RNASEH1

Available structures

Human UniProt search: PDBe RCSB

List of PDB id codes
2QK9, 2QKB, 2QKK, 3BSU

Identifiers

Aliases

RNASEH1, H1RNA, RNH1, PEOB2, ribonuclease H1

External IDs

MGI: 1335073 HomoloGene: 2202 GeneCards: RNASEH1

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
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


n/a

RefSeq (mRNA)


NM_001286834 NM_001286837 NM_002936


NM_001286865 NM_011275

RefSeq (protein)


NP_001273763.1 NP_001273766.1 NP_002927.2


n/a

Location (UCSC)

Chr 2: 3.54 – 3.56 Mb

Chr 12: 28.65 – 28.66 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Ribonuclease H1 also known as RNase H1 is an enzyme that in humans is encoded by the RNASEH1 gene.^[3]^[4]^[5] The RNase H1 is a non-specific endonuclease and catalyzes the cleavage of RNA via a hydrolytic mechanism.

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: ribonuclease H1".
↑ 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.
↑ 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.

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.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

DNA replication (comparing Prokaryotic to Eukaryotic)

Initiation

Prokaryotic (initiation)	Pre-replication complex dnaC Cdc6 Helicase dnaA dnaB T7 Primase dnaG

Eukaryotic (preparation in G1 phase)	Pre-replication complex Origin recognition complex ORC1 ORC2 ORC3 ORC4 ORC5 ORC6 Cdc6 Cdt1 Minichromosome maintenance MCM2 MCM3 MCM4 MCM5 MCM6 MCM7 Licensing factor Autonomously replicating sequence Single-strand binding protein SSBP2 SSBP3 SSBP4 RNase H RNASEH1 RNASEH2A Helicase: HFM1 Primase: PRIM1 PRIM2

Both	Origin of replication/Ori/Replicon Replication fork Lagging and leading strands Okazaki fragments Primer

Replication

Prokaryotic (elongation)	DNA polymerase III holoenzyme dnaC dnaE dnaH dnaN dnaQ dnaT dnaX holA holB holC holD holE Replisome DNA ligase DNA clamp Topoisomerase DNA gyrase Prokaryotic DNA polymerase: DNA polymerase I Klenow fragment

Eukaryotic (synthesis in S phase)	Replication factor C RFC1 Flap endonuclease FEN1 Topoisomerase Replication protein A RPA1 Eukaryotic DNA polymerase: alpha POLA1 POLA2 PRIM1 PRIM2 delta POLD1 POLD2 POLD3 POLD4 epsilon POLE POLE2 POLE3 POLE4 DNA clamp PCNA Control of chromosome duplication

Both	Movement: Processivity DNA ligase

Termination

Telomere: Telomerase
- TERT
- TERC
- DKC1

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RNASEH1

References

Further reading