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PMID:16143456
| Citation |
Dassanayake, RP, Griep, MA and Duhamel, GE (2005) The cytolethal distending toxin B sub-unit of Helicobacter hepaticus is a Ca2+- and Mg2+-dependent neutral nuclease. FEMS Microbiol. Lett. 251:219-25 |
|---|---|
| Abstract |
The cytolethal distending toxin B (CdtB) of the mouse pathogen Helicobacter hepaticus has cation binding and DNA catalysis residues in common with members of the mammalian deoxyribonuclease I (DNase I) family. The purpose of the present study was to characterize CdtB nuclease. To establish optimal digestion conditions and to evaluate co-factor requirements, a novel and sensitive fluorometric assay that quantitatively determines double stranded DNA digestion was developed. Although the Ca2+- and Mg2+-dependence and neutral properties of CdtB were similar to DNase I, hydrolysis of DNA by CdtB was approximately 100-fold less active than DNase I and was considerably more resistant to inhibition by ZnCl2 and G-actin. |
| Links |
PubMed Online version:10.1016/j.femsle.2005.08.005 |
| Keywords |
Bacterial Toxins/biosynthesis; Bacterial Toxins/chemistry; Bacterial Toxins/genetics; Bacterial Toxins/toxicity; Calcium/metabolism; Helicobacter hepaticus/enzymology; Helicobacter hepaticus/genetics; Helicobacter hepaticus/metabolism; Magnesium/metabolism; Nucleotidases/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004518: nuclease activity |
ECO:0000314: |
F |
Figure 3 shows DNA catalysis which can be recognized in known members of mammalian deoxyribonuclease 1 (DNase 1). |
complete | ||||
|
enables |
GO:0004518: nuclease activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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