DNase II: genes, enzymes and function

Evans, Cory J.; Aguilera, Renato J.

doi:10.1016/j.gene.2003.08.022

Cited by 214 publications

(161 citation statements)

References 82 publications

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Section: Introductionmentioning

confidence: 92%

“…In the collagen type IV-specific enhancer-promoter Cg-gal4 line, GAL4 is predominantly expressed in the fat body, anterior-most lobes of the lymph gland and hemocytes but apparently not in lamellocytes [21]. Additional lines that were obtained from the fly stock center were the following: yw, DNase II lo , Df(3R)Sr16 or w[*]:Df(3R)Sr16, h [1] …”

Section: Drosophila Stocksmentioning

confidence: 99%

“…Unlike most nucleases, these enzymes do not require divalent cations and are most active at an acidic pH [1,2]. Consistent with a generalized role in DNA degradation and an acidic pH optima, DNase II enzymes exhibit a ubiquitous tissue distribution and are localized within lysosomes [1,3]. While DNase II enzymes can degrade DNA substrates to completion, they also exhibit cleavage preferences that are site-and speciesspecific [1,[4][5][6].…”

Section: Introductionmentioning

confidence: 96%

“…In these mutant mice, removal of apoptotic cell DNA was apparently efficiently mediated by phagocytosis and the action of DNase II [17]. As would be expected, CAD-deficient flies exhibit a loss of nucleosomal DNA fragmentation, while flies deficient in DNase II (DNase II lo mutants) exhibited an enhanced fragmentation phenotype (due to the action of CAD [1,18]). Since flies deficient in both enzymes did not contain fragmented/degraded DNA [18], it would appear that CAD is required to generate the nucleosomal fragments while DNase II is required to completely degrade such fragments.…”

Section: Introductionmentioning

confidence: 99%

“…DNase II enzymes belong to a unique family of nucleases whose main function is to degrade DNA within phagolysosomes [1,2]. Unlike most nucleases, these enzymes do not require divalent cations and are most active at an acidic pH [1,2].…”

Section: Introductionmentioning

confidence: 99%

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DNase II deficiency impairs innate immune function in Drosophila

Seong

Varela-Ramı́rez

Aguilera

2006

Cellular Immunology

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DNase II enzymes are highly conserved proteins that are required for the degradation of DNA within phagolysosomes. Engulfment of apoptotic cells and/or bacteria by phagocytic cells requires the function of DNase II to completely destroy ingested DNA. Mutation of the dnase II gene results in an increase of undegraded apoptotic DNA within phagocytic cells in mice and nematodes. Additionally, reduction of DNase II enzymatic activity in Drosophila melanogaster has been shown to lead to increased accumulation of DNA in the ovaries. Due to the importance of DNA clearance during infection, we hypothesized that a severe reduction of DNase II activity would result in diminished immune function and viability. To test this hypothesis, we knocked down DNase II activity in flies using RNAi. As expected, expression of a dnase II-RNAi construct in flies resulted in a dramatic reduction of DNase II activity and a significant decrease in total hemocyte numbers. Furthermore, infection of dnase II-RNAi flies with Gram negative or positive bacteria resulted in a severe reduction in fly viability. These results confirm that DNase II and the ability to clear macromolecular DNA is essential for maintaining proper immune function in Drosophila.

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