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Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability
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SYSNO ASEP 0569403 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability Tvůrce(i) Makarov, M. (CZ)
Sanchez Rocha, A. C. (CZ)
Kryštůfek, Robin (UOCHB-X) ORCID
Cherepashuk, I. (CZ)
Dzmitruk, Volha (BTO-N)
Charnavets, Tatsiana (BTO-N)
Faustino, A. M. (US)
Lebl, Michal (UOCHB-X)
Fujishima, K. (JP)
Fried, S. D. (US)
Hlouchová, Klára (UOCHB-X) ORCIDZdroj.dok. Journal of the American Chemical Society. - : American Chemical Society - ISSN 0002-7863
Roč. 145, č. 9 (2023), s. 5320-5329Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova intramolecular aminolysis ; peptides ; protein Obor OECD Biochemistry and molecular biology CEP LM2018127 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy EF18_046/0015974 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora UOCHB-X - RVO:61388963 ; BTO-N - RVO:86652036 UT WOS 000938213200001 EID SCOPUS 85148939989 DOI 10.1021/jacs.2c12987 Anotace Whereas modern proteins rely on a quasi-universal repertoire of 20 canonical amino acids (AAs), numerous lines of evidence suggest that ancient proteins relied on a limited alphabet of 10 “early” AAs and that the 10 “late” AAs were products of biosynthetic pathways. However, many nonproteinogenic AAs were also prebiotically available, which begs two fundamental questions: Why do we have the current modern amino acid alphabet and would proteins be able to fold into globular structures as well if different amino acids comprised the genetic code? Here, we experimentally evaluate the solubility and secondary structure propensities of several prebiotically relevant amino acids in the context of synthetic combinatorial 25-mer peptide libraries. The most prebiotically abundant linear aliphatic and basic residues were incorporated along with or in place of other early amino acids to explore these alternative sequence spaces. The results show that foldability was likely a critical factor in the selection of the canonical alphabet. Unbranched aliphatic amino acids were purged from the proteinogenic alphabet despite their high prebiotic abundance because they generate polypeptides that are oversolubilized and have low packing efficiency. Surprisingly, we find that the inclusion of a short-chain basic amino acid also decreases polypeptides’ secondary structure potential, for which we suggest a biophysical model. Our results support the view that, despite lacking basic residues, the early canonical alphabet was remarkably adaptive at supporting protein folding and explain why basic residues were only incorporated at a later stage of protein evolution. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2024 Elektronická adresa https://doi.org/10.1021/jacs.2c12987
Počet záznamů: 1