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Ensuring correct translation of the genetic code : interactions between aminoacyl-tRNA synthetases and their amino acid ligands

  • Aminoacyl-tRNA synthetases (aaRSs) are key enzymes in the process of protein biosynthesis, charging tRNA molecules with their corresponding amino acid. Whereas adenosine phosphate fixation is common to all aaRSs, recognition of the respective amino acid to ensure correct translation poses a complex task, which is still not understood to its full extent. Using all aaRS structures in the Protein Data Bank (PDB), this thesis reveals further details about the specificitydetermining interactions of each aaRS. Moreover, inspection of the similarities between these enzymes using the structure-derived interaction data reinforces the sequence-based evolutionary trace of aaRSs to a certain degree: The concurrent development of two distinct Classes of aaRS is apparent at functional level, and previously determined evolutionary subclasses coincide altogether with specific aminoacyl recognition in each aaRS Type. Still, discrimination of amino acids in aaRSs involves a multitude of further relevant mechanisms. Eventually, analysis of specificity-relevant binding site interactions sheds light on how aaRS evolved to distinguish different amino acids.

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Metadaten
Author:Sarah Krautwurst
Advisor:Dirk Labudde, Florian Kaiser
Document Type:Bachelor Thesis
Language:English
Year of Completion:2018
Granting Institution:Hochschule Mittweida
Release Date:2020/08/26
GND Keyword:Proteinbiosynthese
Note:
Printexemplar Präsenz
Institutes:Angewandte Computer‐ und Bio­wissen­schaften
DDC classes:572.645 Proteinbiosynthese
Open Access:Innerhalb der Hochschule
Licence (German):License LogoUrheberrechtlich geschützt