Gruić-Sovulj, Ita; Rokov-Plavec, Jasmina; Močibob, Marko; Kamenski, Tomislav; Weygand-Đurašević, Ivana
(2004)
Stability of the complex between yeast seryl-tRNA synthetase and tRNA(Ser) under different electrophoretic conditions.
Croatica Chemica Acta, 77
(4).
pp. 599-604.
ISSN 0011-1643
Abstract
Noncovalent interactions of yeast homodimeric seryl-tRNA synthetase (SerRS) and cognate tRNA(Ser) were studied by the gel mobility shift assay and zone-interference gel electrophoresis performed under the same binding and electrophoretic conditions. Purified tRNA(Ser) as well as total yeast tRNA were applied as ligands. In the absence of Mg2+ SerRS:(tRNA(Ser))(1) noncovalent complex was detected only by zone-interference gel electrophoresis. K-d 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.
Item Type: |
Article
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Uncontrolled Keywords: |
aminoacyl-tRNA synthetase; gel mobility shift assay; zone-interference gel electrophoresis; SerRS : tRNAs(Ser) noncovalent complexes; Mg2+ influence; aminoacyl-transfer-rna; elongation-factor-tu; escherichia-coli; gel-electrophoresis; thermus-thermophilus; transfer rna(ser); binding; recognition; specificity; magnesium |
Subjects: |
NATURAL SCIENCES > Chemistry |
Divisions: |
Division of Molecular Medicine |
Projects: |
Project title | Project leader | Project code | Project type |
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Seril-tRNA-sintetaze: mehanizmi i kontrola serilacije u biosintezi proteina | Ivana Weygand-Đurašević | 0119650 | MZOS |
|
Depositing User: |
Tomislav Štrkalec
|
Date Deposited: |
08 Nov 2013 12:07 |
URI: |
http://fulir.irb.hr/id/eprint/908 |
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908
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