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Bioinformatics Advance Access published online on September 8, 2005
Bioinformatics, doi:10.1093/bioinformatics/bti659
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© The Author (2005). Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
Received February 25, 2005
Revised July 16, 2005
Accepted September 1, 2005

Discovery note

DNase II is a member of the phospholipase D superfamily

Iwona A. Cymerman 1, Gregor Meiss 2, and Janusz M. Bujnicki 1*

1 Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology, Trojdena 4, 02-109 Warsaw, Poland
2 Institute of Biochemistry, Justus-Liebig-University Giessen, 35392 Giessen, Germany

* To whom correspondence should be addressed.
Janusz M. Bujnicki, E-mail: iamb{at}genesilico.pl


  Abstract

Motivation: DNase II is an endodeoxyribonuclease involved in apoptosis and essential for the mammalian development. Despite the understanding of biochemical properties of this enzyme, its structure and relationships to other protein families remain unknown.

Results: Using protein fold-recognition we found that DNase II exhibits a catalytic domain common to the phospholipase D superfamily. Our model explains the available experimental data, and provides the first structural platform for sequence-function analyses of this important nuclease.


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