In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00556783" target="_blank" >RIV/61388963:_____/22:00556783 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/22:00556783 RIV/00216208:11310/22:10444662
Result on the web
<a href="https://doi.org/10.1093/molbev/msac032" target="_blank" >https://doi.org/10.1093/molbev/msac032</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/molbev/msac032" target="_blank" >10.1093/molbev/msac032</a>
Alternative languages
Result language
angličtina
Original language name
In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions
Original language description
RNA-peptide/protein interactions have been of utmost importance to life since its earliest forms, reaching even before the last universal common ancestor (LUCA). However, the ancient molecular mechanisms behind this key biological interaction remain enigmatic because extant RNA-protein interactions rely heavily on positively charged and aromatic amino acids that were absent (or heavily under-represented) in the early pre-LUCA evolutionary period. Here, an RNA-binding variant of the ribosomal uL11 C-terminal domain was selected from an approximately 10(10) library of partially randomized sequences, all composed of ten prebiotically plausible canonical amino acids. The selected variant binds to the cognate RNA with a similar overall affinity although it is less structured in the unbound form than the wild-type protein domain. The variant complex association and dissociation are both slower than for the wild-type, implying different mechanistic processes involved. The profile of the wild-type and mutant complex stabilities along with molecular dynamics simulations uncovers qualitative differences in the interaction modes. In the absence of positively charged and aromatic residues, the mutant uL11 domain uses ion bridging (K+/Mg2+) interactions between the RNA sugar-phosphate backbone and glutamic acid residues as an alternative source of stabilization. This study presents experimental support to provide a new perspective on how early protein-RNA interactions evolved, where the lack of aromatic/basic residues may have been compensated by acidic residues plus metal ions.
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
Result was created during the realization of more than one project. More information in the Projects tab.
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
Molecular Biology and Evolution
ISSN
0737-4038
e-ISSN
1537-1719
Volume of the periodical
39
Issue of the periodical within the volume
3
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
msac032
UT code for WoS article
000764264700001
EID of the result in the Scopus database
2-s2.0-85125682104