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1

A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis thaliana that is activated preferentially by Mn2+ ions

100%

Szurmak B., Wysłouch-Cieszyńska A., Wszelaka-Rylik M., Bal W., Dobrzańska M.

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2008

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vol. 55

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issue 1

151-160

EN

Asymmetrical diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolases are key enzymes controlling the in vivo concentration of Ap4A - an important signaling molecule involved in regulation of DNA replication and repair, signaling in stress response and apoptosis. Sequence homologies indicate that the genome of the model plant Arabidopsis thaliana contains at least three open reading frames encoding presumptive Ap4A hydrolases: At1g30110, At3g10620, and At5g06340. In this work we present efficient overexpression and detailed biochemical characteristics of the AtNUDX25 protein encoded by the At1g30110 gene. Aided by the determination of the binding constants of Mn(Ap4A) and Mg(Ap4A) complexes using isothermal titration calorimetry (ITC) we show that AtNUDX25 preferentially hydrolyzes Ap4A in the form of a Mn2+ complex.

2

Phosphorylation in vitro and in vivo of the wheat embryo RNA polymerase II

85%

Mazuś B., Szurmak B., Buchowicz J.

Acta Biochimica Polonica

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1980

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vol. 27

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issue 1

9-19

3

Autonomous replication of a wheat DNA sequence in isolated wheat nuclei

85%

Szurmak B., Buchowicz J.

Acta Biochimica Polonica

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1997

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vol. 44

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issue 1

79-82

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3 Acta Biochimica Polonica

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3 Szurmak B.

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1 Dobrzańska M.

1 Mazuś B.

1 Wszelaka-Rylik M.

1 Wysłouch-Cieszyńska A.

A diadenosine 5',5''-P1P4 tetraphosphate (Ap4A) hydrolase from Arabidopsis thaliana that is activated preferentially by Mn2+ ions

Phosphorylation in vitro and in vivo of the wheat embryo RNA polymerase II

Autonomous replication of a wheat DNA sequence in isolated wheat nuclei