Back رناز هتش Arabic Ribonukleasen H German Ribonucleasa H Spanish Ribonucléase H French Ribonuclease H Galician リボヌクレアーゼH Japanese Ribonuklease H Malay Ribonuclease H Portuguese Рибонуклеаза H Russian Ribonukleaza H telećeg timusa Serbo-Croatian
| ribonuclease H | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.1.26.4 | ||||||||
| CAS no. | 9050-76-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| retroviral ribonuclease H | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.1.26.13 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Ribonuclease H (abbreviated RNase H or RNH) is a family of non-sequence-specific endonuclease enzymes that catalyze the cleavage of RNA in an RNA/DNA substrate via a hydrolytic mechanism. Members of the RNase H family can be found in nearly all organisms, from bacteria to archaea to eukaryotes.
The family is divided into evolutionarily related groups with slightly different substrate preferences, broadly designated ribonuclease H1 and H2.[2] The human genome encodes both H1 and H2. Human ribonuclease H2 is a heterotrimeric complex composed of three subunits, mutations in any of which are among the genetic causes of a rare disease known as Aicardi–Goutières syndrome.[3] A third type, closely related to H2, is found only in a few prokaryotes,[4] whereas H1 and H2 occur in all domains of life.[4] Additionally, RNase H1-like retroviral ribonuclease H domains occur in multidomain reverse transcriptase proteins, which are encoded by retroviruses such as HIV and are required for viral replication.[5][6]
In eukaryotes, ribonuclease H1 is involved in DNA replication of the mitochondrial genome. Both H1 and H2 are involved in genome maintenance tasks such as processing of R-loop structures.[2][7]
- ^ PDB: 1JL1; Goedken ER, Marqusee S (December 2001). "Native-state energetics of a thermostabilized variant of ribonuclease HI". Journal of Molecular Biology. 314 (4): 863–71. doi:10.1006/jmbi.2001.5184. PMID 11734003.
- ^ a b Cerritelli SM, Crouch RJ (March 2009). "Ribonuclease H: the enzymes in eukaryotes". The FEBS Journal. 276 (6): 1494–505. doi:10.1111/j.1742-4658.2009.06908.x. PMC 2746905. PMID 19228196.
- ^ Cite error: The named reference
crow_2006was invoked but never defined (see the help page). - ^ a b Figiel M, Nowotny M (August 2014). "Crystal structure of RNase H3-substrate complex reveals parallel evolution of RNA/DNA hybrid recognition". Nucleic Acids Research. 42 (14): 9285–94. doi:10.1093/nar/gku615. PMC 4132731. PMID 25016521.
- ^ Davies JF, Hostomska Z, Hostomsky Z, Jordan SR, Matthews DA (April 1991). "Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase". Science. 252 (5002): 88–95. Bibcode:1991Sci...252...88D. doi:10.1126/science.1707186. PMID 1707186.
- ^ Hansen J, Schulze T, Mellert W, Moelling K (January 1988). "Identification and characterization of HIV-specific RNase H by monoclonal antibody". The EMBO Journal. 7 (1): 239–43. doi:10.1002/j.1460-2075.1988.tb02805.x. PMC 454263. PMID 2452083.
- ^ Cite error: The named reference
tadokoro_2009was invoked but never defined (see the help page).
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