Characterization, crystallization and preliminary X-ray diffraction studies of tomato nuclease I

 

Koval T.1,2, Dohnalek J.2, 3, Lipovova P.4, Podzimek T.4, Matousek J.5

 

1Faculty of Mathematics and Physics, Charles University in Prague, Ke Karlovu 3, 121 16 Praha 2, Czech Republic                                                                                                                                    2Institute of Physics, Cukrovarnicka 10, 162 00 Praha 6, Czech Republic
3Institute of Macromolecular Chemistry AS CR, Heyrovskeho nam.2, 162 06 Praha 6, Czech Republic
                                  4Institute of Chemical Technology, Technicka 5, 166 28  Praha 6, Czech Republic

5Institute of Plant Molecular Biology, Biology Centre, AS CR, Branisovska 31, 37005 Ceske Budejovice, Czech republic

                                     

Tomato Nuclease I is a Zn2+ dependent plant endonuclease, which cleaves both RNA and DNA in ss and ds form. This enzyme belongs to plant nuclease I group, is relatively small glycoprotein and shows considerable activity in cell apoptosis. Therefore detailed structural study of this enzyme can lead to new ways of cancer and bacterial disease treatment. Heterelogous expression yields amounts and quality of the enzyme suitable for structural studies. Biochemical characterisation of tomato nuclease I focused on 3D structure determination using crystallographic methods and also crystallization and preliminary X-ray diffraction experiments are reviewed.