| RNase H1 facilitates recombinase recruitment by degrading DNA-RNA hybrids during meiosis. | RNase H1 facilitates recombinase recruitment by degrading DNA-RNA hybrids during meiosis.
Liu C, Wang L, Li Y, Guo M, Hu J, Wang T, Li M, Yang Z, Lin R, Xu W, Chen Y, Luo M, Gao F, Chen JY, Sun Q, Liu H, Sun B, Li W., Free PMC Article | 08/16/2023 |
| A pan-cancer analysis of RNASEH1, a potential regulator of the tumor microenvironment. | A pan-cancer analysis of RNASEH1, a potential regulator of the tumor microenvironment.
Yi C, Yang J, Zhang T, Xie S, Li W, Qin L, Chen D. | 06/28/2023 |
| BRCA2 deficiency reveals that oxidative stress impairs RNaseH1 function to cripple mitochondrial DNA maintenance. | BRCA2 deficiency reveals that oxidative stress impairs RNaseH1 function to cripple mitochondrial DNA maintenance.
Renaudin X, Lee M, Shehata M, Surmann EM, Venkitaraman AR., Free PMC Article | 02/12/2022 |
| A non-coding RNASEH1 gene variant associates with type 1 diabetes and interacts with HLA tagSNPs in families from Colombia. | A non-coding RNASEH1 gene variant associates with type 1 diabetes and interacts with HLA tagSNPs in families from Colombia.
Gomez-Lopera N, Alfaro JM, Rodriguez AM, Ramirez A, Leal SM, Pineda-Trujillo N. | 11/22/2021 |
| Progressive External Ophthalmoplegia in Polish Patients-From Clinical Evaluation to Genetic Confirmation. | Progressive External Ophthalmoplegia in Polish Patients-From Clinical Evaluation to Genetic Confirmation.
Kierdaszuk B, Kaliszewska M, Rusecka J, Kosińska J, Bartnik E, Tońska K, Kamińska AM, Kostera-Pruszczyk A., Free PMC Article | 07/24/2021 |
| The protein-protein interaction between P54nrb and RNase H1 requires the spacer region of RNAse H1, while the P54nrb core domains are required for association with RNase H1. | Kinetic and subcellular analysis of PS-ASO/protein interactions with P54nrb and RNase H1.
Vickers TA, Rahdar M, Prakash TP, Crooke ST., Free PMC Article | 05/16/2020 |
| A second nuclease is therefore required to remove the last ribonucleotides and we demonstrate that Flap endonuclease 1 (FEN1) can execute this function in vitro. Removal of RNA primers at OriL thus depends on a two-nuclease model, which in addition to RNase H1 requires FEN1 or a FEN1-like activity. These findings define the role of RNase H1 at OriL and help to explain the pathogenic consequences of disease causing mutatio | A two-nuclease pathway involving RNase H1 is required for primer removal at human mitochondrial OriL.
Al-Behadili A, Uhler JP, Berglund AK, Peter B, Doimo M, Reyes A, Wanrooij S, Zeviani M, Falkenberg M., Free PMC Article | 06/29/2019 |
| In combination with previously published in vivo data, the findings presented here suggest a model, in which R-loop processing by RNase H1 directs origin-specific initiation of DNA replication in human mitochondria. | RNase H1 directs origin-specific initiation of DNA replication in human mitochondria.
Posse V, Al-Behadili A, Uhler JP, Clausen AR, Reyes A, Zeviani M, Falkenberg M, Gustafsson CM., Free PMC Article | 03/16/2019 |
| RNASEH1 gene variants associate with susceptibility/protection to T1 Diabetes in Colombia. | RNASEH1 gene variants are associated with autoimmune type 1 diabetes in Colombia.
Pineda-Trujillo N, Rodríguez-Acevedo A, Rodríguez A, Ruíz-Linares A, Bedoya G, Rivera A, Alfaro JM. | 10/27/2018 |
| Studies indicate that ribonuclease H1 is essential for mitochondrial DNA replication. | Pathological ribonuclease H1 causes R-loop depletion and aberrant DNA segregation in mitochondria.
Akman G, Desai R, Bailey LJ, Yasukawa T, Dalla Rosa I, Durigon R, Holmes JB, Moss CF, Mennuni M, Houlden H, Crouch RJ, Hanna MG, Pitceathly RD, Spinazzola A, Holt IJ., Free PMC Article | 02/10/2018 |
| Data show that the catalytic domains of E. coli and human RNase H have nearly identical sequence preferences, which correlate with the efficiency of RNase H-recruiting antisense oligonucleotides. | RNase H sequence preferences influence antisense oligonucleotide efficiency.
Kielpinski LJ, Hagedorn PH, Lindow M, Vinther J., Free PMC Article | 01/20/2018 |
| Data suggest that ribonuclease H1 (RNASEH1) plays important role in replication fork movement by resolving R-loops (RNA-DNA hybrids); RNASEH1 depletion results in accumulation of RNA-DNA hybrids, slowing of replication forks, and increased DNA damage; RNASEH1 appears to contribute to genome stability and preserves telomere integrity. | Human ribonuclease H1 resolves R-loops and thereby enables progression of the DNA replication fork.
Parajuli S, Teasley DC, Murali B, Jackson J, Vindigni A, Stewart SA., Free PMC Article | 09/30/2017 |
| RPA is a sensor of R loops and a regulator of RNaseH1, extending the versatile role of RPA in suppression of genomic instability. | Functions of Replication Protein A as a Sensor of R Loops and a Regulator of RNaseH1.
Nguyen HD, Yadav T, Giri S, Saez B, Graubert TA, Zou L., Free PMC Article | 09/9/2017 |
| RNaseH1 maintains regulated levels of telomeric RNA-DNA hybrids at ALT telomeres to trigger homologous recombination without compromising telomere integrity too severely | RNaseH1 regulates TERRA-telomeric DNA hybrids and telomere maintenance in ALT tumour cells.
Arora R, Lee Y, Wischnewski H, Brun CM, Schwarz T, Azzalin CM., Free PMC Article | 02/27/2016 |
| found that the 3' fragments of target pre-mRNA generated by ASO were almost completely degraded from their 5' ends by nuclear XRN2 after RNase H1-mediated cleavage | XRN2 is required for the degradation of target RNAs by RNase H1-dependent antisense oligonucleotides.
Hori S, Yamamoto T, Obika S. | 11/21/2015 |
| Altered RNaseH1 has a reduced capability to remove the RNA from RNA-DNA hybrids leading to impaired mtDNA replication and adult-onset mitochondrial encephalomyopathy. | RNASEH1 Mutations Impair mtDNA Replication and Cause Adult-Onset Mitochondrial Encephalomyopathy.
Reyes A, Melchionda L, Nasca A, Carrara F, Lamantea E, Zanolini A, Lamperti C, Fang M, Zhang J, Ronchi D, Bonato S, Fagiolari G, Moggio M, Ghezzi D, Zeviani M., Free PMC Article | 09/26/2015 |
| RNase H1 and protein P32 are involved in mitochondrial pre-rRNA processing | Human RNase H1 is associated with protein P32 and is involved in mitochondrial pre-rRNA processing.
Wu H, Sun H, Liang X, Lima WF, Crooke ST., Free PMC Article | 04/26/2014 |
| data implicate the H264 side chain in phosphodiester hydrolysis as well as in product release, and are consistent with a proposed model in which the RNAse H1 H264 side chain interacts with a divalent metal ion to support catalysis | Evidence for a dual functional role of a conserved histidine in RNA·DNA heteroduplex cleavage by human RNase H1.
Alla NR, Nicholson AW., Free PMC Article | 02/9/2013 |
| On the basis of its nuclear magnetic resonance (NMR) nucleic acid structure, a boranophosphonate-modified, fully R(P) BH(3) DNA/RNA hybrid is predicted not to be a substrate for RNase H1. | Structural basis of the RNase H1 activity on stereo regular borano phosphonate DNA/RNA hybrids.
Johnson CN, Spring AM, Sergueev D, Shaw BR, Germann MW., Free PMC Article | 08/6/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article | 12/5/2010 |
| Characterization of full-length enzymes with defective hybrid binding domain indicates that this domain dramatically enhances both the specific activity and processivity of RNase H1. | Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.
Nowotny M, Cerritelli SM, Ghirlando R, Gaidamakov SA, Crouch RJ, Yang W., Free PMC Article | 01/21/2010 |
| Report crystal structures of RNase H1 in complex with RNA/DNA hybrids. | Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription.
Nowotny M, Gaidamakov SA, Ghirlando R, Cerritelli SM, Crouch RJ, Yang W. | 01/21/2010 |
| THE role substrate structure plays in directing human RNase H1 activity as well as the design of effective antisense oligodeoxyribonucleotides. | Human RNase H1 discriminates between subtle variations in the structure of the heteroduplex substrate.
Lima WF, Rose JB, Nichols JG, Wu H, Migawa MT, Wyrzykiewicz TK, Siwkowski AM, Crooke ST. | 01/21/2010 |
| method for enhancing the human RNase H1 activity of chimeric antisense oligonucleotides | The positional influence of the helical geometry of the heteroduplex substrate on human RNase H1 catalysis.
Lima WF, Rose JB, Nichols JG, Wu H, Migawa MT, Wyrzykiewicz TK, Vasquez G, Swayze EE, Crooke ST. | 01/21/2010 |
| in human cells RNase H1 is responsible for most of the activity of DNA-like antisense drugs | Determination of the role of the human RNase H1 in the pharmacology of DNA-like antisense drugs.
Wu H, Lima WF, Zhang H, Fan A, Sun H, Crooke ST. | 01/21/2010 |