Protein domains of aminoacyl-tRNA synthetases and interactions with other proteins

Podolski, Marija (2009) Protein domains of aminoacyl-tRNA synthetases and interactions with other proteins. Diploma thesis, Faculty of Science > Department of Biology.

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Recently resolved crystal structure of methanogenic type seryl-tRNA synthetase (SerRS) from Methanosarcina barkeri revealed some atypical features, one of which was an idiosyncratic helix-turn-helix motif within C-terminal domain of the protein. This motif seems to be important for dimerization of the enzyme and interaction between Nand C-terminal domains. This assumption was supported by our experimental results achieved by yeast two-hybrid assays. In addition, the yeast two-hybrid approach was used to screen for proteins interacting with SerRS in Methanothermobacter thermautotrophicus. One of the proteins which was found to interact with SerRS was arginyl-tRNA synthetase. To support this finding, we proved this interaction by affinity chromatography (GST-pulldown assay). As it was established for some methanogenic type SerRSs previously, some of these enzymes are capable of recognizing both eukaryotic and prokariotyc tRNASer in addition to the homologous tRNASer and tRNASec substrates. Our results indicate that this feature is also displayed by M.thermautotrophicus SerRS.

Item Type: Thesis (Diploma thesis)
Keywords: seryl-tRNA synthetase, protein-protein interactions, methanogenic archaea, yeast two-hybrid system
Supervisor: Weygand-Đurašević, Ivana
Date: 2009
Number of Pages: 91
Subjects: NATURAL SCIENCES > Biology
Divisions: Faculty of Science > Department of Biology
Depositing User: Silvana Šehić
Date Deposited: 12 Sep 2014 08:34
Last Modified: 12 Sep 2014 08:34

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