デオキシリボヌクレアーゼI
- 関
- DNA endonuclease、DNase I
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/01/20 00:55:32」(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
• endodeoxyribonuclease activity
• deoxyribonuclease I activity
• protein binding
|
Cellular component |
• extracellular region
• nucleus
• nuclear envelope
• extracellular exosome
|
Biological process |
• DNA catabolic process, endonucleolytic
• apoptotic process
|
Sources: Amigo / QuickGO |
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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:
3.61 – 3.68 Mb |
Chr 16:
4.04 – 4.04 Mb |
PubMed search |
[1] |
[2] |
|
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]
In genomics
In genomics, DNase I hypersensitive sites are thought to be characterized by open, accessible chromatin; therefore, a DNase I sensitivity assay is a widely used methodology in genomics for identifying which regions of the genome are likely to contain active genes [6]
DNase I Sequence Specificity
It has been recently reported that DNase I shows some levels of sequence specificity that may depend on experimental conditions.[7] In contrast to other enzymes which have high substrate specificity, DNase I certainly does not cleave with an absolute sequence specificity. However, cleavage at sites that contain C or G at their 3' end is less efficient.
References
- ^ a b "Entrez Gene: DNASE1 deoxyribonuclease I".
- ^ 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.
- ^ 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.
- ^ Boyle AP, Davis S, Shulha HP, Meltzer P, Margulies EH, Weng Z, Furey TS, Crawford GE (2008). "High-resolution mapping and characterization of open chromatin across the genome". Cell 132: 311–322. doi:10.1016/j.cell.2007.12.014. PMC 2669738. PMID 18243105.
- ^ Koohy, Hashem; Down, Thomas A.; Hubbard, Tim J.; Mariño-Ramírez, Leonardo (26 July 2013). "Chromatin Accessibility Data Sets Show Bias Due to Sequence Specificity of the DNase I Enzyme". PLoS ONE 8 (7): e69853. doi:10.1371/journal.pone.0069853.
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.
- 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.
- 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
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3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein 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
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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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
- Five non-synonymous SNPs in the gene encoding human deoxyribonuclease I-like 2 implicated in terminal differentiation of keratinocytes reduce or abolish its activity.
- Ueki M, Fujihara J, Kimura-Kataoka K, Takeshita H, Iida R, Yasuda T.SourceDivision of Medical Genetics and Biochemistry, Faculty of Medical Sciences, University of Fukui, Eiheiji, Fukui, Japan.
- Electrophoresis.Electrophoresis.2013 Feb;34(3):456-62. doi: 10.1002/elps.201200415. Epub 2013 Jan 3.
- Several non-synonymous SNPs in the human deoxyribonuclease I-like 2 (DNase 1L2) gene responsible for DNA degradation during terminal differentiation of epidermal keratinocytes have been identified. However, only limited population data are available, and furthermore the effect of these SNPs on the D
- PMID 23161465
- Genomic occupancy of HLH, AP1 and Runx2 motifs within a nuclease sensitive site of the Runx2 gene.
- Hovhannisyan H, Zhang Y, Hassan MQ, Wu H, Glackin C, Lian JB, Stein JL, Montecino M, Stein GS, van Wijnen AJ.SourceDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
- Journal of cellular physiology.J Cell Physiol.2013 Feb;228(2):313-21. doi: 10.1002/jcp.22109.
- Epigenetic mechanisms mediating expression of the Runt-related transcription factor Runx2 are critical for controlling its osteogenic activity during skeletal development. Here, we characterized bona fide regulatory elements within 120 kbp of the endogenous bone-related Runx2 promoter (P1) in oste
- PMID 22886425
- Changes in histone modification and DNA methylation of the StAR and Cyp19a1 promoter regions in granulosa cells undergoing luteinization during ovulation in rats.
- Lee L, Asada H, Kizuka F, Tamura I, Maekawa R, Taketani T, Sato S, Yamagata Y, Tamura H, Sugino N.SourceDepartment of Obstetrics and Gynecology, Yamaguchi University Graduate School of Medicine, Minamikogushi 1-1-1, Ube 755-8505, Japan.
- Endocrinology.Endocrinology.2013 Jan;154(1):458-70. doi: 10.1210/en.2012-1610. Epub 2012 Nov 26.
- The ovulatory LH surge induces rapid up-regulation of steroidogenic acute regulatory (StAR) protein and rapid down-regulation of aromatase (Cyp19a1) in granulosa cells (GCs) undergoing luteinization during ovulation. This study investigated in vivo whether epigenetic mechanisms including histone mod
- PMID 23183184
Japanese Journal
- ノニルフェノールポリエトキシレートはどのようにしてDNA二本鎖切断を誘導するのか
- 豊岡 達士,伊吹 裕子
- 日本毒性学会学術年会 40.1(0), 1002020, 2013
- … 本研究ではNPEOsによるDSBs生成メカニズムをDNAのホスホジエステル結合を切断・分解する酵素であるDeoxyribonuclease I (DNase I)に着目し検討、その一端を明らかにしたので報告する。 …
- NAID 130004676500
- 第99回生涯教育講座 自己免疫疾患と関連するDeoxyribonuclease Ⅱ(DNase Ⅱ)遺伝子SNPと酵素プロモーター活性の相関解析
- 竹下 治男
- 島根医学 : the journal of the Shimane Medical Association 32(4), 169-177, 2012-12
- NAID 40019567450
- Serum deoxyribonuclease l activity can be a useful diagnostic marker for the early diagnosis of unstable angina pectoris or non-ST-segment elevation myocardial infarction
- FUJIBAYASHI Kousuke,KAWAI Yasuyuki,KITAYAMA Michihiko,AKAO Hironubu,ISHIDA Ryoko,MOTOYAMA Atsushi,WAKASA Minoru,ARAKAWA Kenichiro,UEKI Misuzu,KAJINAMI Kouji,YASUDA Toshihiro
- Journal of cardiology 59(3), 258-265, 2012-05-15
- NAID 10031187744
Related Links
- Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding ...
Related Pictures
★リンクテーブル★
[★]
- 関
- deoxyribonuclease I、DNA endonuclease
[★]
- 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
[★]
デオキシリボヌクレアーゼIV
- 関
- endonuclease IV
[★]
[★]
デオキシリボヌクレアーゼ、DNA分解酵素
- 関
- desoxyribonuclease、DNA nuclease、DNAase、DNase
- 同
- dornase
[★]