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the 9th letter of the Roman alphabet (同)i

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iodineの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/03/05 10:00:48」(JST)

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Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1.^[1] DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis.^[2]

DNase I binds to the cytoskeletal protein actin. It binds actin monomers with very high (sub-nanomolar) affinity and actin polymers with lower affinity. The function of this interaction is unclear. However, since actin-bound DNase I is enzymatically inactive, the DNase-actin complex might be a storage form of DNase I that prevents damage of the genetic information.

This gene encodes a member of the DNase family. This protein is stored in the zymogen granules of the nuclear envelope and functions by cleaving DNA in an endonucleolytic manner. At least six autosomal codominant alleles have been characterized, DNASE1*1 through DNASE1*6, and the sequence of DNASE1*2 represented in this record. Mutations in this gene, as well as factor inactivating its enzyme product, have been associated with systemic lupus erythematosus (SLE), an autoimmune disease.^[3]^[4] A recombinant form of this protein is used to treat one of the symptoms of cystic fibrosis by hydrolyzing the extracellular DNA in sputum and reducing its viscosity.^[5] Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.^[1]

References

^ ^a ^b "Entrez Gene: DNASE1 deoxyribonuclease I". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1773.
^ Samejima1, K and Earnshaw, W.C. (2005). "Trashing the genome: the role of nucleases during apoptosis". Nat Rev Mol Cell Biol 6: 677–88. doi:10.1038/nrm1715.
^ Hakkim A, Fürnrohr BG, Amann K, Laube B, Abed UA, Brinkmann V, Herrmann M, Voll RE, Zychlinsky A. (2010). "Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis". Proc Natl Acad Sci U S A 107 (21): 9813–8. doi:10.1073/pnas.0909927107. PMC 2906830. PMID 20439745. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2906830/.
^ Yasutomo K, Horiuchi T, Kagami S, et al. (2001). "Mutation of DNASE1 in people with systemic lupus erythematosus". Nat. Genet. 28 (4): 313–4. doi:10.1038/91070. PMID 11479590.
^ Shak S, Capon DJ, Hellmiss R, et al. (1991). "Recombinant human DNase I reduces the viscosity of cystic fibrosis sputum". Proc. Natl. Acad. Sci. U.S.A. 87 (23): 9188–92. doi:10.1073/pnas.87.23.9188. PMC 55129. PMID 2251263. //www.ncbi.nlm.nih.gov/pmc/articles/PMC55129/.

External links

deoxyribonuclease+I at the US National Library of Medicine Medical Subject Headings (MeSH)

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1. 嚢胞性線維症：肺疾患治療の概要 cystic fibrosis overview of the treatment of lung disease
2. 慢性閉塞性肺疾患（COPD）治療における粘膜作用剤の役割 role of mucoactive agents in the treatment of copd
3. A群レンサ球菌：病原性因子および発症機序 group a streptococcus virulence factors and pathogenic mechanisms
4. 小児における無気肺 atelectasis in children
5. 成人における肺炎随伴性胸水および膿胸 parapneumonic effusion and empyema in adults

English Journal

Transcriptional and epigenetic effects of deleting large regions, alone or in combination, from their natural context in the chicken Ig-β gene.

Chayahara K, Itaya K, Ono M.AbstractPreviously, we used homologous recombination to delete six groups of cell-type-specific DNase I hypersensitive sites (DHSs), potential transcriptional and epigenetic regulators, scattered in and around the Ig-β gene from their natural context in B-lymphocyte-derived chicken DT40 cells. Simultaneous deletion of all six groups completely shut down transcription and epigenetic regulation of the Ig-β gene; therefore, the cooperation of the scattered regulatory regions was essential for transcription and epigenetic regulation. In this study, we regrouped the cell-type-specific DHSs of Ig-β, those in the original six deletions and three additional ones, into three larger regional groups-the long upstream region, the intron, and the long downstream region-and deleted these groups individually or in combination. Combinatorial deletion of all three regional groups decreased Ig-β mRNA levels to 0.4% of the control, which was significantly higher than <0.1%, the level resulting from deletion of all six smaller groups. Histone H3 and H4 acetylation and H3K4 dimethylation levels at the Ig-β promoter were low in cells carrying deletions of all six smaller groups, but intermediate levels of acetylation and enhanced H3K4 dimethylation were observed in cells carrying deletions of all three larger groups. While CG methylation was definitely present at the Ig-β promoter in cells carrying all six smaller deletions, it was nearly absent from the Ig-β promoter in cells carrying all three larger deletions. Thus, combinatorial deletion of larger regulatory regions had less effect on transcription and epigenetic regulation at the chicken Ig-β gene than combinatorial deletion of shorter ones. Analysis of several combinatorial deletions, where combinations included two larger deletions and one smaller deletion, revealed the relative effects of each deletion on transcription of the Ig-β gene. Investigation of the CG methylation status at the Ig-β promoter in one combinatorial deletion demonstrated that USI was involved in the maintenance of CG methylation.
Gene.Gene.2011 Oct 15;486(1-2):1-7. Epub 2011 Jul 2.
Previously, we used homologous recombination to delete six groups of cell-type-specific DNase I hypersensitive sites (DHSs), potential transcriptional and epigenetic regulators, scattered in and around the Ig-β gene from their natural context in B-lymphocyte-derived chicken DT40 cells. Simultaneous
PMID 21749917

Immunolabeling of cells grown attached to a substratum or in suspension with actin antibodies.

Spudich A.AbstractINTRODUCTION Actin is a major component of all eukaryotic cells and is highly conserved across species. The different isoforms of actin show a very high degree of homology, and almost all actins bind cytochalasins, phallotoxins, and DNase I. Actin is important for maintaining cell shape and for myosin-based movements in cells. In addition, the actin cytoskeleton is involved in localization of other molecules in the cytoplasm and in cellular compartmentalization. Polyclonal and monoclonal antibodies with different specificities are commercially available for labeling actin-containing structures in cells. This article describes a protocol for immunolabeling actin that works well for cells grown in tissue culture as monolayers and for cells grown in suspension cultures that can be attached to polylysine-coated coverslips.
Cold Spring Harbor protocols.Cold Spring Harb Protoc.2011 Sep 1;2011(9). pii: pdb.prot065557. doi: 10.1101/pdb.prot065557.
INTRODUCTION Actin is a major component of all eukaryotic cells and is highly conserved across species. The different isoforms of actin show a very high degree of homology, and almost all actins bind cytochalasins, phallotoxins, and DNase I. Actin is important for maintaining cell shape and for myos
PMID 21880818

Japanese Journal

Improvements in Transfection Efficiency with Chitosan Modified Poly(DL-lactide-co-glycolide) Nanospheres Prepared by the Emulsion Solvent Diffusion Method, for Gene Delivery

Tahara Kohei,Sakai Takeshi,Yamamoto Hiromitsu,Takeuchi Hirofumi,Hirashima Naohide,Kawashima Yoshiaki
CHEMICAL & PHARMACEUTICAL BULLETIN 59(3), 298-301, 2011
… These phenomena should be in accordance with the sustained-release profile of pDNA from PLGA NS in the cytosol and the pDNA protection against DNase. …
NAID 130000648936

ヌクレアーゼ抵抗性化学修飾核酸の開発研究

松田彰
YAKUGAKU ZASSHI 131(2), 285-298, 2011
… On the other hand, ODNs containing 4′-C-(aminoethyl)thymidine (14b), which was synthesized by a newly developed radical cyclization-ring-enlargement reaction by us, were 87 times more stable to hydrolysis by DNase I (an endonuclease) and 133 times more stable in 50% human serum than unmodified ODNs. …
NAID 130000451463

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★リンクテーブル★

リンク元	「deoxyribonuclease I」「デオキシリボヌクレアーゼI」「DNA endonuclease」
関連記事	「I」「Id」

「deoxyribonuclease I」

Deoxyribonuclease I
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	4AWN
Identifiers
Symbols	DNASE1; DNL1; DRNI
External IDs	OMIM: 125505 MGI: 103157 HomoloGene: 3826 GeneCards: DNASE1 Gene
EC number	3.1.21.1
Gene Ontology
Molecular function	• actin binding; • deoxyribonuclease I activity; • protein binding;
Cellular component	• extracellular region; • nuclear envelope;
Biological process	• DNA catabolic process; • apoptotic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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