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Journal articles on the topic 'RNases H'

Author: Grafiati

Published: 4 May 2024

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1

Allen, S. J. W., S. H. Krawczyk, L. R. McGee, N. Bischofberger, A. S. Mulato, and J. M. Cherrington. "Inhibition of HIV-1 RNase H Activity by Nucleotide Dimers and Monomers." Antiviral Chemistry and Chemotherapy 7, no. 1 (1996): 37–45. http://dx.doi.org/10.1177/095632029600700107.

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Nucleotide dimers and monomers were shown to inhibit human immunodeficiency virus type 1 (HIV) RNase H activity. Several effective inhibitors were identified and placed into three general groups based on biochemical characterization of their inhibition, The first group (group A) inhibited HIV RNase H and the closely related feline immunodeficiency virus (FIV) RNase H, but did not inhibit less related retroviral or cellular RNases H or HIV reverse transcriptase (RT). The second group (group B) inhibited the RNase H activity of several retroviruses as well as the reverse transcriptase function o

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2

Leich, Franziska, Nadine Stöhr, Anne Rietz, Renate Ulbrich-Hofmann, and Ulrich Arnold. "Endocytotic Internalization as a Crucial Factor for the Cytotoxicity of Ribonucleases." Journal of Biological Chemistry 282, no. 38 (2007): 27640–46. http://dx.doi.org/10.1074/jbc.m702240200.

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The cytotoxic action of ribonucleases (RNases) requires the interaction of the enzyme with the cellular membrane, its internalization, translocation to the cytosol, and the degradation of ribonucleic acid. The interplay of these processes as well as the role of the thermodynamic and proteolytic stability, the catalytic activity, and the evasion from the intracellular ribonuclease inhibitor (RI) has not yet been fully elucidated. As cytosolic internalization is indispensable for the cytotoxicity of extracellular ribonucleases, we investigated the extent of cytosolic internalization of a cytotox

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3

Watkins, Harriet A., and Edward N. Baker. "Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis." Journal of Bacteriology 192, no. 11 (2010): 2878–86. http://dx.doi.org/10.1128/jb.01615-09.

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ABSTRACT The open reading frame Rv2228c from Mycobacterium tuberculosis is predicted to encode a protein composed of two domains, each with individual functions, annotated through sequence similarity searches. The N-terminal domain is homologous with prokaryotic and eukaryotic RNase H domains and the C-terminal domain with α-ribazole phosphatase (CobC). The N-terminal domain of Rv2228c (Rv2228c/N) and the full-length protein were expressed as fusions with maltose binding protein (MBP). Rv2228c/N was shown to have RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase

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4

Ohtani, Naoto, Mitsuru Haruki, Masaaki Morikawa, and Shigenori Kanaya. "Molecular diversities of RNases H." Journal of Bioscience and Bioengineering 88, no. 1 (1999): 12–19. http://dx.doi.org/10.1016/s1389-1723(99)80168-6.

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5

Hyjek, Malwina, Małgorzata Figiel, and Marcin Nowotny. "RNases H: Structure and mechanism." DNA Repair 84 (December 2019): 102672. http://dx.doi.org/10.1016/j.dnarep.2019.102672.

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6

Goulian, Mehran, and Cheryl J. Heard. "Discrimination between mammalian RNases H-1 and H-2." Analytical Biochemistry 192, no. 2 (1991): 398–402. http://dx.doi.org/10.1016/0003-2697(91)90555-8.

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7

Lim, Shion A., Kathryn M. Hart, Michael J. Harms, and Susan Marqusee. "Evolutionary trend toward kinetic stability in the folding trajectory of RNases H." Proceedings of the National Academy of Sciences 113, no. 46 (2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.

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Proper folding of proteins is critical to producing the biological machinery essential for cellular function. The rates and energetics of a protein’s folding process, which is described by its energy landscape, are encoded in the amino acid sequence. Over the course of evolution, this landscape must be maintained such that the protein folds and remains folded over a biologically relevant time scale. How exactly a protein’s energy landscape is maintained or altered throughout evolution is unclear. To study how a protein’s energy landscape changed over time, we characterized the folding trajecto

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8

Hiller, Bjoern, Martin Achleitner, Silke Glage, Ronald Naumann, Rayk Behrendt, and Axel Roers. "Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity." Journal of Experimental Medicine 209, no. 8 (2012): 1419–26. http://dx.doi.org/10.1084/jem.20120876.

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Ribonucleases H (RNases H) are endonucleases which cleave the RNA moiety of RNA/DNA hybrids. Their function in mammalian cells is incompletely understood. RNase H2 mutations cause Aicardi-Goutières syndrome, an inflammatory condition clinically overlapping with lupus erythematosus. We show that RNase H2 is essential in mouse embryonic development. RNase H2–deficient cells proliferated slower than control cells and accumulated in G2/M phase due to chronic activation of a DNA damage response associated with an increased frequency of single-strand breaks, increased histone H2AX phosphorylation, a

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9

Kirby, Karen A., Bruno Marchand, Yee Tsuey Ong, et al. "Structural and Inhibition Studies of the RNase H Function of Xenotropic Murine Leukemia Virus-Related Virus Reverse Transcriptase." Antimicrobial Agents and Chemotherapy 56, no. 4 (2012): 2048–61. http://dx.doi.org/10.1128/aac.06000-11.

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ABSTRACTRNase H inhibitors (RNHIs) have gained attention as potential HIV-1 therapeutics. Although several RNHIs have been studied in the context of HIV-1 reverse transcriptase (RT) RNase H, there is no information on inhibitors that might affect the RNase H activity of other RTs. We performed biochemical, virological, crystallographic, and molecular modeling studies to compare the RNase H function and inhibition profiles of the gammaretroviral xenotropic murine leukemia virus-related virus (XMRV) and Moloney murine leukemia virus (MoMLV) RTs to those of HIV-1 RT. The RNase H activity of XMRV

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10

Cerritelli, Susana M., and Robert J. Crouch. "RNases H: Multiple roles in maintaining genome integrity." DNA Repair 84 (December 2019): 102742. http://dx.doi.org/10.1016/j.dnarep.2019.102742.

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11

OHTANI, Naoto, Hiroshi YANAGAWA, Masaru TOMITA, and Mitsuhiro ITAYA. "Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: archaeal RNase HI can cleave an RNA–DNA junction." Biochemical Journal 381, no. 3 (2004): 795–802. http://dx.doi.org/10.1042/bj20040153.

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All the archaeal genomes sequenced to date contain a single Type 2 RNase H gene. We found that the genome of a halophilic archaeon, Halobacterium sp. NRC-1, contains an open reading frame with similarity to Type 1 RNase H. The protein encoded by the Vng0255c gene, possessed amino acid sequence identities of 33% with Escherichia coli RNase HI and 34% with a Bacillus subtilis RNase HI homologue. The B. subtilis RNase HI homologue, however, lacks amino acid sequences corresponding to a basic protrusion region of the E. coli RNase HI, and the Vng0255c has the similar deletion. As this deletion app

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12

Stafford, Kate A., and Arthur G. Palmer III. "Evidence from molecular dynamics simulations of conformational preorganization in the ribonuclease H active site." F1000Research 3 (March 7, 2014): 67. http://dx.doi.org/10.12688/f1000research.3605.1.

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Ribonuclease H1 (RNase H) enzymes are well-conserved endonucleases that are present in all domains of life and are particularly important in the life cycle of retroviruses as domains within reverse transcriptase. Despite extensive study, especially of the E. coli homolog, the interaction of the highly negatively charged active site with catalytically required magnesium ions remains poorly understood. In this work, we describe molecular dynamics simulations of the E. coli homolog in complex with magnesium ions, as well as simulations of other homologs in their apo states. Collectively, these re

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13

Schultz, Sharon J., Miaohua Zhang, and James J. Champoux. "Recognition of Internal Cleavage Sites by Retroviral RNases H." Journal of Molecular Biology 344, no. 3 (2004): 635–52. http://dx.doi.org/10.1016/j.jmb.2004.09.081.

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14

Ohtani, Naoto, Masaru Tomita, and Mitsuhiro Itaya. "Junction ribonuclease: a ribonuclease HII orthologue from Thermus thermophilus HB8 prefers the RNA–DNA junction to the RNA/DNA heteroduplex." Biochemical Journal 412, no. 3 (2008): 517–26. http://dx.doi.org/10.1042/bj20080140.

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The genome of an extremely thermophilic bacterium, Thermus thermophilus HB8, contains a single ORF (open reading frame) encoding an RNase-HII-like sequence. Despite the presence of significant amino acid sequence identities with RNase (ribonuclease) HII enzymes, the ORF TTHA0198 could not suppress the temperature-sensitive growth defect of an RNase-H-deficient Escherichia coli mutant and the purified recombinant protein could not cleave an RNA strand of an RNA/DNA heteroduplex, suggesting that the TTHA0198 exhibited no RNase H activity both in vivo and in vitro. When oligomeric RNA–DNA/DNAs we

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15

Lim, David, G. Glenn Gregorio, Craig Bingman, Erik Martinez-Hackert, Wayne A. Hendrickson, and Stephen P. Goff. "Crystal Structure of the Moloney Murine Leukemia Virus RNase H Domain." Journal of Virology 80, no. 17 (2006): 8379–89. http://dx.doi.org/10.1128/jvi.00750-06.

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ABSTRACT A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (ΔC). The 1.6-Å resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge

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16

Zimmer, Anjali D., and Douglas Koshland. "Differential roles of the RNases H in preventing chromosome instability." Proceedings of the National Academy of Sciences 113, no. 43 (2016): 12220–25. http://dx.doi.org/10.1073/pnas.1613448113.

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DNA:RNA hybrids can lead to DNA damage and genome instability. This damage can be prevented by degradation of the RNA in the hybrid by two evolutionarily conserved enzymes, RNase H1 and H2. Indeed, RNase H-deficient cells have increased chromosomal rearrangements. However, the quantitative and spatial contributions of the individual enzymes to hybrid removal have been unclear. Additionally, RNase H2 can remove single ribonucleotides misincorporated into DNA during replication. The relative contribution of DNA:RNA hybrids and misincorporated ribonucleotides to chromosome instability also was un

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17

Good-Avila, S. V., D. Majumder, H. Amos, and A. G. Stephenson. "Characterization of self-incompatibility in Campanula rapunculoides (Campanulaceae) through genetic analyses and microscopy." Botany 86, no. 1 (2008): 1–13. http://dx.doi.org/10.1139/b07-100.

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In this paper, we seek to identify the genetic basis of self-incompatibility (SI) in Campanula rapunculoides L. through diallel analysis of full siblings; to characterize the growth of pollen tubes in vivo after incompatible and compatible pollination; and to determine whether the SI system is based on pistil S-RNases. Pollinations were performed among individuals from five diallel crosses and scored for both fruit set and pollen-tube growth to determine the genetic basis of SI. On a subset of these individuals with known cross-(in)compatibility relationships, additional crosses were performed

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18

Nowotny, Marcin, Sergei Gaidamakov, Robert J. Crouch, and Wei Yang. "Structural studies of RNases H and their complexes with RNA/DNA hybrids." Acta Crystallographica Section A Foundations of Crystallography 65, a1 (2009): s138. http://dx.doi.org/10.1107/s0108767309097232.

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19

Ohtani, Naoto, Mitsuru Haruki, Masaaki Morikawa, Robert J. Crouch, Mitsuhiro Itaya, and Shigenori Kanaya. "Identification of the Genes Encoding Mn2+-Dependent RNase HII and Mg2+-Dependent RNase HIII fromBacillus subtilis: Classification of RNases H into Three Families†." Biochemistry 38, no. 2 (1999): 605–18. http://dx.doi.org/10.1021/bi982207z.

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20

An Lim, Shion, Kathryn M. Hart, Michael J. Harms, and Susan Marqusee. "An Evolutionary Trend towards Kinetic Stability in the Folding Trajectory of RNases H." Biophysical Journal 112, no. 3 (2017): 59a—60a. http://dx.doi.org/10.1016/j.bpj.2016.11.359.

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21

Permanasari, Etin-Diah, Kiyoshi Yasukawa, and Shigenori Kanaya. "Enzymatic Activities of RNase H Domains of HIV-1 Reverse Transcriptase with Substrate Binding Domains of Bacterial RNases H1 and H2." Molecular Biotechnology 57, no. 6 (2015): 526–38. http://dx.doi.org/10.1007/s12033-015-9846-5.

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22

Hafkemeyer, Peter, Klaus Neftel, Reinhard Hobi, et al. "HP 0.35, a cephalosporin degradation product is a specific inhibitor of lentiviral RNAses H." Nucleic Acids Research 19, no. 15 (1991): 4059–65. http://dx.doi.org/10.1093/nar/19.15.4059.

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23

Rosen, Laura E., and Susan Marqusee. "Autonomously Folding Protein Fragments Reveal Differences in the Energy Landscapes of Homologous RNases H." PLOS ONE 10, no. 3 (2015): e0119640. http://dx.doi.org/10.1371/journal.pone.0119640.

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24

Staroseletz, Yaroslav, Svetlana Gaponova, Olga Patutina, et al. "Site-Selective Artificial Ribonucleases: Renaissance of Oligonucleotide Conjugates for Irreversible Cleavage of RNA Sequences." Molecules 26, no. 6 (2021): 1732. http://dx.doi.org/10.3390/molecules26061732.

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RNA-targeting therapeutics require highly efficient sequence-specific devices capable of RNA irreversible degradation in vivo. The most developed methods of sequence-specific RNA cleavage, such as siRNA or antisense oligonucleotides (ASO), are currently based on recruitment of either intracellular multi-protein complexes or enzymes, leaving alternative approaches (e.g., ribozymes and DNAzymes) far behind. Recently, site-selective artificial ribonucleases combining the oligonucleotide recognition motifs (or their structural analogues) and catalytically active groups in a single molecular scaffo

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25

Smith, Robert M., Cherie M. Walton, Catherine H. Wu, and George Y. Wu. "Secondary Structure and Hybridization Accessibility of Hepatitis C Virus 3′-Terminal Sequences." Journal of Virology 76, no. 19 (2002): 9563–74. http://dx.doi.org/10.1128/jvi.76.19.9563-9574.2002.

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ABSTRACT The 3′-terminal sequences of hepatitis C virus (HCV) positive- and negative-strand RNAs contribute cis-acting functions essential for viral replication. The secondary structure and protein-binding properties of these highly conserved regions are of interest not only for the further elucidation of HCV molecular biology, but also for the design of antisense therapeutic constructs. The RNA structure of the positive-strand 3′ untranslated region has been shown previously to influence binding by various host and viral proteins and is thus thought to promote HCV RNA synthesis and genome sta

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Schultz, Sharon J., Miaohua Zhang, and James J. Champoux. "Sequence, Distance, and Accessibility Are Determinants of 5′-End-directed Cleavages by Retroviral RNases H." Journal of Biological Chemistry 281, no. 4 (2005): 1943–55. http://dx.doi.org/10.1074/jbc.m510504200.

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27

Shen, Ying, Kyung Duk Koh, Bernard Weiss, and Francesca Storici. "Mispaired rNMPs in DNA are mutagenic and are targets of mismatch repair and RNases H." Nature Structural & Molecular Biology 19, no. 1 (2011): 98–104. http://dx.doi.org/10.1038/nsmb.2176.

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28

Meng, Wenzhao, and Allen W. Nicholson. "Heterodimer-based analysis of subunit and domain contributions to double-stranded RNA processing by Escherichia coli RNase III in vitro." Biochemical Journal 410, no. 1 (2008): 39–48. http://dx.doi.org/10.1042/bj20071047.

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Members of the RNase III family are the primary cellular agents of dsRNA (double-stranded RNA) processing. Bacterial RNases III function as homodimers and contain two dsRBDs (dsRNA-binding domains) and two catalytic sites. The potential for functional cross-talk between the catalytic sites and the requirement for both dsRBDs for processing activity are not known. It is shown that an Escherichia coli RNase III heterodimer that contains a single functional wt (wild-type) catalytic site and an inactive catalytic site (RNase III[E117A/wt]) cleaves a substrate with a single scissile bond with a kca

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Li, Chang, Mengqi Lu, Junqin Zhou, et al. "Transcriptome Analysis of the Late-Acting Self-Incompatibility Associated with RNase T2 Family in Camellia oleifera." Plants 12, no. 10 (2023): 1932. http://dx.doi.org/10.3390/plants12101932.

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The Camellia oil tree (Camellia oleifera Abel.) is an important nonwood forest species in China, and the majority of its cultivars are late-acting self-incompatibility (LSI) types. Although several studies have examined the mechanism of LSI, the process is quite complicated and unclear. In this study, pollen tube growth and fruit setting of two Camellia oil tree cultivars Huashuo (HS) and Huajin (HJ) were investigated after non and self-pollination, and transcriptomic analysis of the ovaries was performed 48 h after self-pollination to identify the potential genes implicated in the LSI of Came

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30

Schultz, Sharon J., Miaohua Zhang, and James J. Champoux. "Multiple Nucleotide Preferences Determine Cleavage-Site Recognition by the HIV-1 and M-MuLV RNases H." Journal of Molecular Biology 397, no. 1 (2010): 161–78. http://dx.doi.org/10.1016/j.jmb.2010.01.059.

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31

Schultz, Sharon J., Miaohua Zhang, and James J. Champoux. "Preferred Sequences within a Defined Cleavage Window Specify DNA 3′ End-directed Cleavages by Retroviral RNases H." Journal of Biological Chemistry 284, no. 47 (2009): 32225–38. http://dx.doi.org/10.1074/jbc.m109.043158.

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32

Gugliotti, Lina A., Kiran B. Sakhuja, Hongsheng Wang, et al. "Constitutive Lymphoid Expression of the Nuclear Form of RNase H1 Is Associated with a Developmental Bottleneck at the Pro-B Cell Stage of B Cell Differentiation." Blood 114, no. 22 (2009): 4702. http://dx.doi.org/10.1182/blood.v114.22.4702.4702.

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Abstract Abstract 4702 The development of B lymphocytes and the process of lineage determination are initiated by expression of a set of transcriptional regulators leading to V(D)J recombination events initiated by double-strand DNA breaks. Subsequently, these recombinations form DNAs that permit transcription of immunoglobulin genes and translation of the corresponding mRNAs, first by joining the V(D)J DNA sequences, then by recombination, that generates various isotypes of immunoglobulins by class-switch recombination (CSR). Formation of R-loops, regions containing RNA/DNA hybrid and a displ

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33

Guo, Yan, Jie Wu, Shilin Zhao, et al. "RNA Sequencing of Formalin-Fixed, Paraffin-Embedded Specimens for Gene Expression Quantification and Data Mining." International Journal of Genomics 2016 (2016): 1–10. http://dx.doi.org/10.1155/2016/9837310.

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Background. Proper rRNA depletion is crucial for the successful utilization of FFPE specimens when studying gene expression. We performed a study to evaluate two major rRNA depletion methods: Ribo-Zero and RNase H. RNAs extracted from 4 samples were treated with the two rRNA depletion methods in duplicate and sequenced (N=16). We evaluated their reducibility, ability to detect RNA, and ability to molecularly subtype these triple negative breast cancer specimens.Results. Both rRNA depletion methods produced consistent data between the technical replicates. We found that the RNase H method produ

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Morris, Shannon, and Jonathan Leis. "Changes in Rous Sarcoma Virus RNA Secondary Structure near the Primer Binding Site upon tRNATrpPrimer Annealing." Journal of Virology 73, no. 8 (1999): 6307–18. http://dx.doi.org/10.1128/jvi.73.8.6307-6318.1999.

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ABSTRACT Predicted secondary-structure elements encompassing the primer binding site in the 5′ untranslated region of Rous sarcoma virus (RSV) RNA play an integral role in multiple viral replications steps including reverse transcription, DNA integration, and RNA packaging (A. Aiyar, D. Cobrinik, Z. Ge, H. J. Kung, and J. Leis, J. Virol. 66:2464–2472, 1992; D. Cobrinik, A. Aiyar, Z. Ge, M. Katzman, H. Huang, and J. Leis, J. Virol. 65:3864–3872, 1991; J. T. Miller, Z. Ge, S. Morris, K. Das, and J. Leis, J. Virol. 71:7648–7656, 1997). These elements include the U5-Leader stem, U5-IR stem-loop, a

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Dharap, Ashuthosh, Kellie Bowen, Robert Place, Long-Cheng Li, and Raghu Vemuganti. "Transient Focal Ischemia Induces Extensive Temporal Changes in Rat Cerebral MicroRNAome." Journal of Cerebral Blood Flow & Metabolism 29, no. 4 (2009): 675–87. http://dx.doi.org/10.1038/jcbfm.2008.157.

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MicroRNAs (miRNAs) are ∼22 nucleotides long, noncoding RNAs that control cellular function by either degrading mRNAs or arresting their translation. To understand their functional significance in ischemic pathophysiology, we profiled miRNAs in adult rat brain as a function of reperfusion time after transient middle cerebral artery occlusion. Of the 238 miRNAs evaluated, 8 showed increased and 12 showed decreased expression at least at 4 out of 5 reperfusion time points studied between 3 h and 3 days compared with sham. Of those, 17 showed > 5 fold change. Bioinformatics analysis indicated a

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Gruber, Cornelia, Torsten Gursinsky, Selma Gago-Zachert, Vitantonio Pantaleo, and Sven-Erik Behrens. "Effective Antiviral Application of Antisense in Plants by Exploiting Accessible Sites in the Target RNA." International Journal of Molecular Sciences 24, no. 24 (2023): 17153. http://dx.doi.org/10.3390/ijms242417153.

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Antisense oligodeoxynucleotides (ASOs) have long been used to selectively inhibit or modulate gene expression at the RNA level, and some ASOs are approved for clinical use. However, the practicability of antisense technologies remains limited by the difficulty of reliably predicting the sites accessible to ASOs in complex folded RNAs. Recently, we applied a plant-based method that reproduces RNA-induced RNA silencing in vitro to reliably identify sites in target RNAs that are accessible to small interfering RNA (siRNA)-guided Argonaute endonucleases. Here, we show that this method is also suit

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Lu, Gaofeng, Elena Lomonosova, Xiaohong Cheng, et al. "Hydroxylated Tropolones Inhibit Hepatitis B Virus Replication by Blocking Viral Ribonuclease H Activity." Antimicrobial Agents and Chemotherapy 59, no. 2 (2014): 1070–79. http://dx.doi.org/10.1128/aac.04617-14.

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ABSTRACTHepatitis B virus (HBV) remains a major human pathogen despite the development of both antiviral drugs and a vaccine, in part because the current therapies do not suppress HBV replication far enough to eradicate the virus. Here, we screened 51 troponoid compounds for their ability to suppress HBV RNaseH activity and HBV replication based on the activities of α-hydroxytropolones against HIV RNaseH, with the goal of determining whether the tropolone pharmacophore may be a promising scaffold for anti-HBV drug development. Thirteen compounds inhibited HBV RNaseH, with the best 50% inhibito

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Arudchandran, Arulvathani, Susana Cerritelli, Scott Narimatsu, et al. "The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: implications for roles of RNases H in DNA replication and repair." Genes to Cells 5, no. 10 (2000): 789–802. http://dx.doi.org/10.1046/j.1365-2443.2000.00373.x.

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39

Sharma, Vasudha, Prachi Thakore, and Sharmistha Majumdar. "THAP9 Transposase Cleaves DNA via Conserved Acidic Residues in an RNaseH-Like Domain." Cells 10, no. 6 (2021): 1351. http://dx.doi.org/10.3390/cells10061351.

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The catalytic domain of most ‘cut and paste’ DNA transposases have the canonical RNase-H fold, which is also shared by other polynucleotidyl transferases such as the retroviral integrases and the RAG1 subunit of V(D)J recombinase. The RNase-H fold is a mixture of beta sheets and alpha helices with three acidic residues (Asp, Asp, Glu/Asp—DDE/D) that are involved in the metal-mediated cleavage and subsequent integration of DNA. Human THAP9 (hTHAP9), homologous to the well-studied Drosophila P-element transposase (DmTNP), is an active DNA transposase that, although domesticated, still retains th

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Corona, Angela, Anna Schneider, Kristian Schweimer, Paul Rösch, Birgitta M. Wöhrl, and Enzo Tramontano. "Inhibition of Foamy Virus Reverse Transcriptase by Human Immunodeficiency Virus Type 1 RNase H Inhibitors." Antimicrobial Agents and Chemotherapy 58, no. 7 (2014): 4086–93. http://dx.doi.org/10.1128/aac.00056-14.

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ABSTRACTRNase H plays an essential role in the replication of human immunodeficiency virus type 1 (HIV-1). Therefore, it is a promising target for drug development. However, the identification of HIV-1 RNase H inhibitors (RHIs) has been hampered by the open morphology of its active site, the limited number of available RNase H crystal structures in complex with inhibitors, and the fact that, due to the high concentrations of Mg2+needed for protein stability, HIV-1 RNase H is not suitable for nuclear magnetic resonance (NMR) inhibitor studies. We recently showed that the RNase H domains of HIV-

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Corona, Angela, Francesco Saverio Di Leva, Sylvain Thierry, et al. "Identification of Highly Conserved Residues Involved in Inhibition of HIV-1 RNase H Function by Diketo Acid Derivatives." Antimicrobial Agents and Chemotherapy 58, no. 10 (2014): 6101–10. http://dx.doi.org/10.1128/aac.03605-14.

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ABSTRACTHIV-1 reverse transcriptase (RT)-associated RNase H activity is an essential function in viral genome retrotranscription. RNase H is a promising drug target for which no inhibitor is available for therapy. Diketo acid (DKA) derivatives are active site Mg2+-binding inhibitors of both HIV-1 RNase H and integrase (IN) activities. To investigate the DKA binding site of RNase H and the mechanism of action, six couples of ester and acid DKAs, derived from 6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester (RDS1643), were synthesized and tested on both RNase H

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Wang, Yafang, Namin Hu, Chang Liu, et al. "An RNase H-powered DNA walking machine for sensitive detection of RNase H and the screening of related inhibitors." Nanoscale 12, no. 3 (2020): 1673–79. http://dx.doi.org/10.1039/c9nr07550j.

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Delviks-Frankenberry, Krista A., Galina N. Nikolenko, Rebekah Barr, and Vinay K. Pathak. "Mutations in Human Immunodeficiency Virus Type 1 RNase H Primer Grip Enhance 3′-Azido-3′-Deoxythymidine Resistance." Journal of Virology 81, no. 13 (2007): 6837–45. http://dx.doi.org/10.1128/jvi.02820-06.

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ABSTRACT We recently observed that mutations in the human immunodeficiency type 1 (HIV-1) reverse transcriptase (RT) connection domain significantly increase 3′-azido-3′-deoxythymidine (AZT) resistance up to 536 times over wild-type (WT) RT in the presence of thymidine analog resistance mutations (TAMs). These mutations also decreased RT template switching, suggesting that they altered the balance between nucleotide excision and template RNA degradation, which in turn increased AZT resistance. Several residues in the HIV-1 connection domain contact the primer strand and form an RNase H primer

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Lee, Hyunjee, HyeokJin Cho, Jooyoung Kim, et al. "RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids." Nucleic Acids Research 50, no. 4 (2021): 1801–14. http://dx.doi.org/10.1093/nar/gkab1064.

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Abstract RNase H is involved in fundamental cellular processes and is responsible for removing the short stretch of RNA from Okazaki fragments and the long stretch of RNA from R-loops. Defects in RNase H lead to embryo lethality in mice and Aicardi-Goutieres syndrome in humans, suggesting the importance of RNase H. To date, RNase H is known to be a non-sequence-specific endonuclease, but it is not known whether it performs other functions on the structural variants of RNA:DNA hybrids. Here, we used Escherichia coli RNase H as a model, and examined its catalytic mechanism and its substrate reco

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Farias, Richard V., Deborah A. Vargas, Andres E. Castillo, et al. "Expression of an Mg2+-Dependent HIV-1 RNase H Construct for Drug Screening." Antimicrobial Agents and Chemotherapy 55, no. 10 (2011): 4735–41. http://dx.doi.org/10.1128/aac.00658-11.

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ABSTRACTA single polypeptide of the HIV-1 reverse transcriptase that reconstituted Mg2+-dependent RNase H activity has been made. Using molecular modeling, the construct was designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66. This p51-G-TCR construct was purified from the soluble fraction of anEscherichia colistrain, MIC2067(DE3), lacking endogenous RNase HI and HII. The p51-G-TCR RNase H construct displayed Mg2+-dependent activity using a fluorescent nonspecific assay and showed the same cleavage pattern as HIV-1 reverse tran

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Brincat, Jennifer L., Julie K. Pfeiffer, and Alice Telesnitsky. "RNase H Activity Is Required for High-Frequency Repeat Deletion during Moloney Murine Leukemia Virus Replication." Journal of Virology 76, no. 1 (2002): 88–95. http://dx.doi.org/10.1128/jvi.76.1.88-95.2002.

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ABSTRACT It has been postulated that retroviral recombination, like strong stop template switching, requires the RNase H activity of reverse transcriptase. To address this hypothesis, Moloney murine leukemia virus-based vectors, which were designed to test the recombination-related property of direct repeat deletion, were encapsidated in virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant reverse transcriptase. Integrated provirus titers per milliliter were determined for these phenotypically mixed virions, and vector proviruses were screened

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Keck, James L., Eric R. Goedken, and Susan Marqusee. "Activation/Attenuation Model for RNase H." Journal of Biological Chemistry 273, no. 51 (1998): 34128–33. http://dx.doi.org/10.1074/jbc.273.51.34128.

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Krakowiak, Agnieszka, Alina Owczarek, Maria Koziołkiewicz, and Wojciech J. Stec. "Stereochemical Course ofEscherichia coli RNase H." ChemBioChem 3, no. 12 (2002): 1242–50. http://dx.doi.org/10.1002/1439-7633(20021202)3:12<1242::aid-cbic1242>3.0.co;2-y.

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Su, Hua-Poo, Youwei Yan, G. Sridhar Prasad, et al. "Structural Basis for the Inhibition of RNase H Activity of HIV-1 Reverse Transcriptase by RNase H Active Site-Directed Inhibitors." Journal of Virology 84, no. 15 (2010): 7625–33. http://dx.doi.org/10.1128/jvi.00353-10.

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ABSTRACT HIV/AIDS continues to be a menace to public health. Several drugs currently on the market have successfully improved the ability to manage the viral burden in infected patients. However, new drugs are needed to combat the rapid emergence of mutated forms of the virus that are resistant to existing therapies. Currently, approved drugs target three of the four major enzyme activities encoded by the virus that are critical to the HIV life cycle. Although a number of inhibitors of HIV RNase H activity have been reported, few inhibit by directly engaging the RNase H active site. Here, we d

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Corona, Angela, Valentina Onnis, Claudia Del Vecchio, Francesca Esposito, Yung-Chi Cheng, and Enzo Tramontano. "2-(Arylamino)-6-(trifluoromethyl)nicotinic Acid Derivatives: New HIV-1 RT Dual Inhibitors Active on Viral Replication." Molecules 25, no. 6 (2020): 1338. http://dx.doi.org/10.3390/molecules25061338.

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The persistence of the AIDS epidemic, and the life-long treatment required, indicate the constant need of novel HIV-1 inhibitors. In this scenario the HIV-1 Reverse Transcriptase (RT)-associated ribonuclease H (RNase H) function is a promising drug target. Here we report a series of compounds, developed on the 2-amino-6-(trifluoromethyl)nicotinic acid scaffold, studied as promising RNase H dual inhibitors. Among the 44 tested compounds, 34 inhibited HIV-1 RT-associated RNase H function in the low micromolar range, and seven of them showed also to inhibit viral replication in cell-based assays

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