Human lysosomal DNase II contains two requisite PLD-signature (HxK) motifs: Evidence for a pseudodimeric structure of the active enzyme species
| Autor: | Gregor Meiss, Iwona A. Cymerman, Patrick Schäfer, Janusz M. Bujnicki |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Folding Protein Conformation Amino Acid Motifs Molecular Sequence Data In Vitro Techniques Biology Biochemistry Article chemistry.chemical_compound Protein structure Catalytic Domain Humans Amino Acid Sequence Molecular Biology Endodeoxyribonucleases Sequence Homology Amino Acid Phospholipase D Mutagenesis Apoptotic DNA fragmentation Recombinant Proteins Protein Structure Tertiary Amino Acid Substitution chemistry Mutagenesis Site-Directed DNA fragmentation DNase I hypersensitive site Lysosomes Hypersensitive site DNA |
| Zdroj: | Protein Science. 16:82-91 |
| ISSN: | 1469-896X 0961-8368 |
| Popis: | Lysosomal DNase IIalpha 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 IIalpha 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 IIalpha contains two requisite PLD-signature motifs ((113)HTK(115) and (295)HSK(297)) 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 IIalpha. |
| Databáze: | OpenAIRE |
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