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Modern and prebiotic amino acids support distinct structural profiles in proteins
The earliest proteins had to rely on amino acids available on early Earth before the biosynthetic pathways for more complex amino acids evolved. In extant proteins, a significant fraction of the ‘late’ amino acids (such as Arg, Lys, His, Cys, Trp and Tyr) belong to essential catalytic and structure-...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9213115/ https://www.ncbi.nlm.nih.gov/pubmed/35728622 http://dx.doi.org/10.1098/rsob.220040 |
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author | Tretyachenko, Vyacheslav Vymětal, Jiří Neuwirthová, Tereza Vondrášek, Jiří Fujishima, Kosuke Hlouchová, Klára |
author_facet | Tretyachenko, Vyacheslav Vymětal, Jiří Neuwirthová, Tereza Vondrášek, Jiří Fujishima, Kosuke Hlouchová, Klára |
author_sort | Tretyachenko, Vyacheslav |
collection | PubMed |
description | The earliest proteins had to rely on amino acids available on early Earth before the biosynthetic pathways for more complex amino acids evolved. In extant proteins, a significant fraction of the ‘late’ amino acids (such as Arg, Lys, His, Cys, Trp and Tyr) belong to essential catalytic and structure-stabilizing residues. How (or if) early proteins could sustain an early biosphere has been a major puzzle. Here, we analysed two combinatorial protein libraries representing proxies of the available sequence space at two different evolutionary stages. The first is composed of the entire alphabet of 20 amino acids while the second one consists of only 10 residues (ASDGLIPTEV) representing a consensus view of plausibly available amino acids through prebiotic chemistry. We show that compact conformations resistant to proteolysis are surprisingly similarly abundant in both libraries. In addition, the early alphabet proteins are inherently more soluble and refoldable, independent of the general Hsp70 chaperone activity. By contrast, chaperones significantly increase the otherwise poor solubility of the modern alphabet proteins suggesting their coevolution with the amino acid repertoire. Our work indicates that while both early and modern amino acids are predisposed to supporting protein structure, they do so with different biophysical properties and via different mechanisms. |
format | Online Article Text |
id | pubmed-9213115 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-92131152022-06-24 Modern and prebiotic amino acids support distinct structural profiles in proteins Tretyachenko, Vyacheslav Vymětal, Jiří Neuwirthová, Tereza Vondrášek, Jiří Fujishima, Kosuke Hlouchová, Klára Open Biol Research The earliest proteins had to rely on amino acids available on early Earth before the biosynthetic pathways for more complex amino acids evolved. In extant proteins, a significant fraction of the ‘late’ amino acids (such as Arg, Lys, His, Cys, Trp and Tyr) belong to essential catalytic and structure-stabilizing residues. How (or if) early proteins could sustain an early biosphere has been a major puzzle. Here, we analysed two combinatorial protein libraries representing proxies of the available sequence space at two different evolutionary stages. The first is composed of the entire alphabet of 20 amino acids while the second one consists of only 10 residues (ASDGLIPTEV) representing a consensus view of plausibly available amino acids through prebiotic chemistry. We show that compact conformations resistant to proteolysis are surprisingly similarly abundant in both libraries. In addition, the early alphabet proteins are inherently more soluble and refoldable, independent of the general Hsp70 chaperone activity. By contrast, chaperones significantly increase the otherwise poor solubility of the modern alphabet proteins suggesting their coevolution with the amino acid repertoire. Our work indicates that while both early and modern amino acids are predisposed to supporting protein structure, they do so with different biophysical properties and via different mechanisms. The Royal Society 2022-06-22 /pmc/articles/PMC9213115/ /pubmed/35728622 http://dx.doi.org/10.1098/rsob.220040 Text en © 2022 The Authors. https://creativecommons.org/licenses/by/4.0/Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Research Tretyachenko, Vyacheslav Vymětal, Jiří Neuwirthová, Tereza Vondrášek, Jiří Fujishima, Kosuke Hlouchová, Klára Modern and prebiotic amino acids support distinct structural profiles in proteins |
title | Modern and prebiotic amino acids support distinct structural profiles in proteins |
title_full | Modern and prebiotic amino acids support distinct structural profiles in proteins |
title_fullStr | Modern and prebiotic amino acids support distinct structural profiles in proteins |
title_full_unstemmed | Modern and prebiotic amino acids support distinct structural profiles in proteins |
title_short | Modern and prebiotic amino acids support distinct structural profiles in proteins |
title_sort | modern and prebiotic amino acids support distinct structural profiles in proteins |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9213115/ https://www.ncbi.nlm.nih.gov/pubmed/35728622 http://dx.doi.org/10.1098/rsob.220040 |
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