the requirement of high salt concentrations for essentially complete folding is eliminated.…”

Section: Resultsmentioning

confidence: 99%

A single aromatic core mutation converts a designed “primitive” protein from halophile to mesophile folding

et al. 2014

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Abstract:The halophile environment has a number of compelling aspects with regard to the origin of structured polypeptides (i.e., proteogenesis) and, instead of a curious niche that living systems adapted into, the halophile environment is emerging as a candidate "cradle" for proteogenesis. In this viewpoint, a subsequent halophile-to-mesophile transition was a key step in early evolution. Several lines of evidence indicate that aromatic amino acids were a late addition to the codon table and not part of the original "prebiotic" set comprising the earliest polypeptides. We test the hypothesis that the availability of aromatic amino acids could facilitate a halophile-to-mesophile transition by hydrophobic core-packing enhancement. The effects of aromatic amino acid substitutions were evaluated in the core of a "primitive" designed protein enriched for the 10 prebiotic amino acids (A,D,E,G,I,L,P,S,T,V)-having an exclusively prebiotic core and requiring halophilic conditions for folding. The results indicate that a single aromatic amino acid substitution is capable of eliminating the requirement of halophile conditions for folding of a "primitive" polypeptide. Thus, the availability of aromatic amino acids could have facilitated a critical halophile-tomesophile protein folding adaptation-identifying a selective advantage for the incorporation of aromatic amino acids into the codon table.

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The Quiet Revolution: A New Synthesis of Biological Knowledge

Cited by 34 publications

References 33 publications

Prebiotic protein design supports a halophile origin of foldable proteins

Prebiotic protein design supports a halophile origin of foldable proteins

Cloning and characterization of Osmotin (OsmSt) alleles from potato cultivar ‘Kufri Chipsona 1’

A single aromatic core mutation converts a designed “primitive” protein from halophile to mesophile folding

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