- 関
- deoxyribonuclease I、DNA endonuclease
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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 |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
4AWN
|
|
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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 |
Species |
Human |
Mouse |
|
Entrez |
1773 |
13419 |
|
Ensembl |
ENSG00000213918 |
ENSMUSG00000005980 |
|
UniProt |
P24855 |
P49183 |
|
RefSeq (mRNA) |
NM_005223 |
NM_010061 |
|
RefSeq (protein) |
NP_005214 |
NP_034191 |
|
Location (UCSC) |
Chr 16:
3.66 – 3.73 Mb |
Chr 16:
4.04 – 4.04 Mb |
|
PubMed search |
[1] |
[2] |
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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/.
Further reading
- Lachmann PJ (2003). "Lupus and desoxyribonuclease". Lupus 12 (3): 202–6. doi:10.1191/0961203303lu357xx. PMID 12708782.
- Yasuda T, Awazu S, Sato W, et al. (1991). "Human genetically polymorphic deoxyribonuclease: purification, characterization, and multiplicity of urine deoxyribonuclease I". J. Biochem. 108 (3): 393–8. PMID 2277032.
- Kishi K, Yasuda T, Ikehara Y, et al. (1990). "Human serum deoxyribonuclease I (DNase I) polymorphism: pattern similarities among isozymes from serum, urine, kidney, liver, and pancreas". Am. J. Hum. Genet. 47 (1): 121–6. PMC 1683738. PMID 2349940. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1683738/.
- Kabsch W, Mannherz HG, Suck D, et al. (1990). "Atomic structure of the actin:DNase I complex". Nature 347 (6288): 37–44. doi:10.1038/347037a0. PMID 2395459.
- Kishi K, Yasuda T, Awazu S, Mizuta K (1989). "Genetic polymorphism of human urine deoxyribonuclease I". Hum. Genet. 81 (3): 295–7. doi:10.1007/BF00279009. PMID 2921043.
- Rosenstreich DL, Tu JH, Kinkade PR, et al. (1988). "A human urine-derived interleukin 1 inhibitor. Homology with deoxyribonuclease I". J. Exp. Med. 168 (5): 1767–79. doi:10.1084/jem.168.5.1767. PMC 2189114. PMID 3263467. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2189114/.
- Yasuda T, Nadano D, Takeshita H, et al. (1995). "Molecular analysis of the third allele of human deoxyribonuclease I polymorphism". Ann. Hum. Genet. 59 (Pt 2): 139–47. doi:10.1111/j.1469-1809.1995.tb00737.x. PMID 7625762.
- Yasuda T, Kishi K, Yanagawa Y, Yoshida A (1995). "Structure of the human deoxyribonuclease I (DNase I) gene: identification of the nucleotide substitution that generates its classical genetic polymorphism". Ann. Hum. Genet. 59 (Pt 1): 1–15. doi:10.1111/j.1469-1809.1995.tb01601.x. PMID 7762978.
- Yasuda T, Nadano D, Iida R, et al. (1995). "Chromosomal assignment of the human deoxyribonuclease I gene, DNASE 1 (DNL1), to band 16p13.3 using the polymerase chain reaction". Cytogenet. Cell Genet. 70 (3–4): 221–3. doi:10.1159/000134038. PMID 7789176.
- Yasuda T, Nadano D, Takeshita H, et al. (1995). "The molecular basis for genetic polymorphism of human deoxyribonuclease I: identification of the nucleotide substitution that generates the fourth allele". FEBS Lett. 359 (2–3): 211–4. doi:10.1016/0014-5793(95)00037-A. PMID 7867802.
- Yasuda T, Nadano D, Tenjo E, et al. (1996). "Genotyping of human deoxyribonuclease I polymorphism by the polymerase chain reaction". Electrophoresis 16 (10): 1889–93. doi:10.1002/elps.11501601310. PMID 8586059.
- Iida R, Yasuda T, Takeshita H, et al. (1996). "Identification of the nucleotide substitution that generates the fourth polymorphic site in human deoxyribonuclease I (DNase I)". Hum. Genet. 98 (4): 415–8. doi:10.1007/s004390050231. PMID 8792814.
- Iida R, Yasuda T, Aoyama M, et al. (1998). "The fifth allele of the human deoxyribonuclease I (DNase I) polymorphism". Electrophoresis 18 (11): 1936–9. doi:10.1002/elps.1150181108. PMID 9420147.
- Yasuda T, Takeshita H, Iida R, et al. (1999). "A new allele, DNASE1*6, of human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its instability". Biochem. Biophys. Res. Commun. 260 (1): 280–3. doi:10.1006/bbrc.1999.0900. PMID 10381379.
- Oliveri M, Daga A, Cantoni C, et al. (2001). "DNase I mediates internucleosomal DNA degradation in human cells undergoing drug-induced apoptosis". Eur. J. Immunol. 31 (3): 743–51. doi:10.1002/1521-4141(200103)31:3<743::AID-IMMU743>3.0.CO;2-9. PMID 11241278.
- Otterbein LR, Graceffa P, Dominguez R (2001). "The crystal structure of uncomplexed actin in the ADP state". Science 293 (5530): 708–11. doi:10.1126/science.1059700. PMID 11474115.
- 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.
- Ballweber E, Galla M, Aktories K, et al. (2001). "Interaction of ADP-ribosylated actin with actin binding proteins". FEBS Lett. 508 (1): 131–5. doi:10.1016/S0014-5793(01)03040-X. PMID 11707283.
- Tsutsumi S, Kaneko Y, Asao T, et al. (2002). "DNase I is present in the chief cells of human and rat stomachs". Histochem. J. 33 (9–10): 531–5. doi:10.1023/A:1014999624430. PMID 12005024.
External links
- deoxyribonuclease+I at the US National Library of Medicine Medical Subject Headings (MeSH)
Hydrolase: esterases (EC 3.1)
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3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
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3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
|
3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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|
3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
|
|
3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
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Exoribonuclease |
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3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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|
Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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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
- 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
Related Links
- Recombinant DNase I(RNase-free)はウシ膵臓由来のDNase I遺伝子を発現・精製した組 換えタンパク質で、一本鎖および二本鎖のDNAを同程度にランダムに分解し、5'-P末端を 持つオリゴヌクレオチドを生成させる、endodeoxyribonucleaseである。 ...
Related Pictures
★リンクテーブル★
[★]
デオキシリボヌクレアーゼI
- 関
- DNA endonuclease、DNase I
[★]
- 英
- deoxyribonuclease I、DNase I
- 関
- DNAエンドヌクレアーゼ
[★]
DNAエンドヌクレアーゼ
- 関
- deoxyribonuclease I、DNase I
[★]
[★]