RNASEH1

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Ribonukleaza H1

PDB prikaz baziran na 2qk9.
Dostupne strukture
2QK9, 2QKB, 2QKK, 3BSU
Identifikatori
SimboliRNASEH1; H1RNA; RNH1
Vanjski IDOMIM: 604123 MGI: 1335073 HomoloGene: 2202 GeneCards: RNASEH1 Gene
EC broj3.1.26.4
Ontologija gena
Molekulska funkcija • vezivanje jona magnezijuma
• vezivanje nukleinske kiseline
• RNK vezivanje
Ćelijska komponenta • nukleus
• mitohondrija
Biološki proces • mitohondrijska DNK replikacija
• RNK katabolički proces
Ortolozi
VrstaČovekMiš
Entrez24624319819
EnsemblENSG00000171865ENSMUSG00000020630
UniProtO60930E9QLN8
Ref. Sekv. (iRNK)NM_002936NM_011275
Ref. Sekv. (protein)NP_002927NP_035405
Lokacija (UCSC)Chr 2:
3.59 - 3.61 Mb		Chr 12:
28.65 - 28.66 Mb
PubMed pretraga[1][2]

Ribonukleaza H1, takođe poznata kao RNaza H1, je enzim, koji je kod ljudi kodiran RNASEH1 genom.[1][2][3] RNaza H1 je nespecifična endonukleaza koja katalizuje presecanje RNK hidrolitičkim mehanizmom.

Reference

  1. ↑ „Entrez Gene: ribonuclease H1”. 
  2. ↑ ten Asbroek AL, van Groenigen M, Jakobs ME, Koevoets C, Janssen B, Baas F (June 2002). „Ribonuclease H1 maps to chromosome 2 and has at least three pseudogene loci in the human genome”. Genomics 79 (6): 818–23. DOI:10.1006/geno.2002.6776. PMID 12036296. 
  3. ↑ Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W (October 2007). „Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription”. Mol. Cell 28 (2): 264–76. DOI:10.1016/j.molcel.2007.08.015. PMID 17964265. 

Literatura

  • Nowotny M, Cerritelli SM, Ghirlando R, et al. (2008). „Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.”. EMBO J. 27 (7): 1172–81. DOI:10.1038/emboj.2008.44. PMC 2323259. PMID 18337749. 
  • Lima WF, Wu H, Nichols JG, et al. (2003). „Human RNase H1 uses one tryptophan and two lysines to position the enzyme at the 3'-DNA/5'-RNA terminus of the heteroduplex substrate.”. J. Biol. Chem. 278 (50): 49860–7. DOI:10.1074/jbc.M306543200. PMID 14506260. 
  • Lima WF, Rose JB, Nichols JG, et al. (2007). „The positional influence of the helical geometry of the heteroduplex substrate on human RNase H1 catalysis.”. Mol. Pharmacol. 71 (1): 73–82. DOI:10.1124/mol.106.025429. PMID 17028157. 
  • Lima WF, Nichols JG, Wu H, et al. (2004). „Structural requirements at the catalytic site of the heteroduplex substrate for human RNase H1 catalysis.”. J. Biol. Chem. 279 (35): 36317–26. DOI:10.1074/jbc.M405035200. PMID 15205459. 
  • Otsuki T, Ota T, Nishikawa T, et al. (2005). „Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries.”. DNA Res. 12 (2): 117–26. DOI:10.1093/dnares/12.2.117. PMID 16303743. 
  • Wu H, Lima WF, Crooke ST (1999). „Properties of cloned and expressed human RNase H1.”. J. Biol. Chem. 274 (40): 28270–8. DOI:10.1074/jbc.274.40.28270. PMID 10497183. 
  • Frank P, Braunshofer-Reiter C, Pöltl A, Holzmann K (1998). „Cloning, subcellular localization and functional expression of human RNase HII.”. Biol. Chem. 379 (12): 1407–12. DOI:10.1515/bchm.1998.379.12.1407. PMID 9894807. 
  • Wu H, Lima WF, Zhang H, et al. (2004). „Determination of the role of the human RNase H1 in the pharmacology of DNA-like antisense drugs.”. J. Biol. Chem. 279 (17): 17181–9. DOI:10.1074/jbc.M311683200. PMID 14960586. 
  • Hillier LW, Graves TA, Fulton RS, et al. (2005). „Generation and annotation of the DNA sequences of human chromosomes 2 and 4.”. Nature 434 (7034): 724–31. DOI:10.1038/nature03466. PMID 15815621. 
  • Lima WF, Wu H, Nichols JG, et al. (2003). „Human RNase H1 activity is regulated by a unique redox switch formed between adjacent cysteines.”. J. Biol. Chem. 278 (17): 14906–12. DOI:10.1074/jbc.M211279200. PMID 12473655. 
  • ten Asbroek AL, van Groenigen M, Nooij M, Baas F (2002). „The involvement of human ribonucleases H1 and H2 in the variation of response of cells to antisense phosphorothioate oligonucleotides.”. Eur. J. Biochem. 269 (2): 583–92. DOI:10.1046/j.0014-2956.2001.02686.x. PMID 11856317. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). „The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”. Genome Res. 14 (10B): 2121–7. DOI:10.1101/gr.2596504. PMC 528928. PMID 15489334. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). „Complete sequencing and characterization of 21,243 full-length human cDNAs.”. Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039. 
  • Cerritelli SM, Crouch RJ (1998). „Cloning, expression, and mapping of ribonucleases H of human and mouse related to bacterial RNase HI.”. Genomics 53 (3): 300–7. DOI:10.1006/geno.1998.5497. PMID 9799596. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). „Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
  • Cerritelli SM, Frolova EG, Feng C, et al. (2003). „Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice.”. Mol. Cell 11 (3): 807–15. DOI:10.1016/S1097-2765(03)00088-1. PMID 12667461. 
  • Lima WF, Rose JB, Nichols JG, et al. (2007). „Human RNase H1 discriminates between subtle variations in the structure of the heteroduplex substrate.”. Mol. Pharmacol. 71 (1): 83–91. DOI:10.1124/mol.106.025015. PMID 17028158. 
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3.1.1: Hidrolaze karboksilnih estara
Holinesteraza (Acetilholinesteraza, Butirilholinesteraza) • Pektinesteraza • 6-fosfoglukonolaktonaza • PAF acetilhidrolaza

Lipaza (Zavisna od žučnih soli, Gastrična/Lingvalna, Pankreasna, Lizozomalna, Hormon-sensitivna, Endotelna, Hepatička, Lipoproteinska, Monoacilglicerolna, Diacilglicerolna)

Fosfolipaza (A1, A2, B)
3.1.2: Tioesteraza
Tioesteraza palmitoil proteina • Ubikvitin karboksilni-terminal hidrolaza L1
3.1.3: Fosfataza
Alkalna fosfataza (ALPI, ALPL, ALPP) • Kiselinska fosfataza (Prostatična)/Tartrat-otporna kiselinska fosfataza/Fosfataze purpurne kiseline • Nukleotidaza • Glukoza 6-fosfataza • Fruktoza 1,6-bisfosfataza •

Kalcineurin • Fosfoproteinska fosfataza (PP2A) • OCRL • Piruvat dehidrogenazna fosfataza • Fruktoza 6-P,2-kinaza:fruktoza 2,6-bisfosfataza •PTEN • Fitaza • Inozitol-fosfat fosfataza (IMPA1)

Fosfoproteinska fosfataza: Proteinska tirozinska fosfataza • Proteinska serin/treoninska fosfataza • Fosfataza dualne-specifičnosti
3.1.4: Fosfodiesteraza
Autotaksin • Fosfolipaza (C, D) • Sfingomijelin fosfodiesteraza (1) • PDE1 • PDE2 • PDE3 • PDE4A/PDE4B • PDE5 • Lecitinaza (Clostridium perfringens alfa toksin) • Fosfodiesteraza cikličnih nukleotida
3.1.6: Sulfataza
arilsulfataza (Arilsulfataza A, Arilsulfataza B, Arilsulfataza E, Steroidna sulfataza) • Galaktozamine-6 sulfataza • Iduronat-2-sulfataza • N-acetilglukosamin-6-sulfataza
Nukleaza (obuhvata
deoksiribonukleazu i
ribonukleazu)
3.1.11-16: Eksonukleaza
Eksodeoksiribonukleaza
3.1.21-31: Endonukleaza
Endodeoksiribonukleaza
Deoksiribonukleaza I • Deoksiribonukleaza II • Deoksiribonukleaza IV • Restrikcioni enzim • UvrABC endonukleaza
Endoribonukleaza
RNaza III • RNaza H (1, 2A, 2B, 2C) • RNaza P • RNaza A (1, 2, 3, 4/5) • RNaza T1 • RNK-indukovani utišavajući kompleks
bilo dezoksi- ili ribo-
Aspergillus nukleaza S1 • Nukleaza mikrokoka
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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Separacija
i inicijacija
Prokariotska
(inicijacija)
Eukariotska
(priprema u
G1 fazi)
Oba
Replikacija
Prokariotska
(elongacija)
Eukariotska
(sinteza u
S fazi)
Oba
Kretanje: Procesivnost • DNK ligaza
Terminacija
B bsyn: dnk (repl, cycl, reco, repr) • tscr (fact, tcrg, nucl, rnat, rept, ptts) • tltn (risu, pttl, nexn) • dnab, rnab/runp • stru (domn, 1°, 2°, 3°, 4°)