Modern and prebiotic amino acids support distinct structural profiles in proteins
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00559020" target="_blank" >RIV/61388963:_____/22:00559020 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/22:10450824
Result on the web
<a href="https://doi.org/10.1098/rsob.220040" target="_blank" >https://doi.org/10.1098/rsob.220040</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1098/rsob.220040" target="_blank" >10.1098/rsob.220040</a>
Alternative languages
Result language
angličtina
Original language name
Modern and prebiotic amino acids support distinct structural profiles in proteins
Original language 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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GJ17-10438Y" target="_blank" >GJ17-10438Y: Terrestrial protein sequence and structure space evolution</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Open Biology
ISSN
2046-2441
e-ISSN
2046-2441
Volume of the periodical
12
Issue of the periodical within the volume
6
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
220040
UT code for WoS article
000814138000003
EID of the result in the Scopus database
2-s2.0-85132280123