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Protein Science (2007), 16:82-91. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Human lysosomal DNase II{alpha} contains two requisite PLD-signature (HxK) motifs: Evidence for a pseudodimeric structure of the active enzyme species

Patrick Schäfer1, Iwona A. Cymerman2, Janusz M. Bujnicki2, and Gregor Meiss1

1 Institute of Biochemistry, Faculty of Biology and Chemistry, Justus-Liebig-University Giessen, D-35392 Giessen, Germany
2 Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland

(RECEIVED September 1, 2006; FINAL REVISION October 17, 2006; ACCEPTED October 17, 2006)

Lysosomal DNase II{alpha} is essential for DNA waste removal and auxiliary apoptotic DNA fragmentation in higher eukaryotes. Despite the key role of this enzyme, little is known about its structure–function relationships. Here, mutational and biochemical analyses were used to characterize human DNase II{alpha} variants expressed in mammalian cells. The resulting data strongly support the hypothesis that the enzyme is a monomeric phospholipase D–family member with a pseudodimeric protein fold. According to our results, DNase II{alpha} contains two requisite PLD-signature motifs (113HTK115 and 295HSK297) in the N- and C-terminal subdomains, respectively, that together form a single active site. Based on these data, we present an experimentally validated structural model of DNase II{alpha}.

Keywords: apoptosis; DNA fragmentation; phospholipase D; DNase; structure; active site


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