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T2 Family ribonucleases: ancient enzymes with diverse roles
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Ribonucleases of the T2 family are found in the genomes of protozoans, plants, bacteria, animals and viruses. A broad range of biological roles for these ribonucleases have been suggested, including scavenging of nucleic acids, degradation of self-RNA, serving as extra- or intracellular cytotoxins, and modulating host immune responses. Recently, RNaseT2 family members have been implicated in human pathologies such as cancer and parasitic diseases. Interestingly, certain functions of RNaseT2 family members are independent of their nuclease activity, suggesting that these proteins have additional functions. Moreover, humans lacking RNASET2 manifest a defect in neurological development, perhaps due to aberrant control of the immune system. We review the basic structure and function of RNaseT2 family members and their biological roles.
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Some T2 ribonucleases, for instance Erns from pestiviruses, can be secreted for degradation of RNA in extracellular spaces or in target cells.
“However, some T2 ribonucleases (for instance Erns from pestiviruses) can also be secreted (Luhtala and Parker, 2010), for degradation of RNA in extracellular spaces or in target cells”
From Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules (2018) · cites this paper as Luhtala and Parker, 2010
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Research works printed but not linked: 75
- Rosenberg, 2008, RNase A ribonucleases and host defense: an evolving story, J. Leukoc. Biol., 83, 1079, 10.1189/jlb.1107725 · DOI
- Deshpande, 2002, Ribonucleases from T2 family, Crit. Rev. Microbiol., 28, 79, 10.1080/1040-840291046704 · DOI
- Irie, 1999, Structure-function relationships of acid ribonucleases: lysosomal, vacuolar, and periplasmic enzymes, Pharmacol. Ther., 81, 77, 10.1016/S0163-7258(98)00035-7 · DOI
- Thompson, 2009, The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae, J. Cell. Biol., 185, 43, 10.1083/jcb.200811119 · DOI
- Goldraij, 2006, Compartmentalization of S-RNase and HT-B degradation in self-incompatible Nicotiana, Nature, 439, 805, 10.1038/nature04491 · DOI
- de Leeuw, 2007, Binding assay and preliminary X-ray crystallographic analysis of ACTIBIND, a protein with anticarcinogenic and antiangiogenic activities, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 63, 716, 10.1107/S1744309107034483 · DOI
- Ida, 2001, The 1.55Å resolution structure of Nicotiana alata S(F11)-RNase associated with gametophytic self-incompatibility, J. Mol. Biol., 314, 103, 10.1006/jmbi.2001.5127 · DOI
- Kawano, 2002, Guanine binding site of the Nicotiana glutinosa ribonuclease NW revealed by X-ray crystallography, Biochemistry, 41, 15195, 10.1021/bi026247l · DOI
- Kawano, 2006, Crystal structures of the Nicotiana glutinosa ribonuclease NT in complex with nucleoside monophosphates, J. Biochem., 140, 375, 10.1093/jb/mvj164 · DOI
- Kimura, 2004, Amino acids conserved at the C-terminal half of the ribonuclease T2 family contribute to protein stability of the enzymes, Biosci. Biotechnol. Biochem., 68, 1748, 10.1271/bbb.68.1748 · DOI
- Kobayashi, 1992, Primary structure of a base non-specific and adenylic acid preferential ribonuclease from the fruit bodies of Lentinus edodes, Biosci. Biotechnol. Biochem., 56, 2003, 10.1271/bbb.56.2003 · DOI
- Kurihara, 1992, Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus, FEBS Lett., 306, 189, 10.1016/0014-5793(92)80997-U · DOI
- Kurihara, 1996, The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0Å resolution, J. Mol. Biol., 255, 310, 10.1006/jmbi.1996.0025 · DOI
- Matsuura, 2001, Crystal structure at 1.5-Å resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility, J. Biol. Chem., 276, 45261, 10.1074/jbc.M107617200 · DOI
- Numata, 2003, Crystal structures of the ribonuclease MC1 mutants N71T and N71S in complex with 5′-GMP: structural basis for alterations in substrate specificity, Biochemistry, 42, 5270, 10.1021/bi034103g · DOI
- Padmanabhan, 2001, Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family, Arch. Biochem. Biophys., 390, 42, 10.1006/abbi.2001.2359 · DOI
- Rodriguez, 2008, Nonspecific base recognition mediated by water bridges and hydrophobic stacking in ribonuclease I from Escherichia coli, Protein Sci., 17, 681, 10.1110/ps.073420708 · DOI
- Suzuki, 2000, Crystal structures of the ribonuclease MC1 from bitter gourd seeds, complexed with 2′-UMP or 3′-UMP, reveal structural basis for uridine specificity, Biochem. Biophys. Res. Commun., 275, 572, 10.1006/bbrc.2000.3318 · DOI
- Tanaka, 2000, Crystal structure of a plant ribonuclease, RNase LE, J. Mol. Biol., 298, 859, 10.1006/jmbi.2000.3707 · DOI
- Nishikawa, 1987, Two histidine residues are essential for ribonuclease T1 activity as is the case for ribonuclease A, Biochemistry, 26, 8620, 10.1021/bi00400a019 · DOI
- Roberts, 1969, The mechanism of action of ribonuclease, Proc. Natl. Acad. Sci. U. S. A., 62, 1151, 10.1073/pnas.62.4.1151 · DOI
- Irie, 1986, Site of alkylation of the major ribonuclease from Aspergillus saitoi with iodoacetate, J. Biochem., 99, 627, 10.1093/oxfordjournals.jbchem.a135521 · DOI
- Kawata, 1990, Identification of two essential histidine residues of ribonuclease T2 from Aspergillus oryzae, Eur. J. Biochem., 187, 255, 10.1111/j.1432-1033.1990.tb15303.x · DOI
- Parry, 1997, Identification of active-site histidine residues of a self-incompatibility ribonuclease from a wild tomato, Plant Physiol., 115, 1421, 10.1104/pp.115.4.1421 · DOI
- Huang, 1994, Ribonuclease activity of Petunia inflata S proteins is essential for rejection of self-pollen, Plant Cell, 6, 1021, 10.1105/tpc.6.7.1021 · DOI
- Ohgi, 1992, Evidence that three histidine residues of a base non-specific and adenylic acid preferential ribonuclease from Rhizopus niveus are involved in the catalytic function, J. Biochem., 112, 132, 10.1093/oxfordjournals.jbchem.a123852 · DOI
- Numata, 2000, Expression and mutational analysis of amino acid residues involved in catalytic activity in a ribonuclease MC1 from the seeds of bitter gourd, Biosci. Biotechnol. Biochem., 64, 603, 10.1271/bbb.64.603 · DOI
- Royo, 1994, Loss of a histidine residue at the active site of S-locus ribonuclease is associated with self-compatibility in Lycopersicon peruvianum, Proc. Natl. Acad. Sci. U. S. A., 91, 6511, 10.1073/pnas.91.14.6511 · DOI
- Hulst, 1994, Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease, Virology, 200, 558, 10.1006/viro.1994.1218 · DOI
- Schneider, 1993, Identification of a structural glycoprotein of an RNA virus as a ribonuclease, Science, 261, 1169, 10.1126/science.8356450 · DOI
- Langedijk, 2002, Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop, J. Biol. Chem., 277, 5308, 10.1074/jbc.M104147200 · DOI
- Makarov, 2003, Cytotoxic ribonucleases: molecular weapons and their targets, FEBS Lett., 540, 15, 10.1016/S0014-5793(03)00225-4 · DOI
- Kobayashi, 2003, A new type of RNase T2 ribonuclease in two Basidiomycetes fungi, Lentinus edodes and Irpex lacteus, Biosci. Biotechnol. Biochem., 67, 2307, 10.1271/bbb.67.2307 · DOI
- MacIntosh, 2001, Characterization of Rny1, the Saccharomyces cerevisiae member of the T2 RNase family of RNases: unexpected functions for ancient enzymes?, Proc. Natl. Acad. Sci. U. S. A., 98, 1018, 10.1073/pnas.98.3.1018 · DOI
- Bariola, 1994, The Arabidopsis ribonuclease gene RNS1 is tightly controlled in response to phosphate limitation, Plant J., 6, 673, 10.1046/j.1365-313X.1994.6050673.x · DOI
- Taylor, 1993, RNS2: a senescence-associated RNase of Arabidopsis that diverged from the S-RNases before speciation, Proc. Natl. Acad. Sci. U. S. A., 90, 5118, 10.1073/pnas.90.11.5118 · DOI
- Loffler, 1992, Phosphate-regulated induction of intracellular ribonucleases in cultured tomato (Lycopersicon esculentum) cells, Plant Physiol., 98, 1472, 10.1104/pp.98.4.1472 · DOI
- Nurnberger, 1990, Induction of an extracellular ribonuclease in cultured tomato cells upon phosphate starvation, Plant Physiol., 92, 970, 10.1104/pp.92.4.970 · DOI
- Abel, 2000, Induction of an extracellular cyclic nucleotide phosphodiesterase as an accessory ribonucleolytic activity during phosphate starvation of cultured tomato cells, Plant Physiol., 122, 543, 10.1104/pp.122.2.543 · DOI
- McGugan, 2007, Identification and biochemical characterization of unique secretory nucleases of the human enteric pathogen, Entamoeba histolytica, J. Biol. Chem., 282, 31789, 10.1074/jbc.M705975200 · DOI
- Kirkin, 2009, A role for ubiquitin in selective autophagy, Mol. Cell, 34, 259, 10.1016/j.molcel.2009.04.026 · DOI
- Strome, 2007, Germ versus soma decisions: lessons from flies and worms, Science, 316, 392, 10.1126/science.1140846 · DOI
- Zhang, 2009, SEPA-1 mediates the specific recognition and degradation of P granule components by autophagy in C. elegans, Cell, 136, 308, 10.1016/j.cell.2008.12.022 · DOI
- Henneke, 2009, RNASET2-deficient cystic leukoencephalopathy resembles congenital cytomegalovirus brain infection, Nat. Genet., 41, 773, 10.1038/ng.398 · DOI
- Child, 2002, Complementation of vaccinia virus lacking the double-stranded RNA-binding protein gene E3L by human cytomegalovirus, J. Virol., 76, 4912, 10.1128/JVI.76.10.4912-4918.2002 · DOI
- Doenhoff, 1981, Immunological control of hepatotoxicity and parasite egg excretion in Schistosoma mansoni infections: stage specificity of the reactivity of immune serum in T-cell deprived mice, Trans. R. Soc. Trop. Med. Hyg., 75, 41, 10.1016/0035-9203(81)90012-2 · DOI
- Murare, 1992, Schistosoma mansoni: control of hepatotoxicity and egg excretion by immune serum in infected immunosuppressed mice is schistosome species-specific, but not S. mansoni strain-specific, Exp. Parasitol., 75, 329, 10.1016/0014-4894(92)90218-Y · DOI
- Pearce, 2005, Priming of the immune response by schistosome eggs, Parasite Immunol., 27, 265, 10.1111/j.1365-3024.2005.00765.x · DOI
- Everts, 2009, Omega-1, a glycoprotein secreted by Schistosoma mansoni eggs, drives Th2 responses, J. Exp. Med., 206, 1673, 10.1084/jem.20082460 · DOI
- Steinfelder, 2009, The major component in schistosome eggs responsible for conditioning dendritic cells for Th2 polarization is a T2 ribonuclease (omega-1), J. Exp. Med., 206, 1681, 10.1084/jem.20082462 · DOI
- Rumenapf, 1993, Processing of the envelope glycoproteins of pestiviruses, J. Virol., 67, 3288, 10.1128/JVI.67.6.3288-3294.1993 · DOI
- Bruschke, 1997, Glycoprotein Erns of pestiviruses induces apoptosis in lymphocytes of several species, J. Virol., 71, 6692, 10.1128/JVI.71.9.6692-6696.1997 · DOI
- Hulst, 1998, Inactivation of the RNase activity of glycoprotein E(rns) of classical swine fever virus results in a cytopathogenic virus, J. Virol., 72, 151, 10.1128/JVI.72.1.151-157.1998 · DOI
- Meyer, 2002, Recovery of virulent and RNase-negative attenuated type 2 bovine viral diarrhea viruses from infectious cDNA clones, J. Virol., 76, 8494, 10.1128/JVI.76.16.8494-8503.2002 · DOI
- Meyers, 1999, Mutations abrogating the RNase activity in glycoprotein E(rns) of the pestivirus classical swine fever virus lead to virus attenuation, J. Virol., 73, 10224, 10.1128/JVI.73.12.10224-10235.1999 · DOI
- von Freyburg, 2004, Comparison of the effects of RNase-negative and wild-type classical swine fever virus on peripheral blood cells of infected pigs, J. Gen. Virol., 85, 1899, 10.1099/vir.0.79988-0 · DOI
- McCubbin, 1997, A mutant S3 RNase of Petunia inflata lacking rnase activity has an allele-specific dominant negative effect on self-incompatibility interactions, Plant Cell, 9, 85, 10.1105/tpc.9.1.85 · DOI
- Murfett, 1996, S RNase and interspecific pollen rejection in the genus Nicotiana: multiple pollen-rejection pathways contribute to unilateral incompatibility between self-incompatible and self-compatible species, Plant Cell, 8, 943, 10.1105/tpc.8.6.943 · DOI
- Anderson, 1986, Cloning of cDNA for a stylar glycoprotein associated with expression of self-incompatibility in Nicotiana alata, Nature, 321, 38, 10.1038/321038a0 · DOI
- Jahnen, 1989, Identification, isolation, and N-terminal sequencing of style glycoproteins associated with self-incompatibility in Nicotiana alata, Plant Cell, 1, 493, 10.1105/tpc.1.5.493 · DOI
- Luu, 2000, S-RNase uptake by compatible pollen tubes in gametophytic self-incompatibility, Nature, 407, 649, 10.1038/35036623 · DOI
- McClure, 1990, Self-incompatibility in Nicotiana alata involves degradation of pollen rRNA, Nature, 347, 757, 10.1038/347757a0 · DOI
- McClure, 2006, Gametophytic self-incompatibility: understanding the cellular mechanisms involved in “self” pollen tube inhibition, Planta, 224, 233, 10.1007/s00425-006-0284-2 · DOI
- Sijacic, 2004, Identification of the pollen determinant of S-RNase-mediated self-incompatibility, Nature, 429, 302, 10.1038/nature02523 · DOI
- Ushijima, 2004, The S haplotype-specific F-box protein gene, SFB, is defective in self-compatible haplotypes of Prunus avium and P. mume, Plant J, 39, 573, 10.1111/j.1365-313X.2004.02154.x · DOI
- Qiao, 2004, The F-box protein AhSLF-S2 physically interacts with S-RNases that may be inhibited by the ubiquitin/26S proteasome pathway of protein degradation during compatible pollination in Antirrhinum, Plant Cell, 16, 582, 10.1105/tpc.017673 · DOI
- Thompson, 2008, tRNA cleavage is a conserved response to oxidative stress in eukaryotes, RNA, 14, 2095, 10.1261/rna.1232808 · DOI
- Campomenosi, 2006, Characterization of RNASET2, the first human member of the Rh/T2/S family of glycoproteins, Arch. Biochem. Biophys., 449, 17, 10.1016/j.abb.2006.02.022 · DOI
- Acquati, 2001, Cloning and characterization of a senescence inducing and class II tumor suppressor gene in ovarian carcinoma at chromosome region 6q27, Oncogene, 20, 980, 10.1038/sj.onc.1204178 · DOI
- Liu, 2002, Physical and transcript map of the region between D6S264 and D6S149 on chromosome 6q27, the minimal region of allele loss in sporadic epithelial ovarian cancer, Oncogene, 21, 387, 10.1038/sj.onc.1205067 · DOI
- Acquati, 2005, Tumor and metastasis suppression by the human RNASET2 gene, Int. J. Oncol., 26, 1159
- Smirnoff, 2006, A recombinant human RNASET2 glycoprotein with antitumorigenic and antiangiogenic characteristics: expression, purification, and characterization, Cancer, 107, 2760, 10.1002/cncr.22327 · DOI
- Roiz, 2006, ACTIBIND, an actin-binding fungal T2-RNase with antiangiogenic and anticarcinogenic characteristics, Cancer, 106, 2295, 10.1002/cncr.21878 · DOI
- Schwartz, 2007, ACTIBIND, a T2 RNase, competes with angiogenin and inhibits human melanoma growth, angiogenesis, and metastasis, Cancer Res., 67, 5258, 10.1158/0008-5472.CAN-07-0129 · DOI
- Gray, 1991, Action of the style product of the self-incompatibility gene of Nicotiana alata (S-RNase) on in vitro-grown pollen tubes, Plant Cell, 3, 271, 10.1105/tpc.3.3.271 · DOI
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Sorted by citations
Modulation of Host Immunity by Helminths: The Expanding Repertoire of Parasite Effector Molecules
Maizels, R. M., Smits, H. H., & McSorley, H. J. (2018) · Immunity · doi:10.1016/j.immuni.2018.10.016 · Cited by 435
Metadata
- Authors
- Luhtala, N., & Parker, R.
- Affiliations
- University of Arizona (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Parker, Roy
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 35
- Issue
- 5
- Pages
- 253-259
- ISSN
- 0968-0004 (ISSN-L)
- PMC
- PMC2888479
- OpenAlex
- W2072667721
- Cited by
- 247
- References
- 0
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 21 · 2023: 16 · 2022: 21 · 2021: 23 · 2020: 21 · 2019: 15 · 2018: 18 · 2017: 14 · 2016: 17 · 2015: 11 · 2014: 8 · 2013: 7 · 2012: 12
- FWCI
- 1.01
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (T32CA009213, P30CA023074)
- National Institute of General Medical Sciences (R37GM045443)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- RNASET2, RNA degradation, cytotoxin, immunomodulation, cancer, parasitic infection, brain development, protein structure-function relationship
- MeSH terms
- Animals, Bacteria, Endoribonucleases, Humans, Neoplasms, Plants, Proteins, Ribonucleases, Viruses, Genome
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