RNASEH1

Ribonuclease H1 also known as RNase H1 is an enzyme that in humans is encoded by the RNASEH1 gene.[5][6][7] The RNase H1 is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism.

RNASEH1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2QK9, 2QKB, 2QKK, 3BSU
Identifiers
Aliases	RNASEH1, H1RNA, RNH1, PEOB2, ribonuclease H1
External IDs	OMIM: 604123 MGI: 1335073 HomoloGene: 2202 GeneCards: RNASEH1
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p25.3 Start 3,541,430 bp[1] End 3,558,333 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 A2 Start 28,649,602 bp[2] End 28,659,589 bp[2]
Gene ontology Molecular function • nuclease activity • endonuclease activity • RNA-DNA hybrid ribonuclease activity • ribonuclease activity • hydrolase activity • magnesium ion binding • metal ion binding • RNA binding • nucleic acid binding Cellular component • cytoplasm • cell nucleus Biological process • nucleic acid phosphodiester bond hydrolysis • RNA catabolic process • DNA replication, removal of RNA primer • RNA phosphodiester bond hydrolysis • RNA phosphodiester bond hydrolysis, endonucleolytic Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	246243	19819
Ensembl	ENSG00000171865	ENSMUSG00000020630
UniProt	O60930	E9QLN8
RefSeq (mRNA)	NM_001286834 NM_001286837 NM_002936 NM_001378271 NM_001378272 NM_001378273	NM_001286865 NM_011275
RefSeq (protein)	NP_001273763 NP_001273766 NP_002927 NP_001365200 NP_001365201 NP_001365202	NP_001273794 NP_035405
Location (UCSC)	Chr 2: 3.54 – 3.56 Mb	Chr 12: 28.65 – 28.66 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000171865 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020630 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: ribonuclease H1".
6. 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.
7. 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.

Further reading

• 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" (PDF). 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.

External links

• Overview of all the structural information available in the PDB for UniProt: O60930 (Human Ribonuclease H1 (RNASEH1)) at the PDBe-KB.