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Stability of the Complex between Yeast Seryl-tRNA Synthetase and tRNASer under Different Electrophoretic Conditions

Ita Gruić-Sovulj ; Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia
Jasmina Rokov-Plavec ; Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia
Marko Močibob ; Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia
Tomislav Kamenski ; Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia
Ivana Weygand-Đurašević ; Department of Chemistry, Faculty of Science, University of Zagreb, Strossmayerov trg 14, 10000 Zagreb, Croatia


Puni tekst: engleski pdf 125 Kb

str. 599-604

preuzimanja: 325

citiraj


Sažetak

Noncovalent interactions of yeast homodimeric seryl-tRNA synthetase (SerRS) and cognate tRNASer were studied by the gel mobility shift assay and zone-interference gel electrophoresis performed under the same binding and electrophoretic conditions. Purified tRNASer as well as total yeast tRNA were applied as ligands. In the absence of Mg2+, SerRS:(tRNASer)1 noncovalent complex was detected only by zone-interference gel electrophoresis. Kd values determined in the presence and absence of Mg2+ were in the same range, suggesting that Mg2+ ions mainly influence dissociation-association kinetics of the complex, with a minor contribution to its thermodynamic stability. Comparison of these two assays was shown to be useful in the analysis of thermodynamic and kinetic properties of protein:nucleic acid complexes.

Ključne riječi

aminoacyl-tRNA synthetase, gel mobility shift assay, zone-interference gel electrophoresis, SerRS:tRNA<sup>Ser</sup> noncovalent complexes, Mg<sup>2+</sup> influence

Hrčak ID:

102984

URI

https://hrcak.srce.hr/102984

Posjeta: 571 *