Gruić-Sovulj, Ita; Rokov-Plavec, Jasmina; Močibob, Marko; Kamenski, Tomislav; Weygand-Đurašević, Ivana
Stability of the complex between yeast seryl-tRNA synthetase and tRNA(Ser) under different electrophoretic conditions.
Croatica Chemica Acta, 77
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.
||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
||NATURAL SCIENCES > Chemistry
||Division of Molecular Medicine
|Project title||Project leader||Project code||Project type|
|Seril-tRNA-sintetaze: mehanizmi i kontrola serilacije u biosintezi proteina||Ivana Weygand-Đurašević||0119650||MZOS|
||08 Nov 2013 12:07
||26 Feb 2014 12:08
Actions (login required)