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Journal articles on the topic 'Ribonuclease III'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Lorenc-Kubis, Irena, and Bronisława Morawiecka. "Preliminary studies on ribonucleases from Poa pratensis seeds." Acta Societatis Botanicorum Poloniae 43, no. 4 (2015): 471–78. http://dx.doi.org/10.5586/asbp.1974.044.

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Ribonuclease was extracted from <i>Poa pratensis</i> seeds with 0.1 M acetate buffer, pH 5.1, and then precipitated with alcohol. The enzyme was separated into 5 fractions (I-V) after chromatography on DEAE-cellulose at pH 5.1. The enzymes were stable at 50°C, at pH 7.1. The activity of ribonucleases I, II, III and V were optimal at pH 7.1-7.3, and that of ribonuclease IV at pH 8.1. Ali enzymes were inhibited by Ca<sup>2+</sup> and EDTA. Mg<sup>2+</sup> inhibited the activity of ribonucleases II, III, IV, and had no influence on that of ribonucleases I and V. Ribonucleases IV and V showed only one activity band in disc electrophoresis, whereas ribonucleases, I, II and III were found to be heterogenous.

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2

MacRae, Ian J., and Jennifer A. Doudna. "Ribonuclease revisited: structural insights into ribonuclease III family enzymes." Current Opinion in Structural Biology 17, no. 1 (February 2007): 138–45. http://dx.doi.org/10.1016/j.sbi.2006.12.002.

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3

Conrad, Christian, and Reinhard Rauhut. "Ribonuclease III: new sense from nuisance." International Journal of Biochemistry & Cell Biology 34, no. 2 (February 2002): 116–29. http://dx.doi.org/10.1016/s1357-2725(01)00112-1.

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4

Wu, Chang-Xian, Xian-Jin Xu, Ke Zheng, Fang Liu, Xu-Dong Yang, Chuang-Fu Chen, Huan-Chun Chen, and Zheng-Fei Liu. "Characterization of ribonuclease III from Brucella." Gene 579, no. 2 (April 2016): 183–92. http://dx.doi.org/10.1016/j.gene.2015.12.068.

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5

Ji, Xinhua. "Ruler-based mechanisms of ribonuclease III enzymes." Acta Crystallographica Section A Foundations and Advances 73, a1 (May 26, 2017): a5. http://dx.doi.org/10.1107/s0108767317099949.

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6

Chelladurai, Bhadrani, Honglin Li, Kejing Zhang, and Allen W. Nicholson. "Mutational analysis of a ribonuclease III processing signal." Biochemistry 32, no. 29 (July 1993): 7549–58. http://dx.doi.org/10.1021/bi00080a029.

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7

Franch, Thomas, Thomas Thisted, and Kenn Gerdes. "Ribonuclease III Processing of Coaxially Stacked RNA Helices." Journal of Biological Chemistry 274, no. 37 (September 10, 1999): 26572–78. http://dx.doi.org/10.1074/jbc.274.37.26572.

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8

Nicholson, Allen W. "Ribonuclease III mechanisms of double-stranded RNA cleavage." Wiley Interdisciplinary Reviews: RNA 5, no. 1 (September 30, 2013): 31–48. http://dx.doi.org/10.1002/wrna.1195.

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9

Schweisguth, David C., Bhadrani S. Chelladurai, Allen W. Nicholson, and Peter B. Moore. "Structural characterization of a ribonuclease III processing signal." Nucleic Acids Research 22, no. 4 (1994): 604–12. http://dx.doi.org/10.1093/nar/22.4.604.

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10

Fanning, Ann-Marie, Sally E. Plush, and Thorfinnur Gunnlaugsson. "Tri- and tetra-substituted cyclen based lanthanide(iii) ion complexes as ribonuclease mimics: a study into the effect of log Ka, hydration and hydrophobicity on phosphodiester hydrolysis of the RNA-model 2-hydroxypropyl-4-nitrophenyl phosphate (HPNP)." Organic & Biomolecular Chemistry 13, no. 20 (2015): 5804–16. http://dx.doi.org/10.1039/c4ob02384f.

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11

DE GREGORIO, Eliana, Chiara ABRESCIA, M. Stella CARLOMAGNO, and Pier Paolo DI NOCERA. "Ribonuclease III-mediated processing of specific Neisseria meningitidis mRNAs." Biochemical Journal 374, no. 3 (September 15, 2003): 799–805. http://dx.doi.org/10.1042/bj20030533.

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Approx. 2% of the Neisseria meningitidis genome consists of small DNA insertion sequences known as Correia or nemis elements, which feature TIRs (terminal inverted repeats) of 26–27 bp in length. Elements interspersed with coding regions are co-transcribed with flanking genes into mRNAs, processed at double-stranded RNA structures formed by TIRs. N. meningitidis RNase III (endoribonuclease III) is sufficient to process nemis+ RNAs. RNA hairpins formed by nemis with the same termini (26/26 and 27/27 repeats) are cleaved. By contrast, bulged hairpins formed by 26/27 repeats inhibit cleavage, both in vitro and in vivo. In electrophoretic mobility shift assays, all hairpin types formed similar retarded complexes upon incubation with RNase III. The levels of corresponding nemis+ and nemis− mRNAs, and the relative stabilities of RNA segments processed from nemis+ transcripts in vitro, may both vary significantly.

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12

Blaszczyk, Jaroslaw, Jianhua Gan, Joseph E. Tropea, Donald L. Court, David S. Waugh, and Xinhua Ji. "Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA." Structure 12, no. 3 (March 2004): 457–66. http://dx.doi.org/10.1016/j.str.2004.02.004.

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13

March, Paul E., and Monica A. Gonzalez. "Characterization of the biochemical properties of recombinant ribonuclease III." Nucleic Acids Research 18, no. 11 (1990): 3293–98. http://dx.doi.org/10.1093/nar/18.11.3293.

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14

Samolygo, Aleksei, Januka S. Athukoralage, Shirley Graham, and Malcolm F. White. "Fuse to defuse: a self-limiting ribonuclease-ring nuclease fusion for type III CRISPR defence." Nucleic Acids Research 48, no. 11 (April 29, 2020): 6149–56. http://dx.doi.org/10.1093/nar/gkaa298.

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Abstract Type III CRISPR systems synthesise cyclic oligoadenylate (cOA) second messengers in response to viral infection of bacteria and archaea, potentiating an immune response by binding and activating ancillary effector nucleases such as Csx1. As these effectors are not specific for invading nucleic acids, a prolonged activation can result in cell dormancy or death. Some archaeal species encode a specialised ring nuclease enzyme (Crn1) to degrade cyclic tetra-adenylate (cA4) and deactivate the ancillary nucleases. Some archaeal viruses and bacteriophage encode a potent ring nuclease anti-CRISPR, AcrIII-1, to rapidly degrade cA4 and neutralise immunity. Homologues of this enzyme (named Crn2) exist in type III CRISPR systems but are uncharacterised. Here we describe an unusual fusion between cA4-activated CRISPR ribonuclease (Csx1) and a cA4-degrading ring nuclease (Crn2) from Marinitoga piezophila. The protein has two binding sites that compete for the cA4 ligand, a canonical cA4-activated ribonuclease activity in the Csx1 domain and a potent cA4 ring nuclease activity in the C-terminal Crn2 domain. The cA4 binding affinities and activities of the two constituent enzymes in the fusion protein may have evolved to ensure a robust but time-limited cOA-activated ribonuclease activity that is finely tuned to cA4 levels as a second messenger of infection.

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15

Zhang, Yuanzheng, Irina Calin-Jageman, James R. Gurnon, Tae-Jin Choi, Byron Adams, Allen W. Nicholson, and James L. Van Etten. "Characterization of a chlorella virus PBCV-1 encoded ribonuclease III." Virology 317, no. 1 (December 2003): 73–83. http://dx.doi.org/10.1016/j.virol.2003.08.044.

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16

Zhang, K., and A. W. Nicholson. "Regulation of ribonuclease III processing by double-helical sequence antideterminants." Proceedings of the National Academy of Sciences 94, no. 25 (December 9, 1997): 13437–41. http://dx.doi.org/10.1073/pnas.94.25.13437.

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17

Srivastava, Neelam, and Rai Ajit Srivastava. "Expression, purification and properties of recombinant E. coli ribonuclease III." IUBMB Life 39, no. 1 (May 1996): 171–80. http://dx.doi.org/10.1080/15216549600201171.

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18

Maruyama, Tatsuo, Saori Sonokawa, Hironari Matsushita, and Masahiro Goto. "Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease." Journal of Inorganic Biochemistry 101, no. 1 (January 2007): 180–86. http://dx.doi.org/10.1016/j.jinorgbio.2006.09.021.

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19

Gan, Jianhua, Joseph E. Tropea, Brian P. Austin, Donald L. Court, David S. Waugh, and Xinhua Ji. "Intermediate States of Ribonuclease III in Complex with Double-Stranded RNA." Structure 13, no. 10 (October 2005): 1435–42. http://dx.doi.org/10.1016/j.str.2005.06.014.

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20

Ji, Xinhua. "Structural basis for non-catalytic and catalytic activities of ribonuclease III." Acta Crystallographica Section D Biological Crystallography 62, no. 8 (July 18, 2006): 933–40. http://dx.doi.org/10.1107/s090744490601153x.

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21

Gan, Jianhua, Gary Shaw, Joseph E. Tropea, David S. Waugh, Donald L. Court, and Xinhua Ji. "A stepwise model for double-stranded RNA processing by ribonuclease III." Molecular Microbiology 67, no. 1 (November 29, 2007): 143–54. http://dx.doi.org/10.1111/j.1365-2958.2007.06032.x.

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22

Davidov, Yael, Guri Zivion, and Ophry Pines. "Ribonuclease III reduces the efficiency of bacteriophage gy1 propagation inE. coli." Current Microbiology 24, no. 2 (February 1992): 63–66. http://dx.doi.org/10.1007/bf01570899.

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23

Athukoralage, Januka S., Shirley Graham, Sabine Grüschow, Christophe Rouillon, and Malcolm F. White. "A Type III CRISPR Ancillary Ribonuclease Degrades Its Cyclic Oligoadenylate Activator." Journal of Molecular Biology 431, no. 15 (July 2019): 2894–99. http://dx.doi.org/10.1016/j.jmb.2019.04.041.

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24

Viegas, Sandra C., Dalila Mil-Homens, Arsénio M. Fialho, and Cecília M. Arraiano. "The Virulence of Salmonella enterica Serovar Typhimurium in the Insect Model Galleria mellonella Is Impaired by Mutations in RNase E and RNase III." Applied and Environmental Microbiology 79, no. 19 (August 2, 2013): 6124–33. http://dx.doi.org/10.1128/aem.02044-13.

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ABSTRACTSalmonella entericaserovar Typhimurium is a Gram-negative bacterium able to invade and replicate inside eukaryotic cells. To cope with the host defense mechanisms, the bacterium has to rapidly remodel its transcriptional status. Regulatory RNAs and ribonucleases are the factors that ultimately control the fate of mRNAs and final protein levels in the cell. There is growing evidence of the direct involvement of these factors in bacterial pathogenicity. In this report, we validate the use of aGalleria mellonelamodel inS. Typhimurium pathogenicity studies through the parallel analysis of a mutant with a mutation inhfq, a well-establishedSalmonellavirulence gene. The results obtained with this mutant are similar to the ones reported in a mouse model. Through the use of this insect model, we demonstrate a role for the main endoribonucleases RNase E and RNase III inSalmonellavirulence. These ribonuclease mutants show an attenuated virulence phenotype, impairment in motility, and reduced proliferation inside the host. Interestingly, the two mutants trigger a distinct immune response in the host, and the two mutations seem to have an impact on distinct bacterial functions.

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25

Cho, Soo Jung, Kyoung Sook Hong, Ji Hun Jeong, Mihye Lee, Augustine M. K. Choi, Heather W. Stout-Delgado, and Jong-Seok Moon. "DROSHA-Dependent AIM2 Inflammasome Activation Contributes to Lung Inflammation during Idiopathic Pulmonary Fibrosis." Cells 8, no. 8 (August 20, 2019): 938. http://dx.doi.org/10.3390/cells8080938.

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Idiopathic pulmonary fibrosis (IPF) has been linked to chronic lung inflammation. Drosha ribonuclease III (DROSHA), a class 2 ribonuclease III enzyme, plays a key role in microRNA (miRNA) biogenesis. However, the mechanisms by which DROSHA affects the lung inflammation during idiopathic pulmonary fibrosis (IPF) remain unclear. Here, we demonstrate that DROSHA regulates the absent in melanoma 2 (AIM2) inflammasome activation during idiopathic pulmonary fibrosis (IPF). Both DROSHA and AIM2 protein expression were elevated in alveolar macrophages of patients with IPF. We also found that DROSHA and AIM2 protein expression were increased in alveolar macrophages of lung tissues in a mouse model of bleomycin-induced pulmonary fibrosis. DROSHA deficiency suppressed AIM2 inflammasome-dependent caspase-1 activation and interleukin (IL)-1β and IL-18 secretion in primary mouse alveolar macrophages and bone marrow-derived macrophages (BMDMs). Transduction of microRNA (miRNA) increased the formation of the adaptor apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) specks, which is required for AIM2 inflammasome activation in BMDMs. Our results suggest that DROSHA promotes AIM2 inflammasome activation-dependent lung inflammation during IPF.

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26

Nashimoto, Hiroko, and Hisao Uchida. "DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations." Molecular and General Genetics MGG 201, no. 1 (September 1985): 25–29. http://dx.doi.org/10.1007/bf00397981.

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27

Zamore, Phillip D. "Thirty-Three Years Later, a Glimpse at the Ribonuclease III Active Site." Molecular Cell 8, no. 6 (December 2001): 1158–60. http://dx.doi.org/10.1016/s1097-2765(01)00418-x.

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28

Akey, David L., and James M. Berger. "Structure of the nuclease domain of ribonuclease III fromM. tuberculosisat 2.1 Å." Protein Science 14, no. 10 (October 2005): 2744–50. http://dx.doi.org/10.1110/ps.051665905.

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29

Hotto, Amber M., Benoît Castandet, Laetitia Gilet, Andrea Higdon, Ciarán Condon, and David B. Stern. "Arabidopsis Chloroplast Mini-Ribonuclease III Participates in rRNA Maturation and Intron Recycling." Plant Cell 27, no. 3 (February 27, 2015): 724–40. http://dx.doi.org/10.1105/tpc.114.134452.

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30

March, Paul E., Joohong Ahnn, and Masayori Inouye. "The DNA sequence of the gene (rnc) encoding ribonuclease III ofEscherichia coli." Nucleic Acids Research 13, no. 13 (1985): 4677–85. http://dx.doi.org/10.1093/nar/13.13.4677.

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31

Calin-Jageman, I. "Ethidium-dependent uncoupling of substrate binding and cleavage by Escherichia coli ribonuclease III." Nucleic Acids Research 29, no. 9 (May 1, 2001): 1915–25. http://dx.doi.org/10.1093/nar/29.9.1915.

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32

Kim, K. s., R. Manasherob, and S. N. Cohen. "YmdB: a stress-responsive ribonuclease-binding regulator of E. coli RNase III activity." Genes & Development 22, no. 24 (December 15, 2008): 3497–508. http://dx.doi.org/10.1101/gad.1729508.

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33

Ji, X., J. Blaszczyk, J. E. Tropea, M. Bubunenko, K. M. Routzahn, D. S. Waugh, and D. L. Court. "Compound active center of ribonuclease III: molecular basis for double-stranded RNA cleavage." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c306. http://dx.doi.org/10.1107/s0108767302097222.

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34

Gan, Jianhua, Joseph E. Tropea, Brian P. Austin, Donald L. Court, David S. Waugh, and Xinhua Ji. "Structural Insight into the Mechanism of Double-Stranded RNA Processing by Ribonuclease III." Cell 124, no. 2 (January 2006): 355–66. http://dx.doi.org/10.1016/j.cell.2005.11.034.

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35

Tong, Xiaohui, Nianjun Yu, Rongchun Han, and Tongsheng Wang. "Function of Dicer with regard to Energy Homeostasis Regulation, Structural Modification, and Cellular Distribution." International Journal of Endocrinology 2020 (July 25, 2020): 1–7. http://dx.doi.org/10.1155/2020/6420816.

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As a type III ribonuclease (RNase III) specifically cleaving double-stranded RNA substrates into short fragments, Dicer is indispensable in a range of physi/pathologic processes, e.g., nutrient deprivation, hypoxia, or DNA damage. Therefore, much interest has been paid to the research of this protein as well as its products like microRNAs (miRNAs). The close relationship between Dicer levels and fluctuations of nutrient availability suggests that the protein participates in the regulation of systemic energy homeostasis. Through miRNAs, Dicer regulates the hypothalamic melanocortin-4 system and central autophagy promoting energy expenditure. Moreover, by influencing canonical energy sensors like adenosine monophosphate-activated protein kinase (AMPK) or mammalian target of rapamycin (mTOR), Dicer favors catabolism in the periphery. Taken together, Dicer might be targeted in the control of energy dysregulation. However, factors affecting its RNase activity should be noted. Firstly, modulation of structural integrity affects its role as a ribonuclease. Secondly, although previously known as a cytosolic endoribonuclease, evidence suggests Dicer can relocalize into the nucleus where it could also produce small RNAs. In this review, we probe into involvement of Dicer in energy homeostasis as well as its structural integrity or cellular distribution which affects its ability to produce miRNAs, in the hope of providing novel insights into its mechanism of action for future application.

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36

Cánovas-Márquez, José Tomás, Sebastian Falk, Francisco E. Nicolás, Subramanian Padmanabhan, Rubén Zapata-Pérez, Álvaro Sánchez-Ferrer, Eusebio Navarro, and Victoriano Garre. "A ribonuclease III involved in virulence of Mucorales fungi has evolved to cut exclusively single-stranded RNA." Nucleic Acids Research 49, no. 9 (April 20, 2021): 5294–307. http://dx.doi.org/10.1093/nar/gkab238.

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Abstract Members of the ribonuclease III (RNase III) family regulate gene expression by processing double-stranded RNA (dsRNA). This family includes eukaryotic Dicer and Drosha enzymes that generate small dsRNAs in the RNA interference (RNAi) pathway. The fungus Mucor lusitanicus, which causes the deadly infection mucormycosis, has a complex RNAi system encompassing a non-canonical RNAi pathway (NCRIP) that regulates virulence by degrading specific mRNAs. In this pathway, Dicer function is replaced by R3B2, an atypical class I RNase III, and small single-stranded RNAs (ssRNAs) are produced instead of small dsRNA as Dicer-dependent RNAi pathways. Here, we show that R3B2 forms a homodimer that binds to ssRNA and dsRNA molecules, but exclusively cuts ssRNA, in contrast to all known RNase III. The dsRNA cleavage inability stems from its unusual RNase III domain (RIIID) because its replacement by a canonical RIIID allows dsRNA processing. A crystal structure of R3B2 RIIID resembles canonical RIIIDs, despite the low sequence conservation. However, the groove that accommodates dsRNA in canonical RNases III is narrower in the R3B2 homodimer, suggesting that this feature could be responsible for the cleavage specificity for ssRNA. Conservation of this activity in R3B2 proteins from other mucormycosis-causing Mucorales fungi indicates an early evolutionary acquisition.

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37

Nicholson, Allen W. "Accurate enzymatic cleavage in vitro of a 2′-deoxyribose-substituted ribonuclease III processing signal." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1129, no. 3 (February 1992): 318–22. http://dx.doi.org/10.1016/0167-4781(92)90509-x.

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38

De Gregorio, Eliana, Chiara Abrescia, M. Stella Carlomagno, and Pier Paolo Di Nocera. "The abundant class of nemis repeats provides RNA substrates for ribonuclease III in Neisseriae." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1576, no. 1-2 (June 2002): 39–44. http://dx.doi.org/10.1016/s0167-4781(02)00290-7.

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39

Viegas, Sandra C., Inês J. Silva, Margarida Saramago, Susana Domingues, and Cecília M. Arraiano. "Regulation of the small regulatory RNA MicA by ribonuclease III: a target-dependent pathway." Nucleic Acids Research 39, no. 7 (December 7, 2010): 2918–30. http://dx.doi.org/10.1093/nar/gkq1239.

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40

Watkins, Kenneth P., Tiffany S. Kroeger, Amy M. Cooke, Rosalind E. Williams-Carrier, Giulia Friso, Susan E. Belcher, Klaas J. van Wijk, and Alice Barkan. "A Ribonuclease III Domain Protein Functions in Group II Intron Splicing in Maize Chloroplasts." Plant Cell 19, no. 8 (August 2007): 2606–23. http://dx.doi.org/10.1105/tpc.107.053736.

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41

Iino, Y., A. Sugimoto, and M. Yamamoto. "S. pombe pac1+, whose overexpression inhibits sexual development, encodes a ribonuclease III-like RNase." EMBO Journal 10, no. 1 (January 1991): 221–26. http://dx.doi.org/10.1002/j.1460-2075.1991.tb07939.x.

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42

Calin-Jageman, I. "RNA structure-dependent uncoupling of substrate recognition and cleavage by Escherichia coli ribonuclease III." Nucleic Acids Research 31, no. 9 (May 1, 2003): 2381–92. http://dx.doi.org/10.1093/nar/gkg329.

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43

Comeau, Marc-Andre, Daniel A. Lafontaine, and Sherif Abou Elela. "The catalytic efficiency of yeast ribonuclease III depends on substrate specific product release rate." Nucleic Acids Research 44, no. 16 (June 1, 2016): 7911–21. http://dx.doi.org/10.1093/nar/gkw507.

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44

Johanson, Timothy M., Andrew M. Lew, and Mark M. W. Chong. "MicroRNA-independent roles of the RNase III enzymes Drosha and Dicer." Open Biology 3, no. 10 (October 2013): 130144. http://dx.doi.org/10.1098/rsob.130144.

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The ribonuclease III enzymes Drosha and Dicer are renowned for their central roles in the biogenesis of microRNAs (miRNAs). For many years, this has overshadowed the true versatility and importance of these enzymes in the processing of other RNA substrates. For example, Drosha also recognizes and cleaves messenger RNAs (mRNAs), and potentially ribosomal RNA. The cleavage of mRNAs occurs via recognition of secondary stem-loop structures similar to miRNA precursors, and is an important mechanism of repressing gene expression, particularly in progenitor/stem cell populations. On the other hand, Dicer also has critical roles in genome regulation and surveillance. These include the production of endogenous small interfering RNAs from many sources, and the degradation of potentially harmful short interspersed element and viral RNAs. These findings have sparked a renewed interest in these enzymes, and their diverse functions in biology.

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45

Peters, David, and Jane Peters. "The ribbon of hydrogen bonds and the pseudomolecule in the three-dimensional structure of globular proteins. III. Bovine pancreatic ribonuclease A and bovine seminal ribonuclease." Biopolymers 65, no. 5 (October 18, 2002): 347–53. http://dx.doi.org/10.1002/bip.10265.

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46

Lavoie, Mathieu, and Sherif Abou Elela. "Yeast Ribonuclease III Uses a Network of Multiple Hydrogen Bonds for RNA Binding and Cleavage†." Biochemistry 47, no. 33 (August 2008): 8514–26. http://dx.doi.org/10.1021/bi800238u.

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47

Redko, Yulia, and Ciarán Condon. "Ribosomal protein L3 bound to 23S precursor rRNA stimulates its maturation by Mini-III ribonuclease." Molecular Microbiology 71, no. 5 (March 2009): 1145–54. http://dx.doi.org/10.1111/j.1365-2958.2008.06591.x.

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48

Bartolucci, Alison F., Tracy Uliasz, and John J. Peluso. "MicroRNA-21 as a regulator of human cumulus cell viability and its potential influence on the developmental potential of the oocyte." Biology of Reproduction 103, no. 1 (April 25, 2020): 94–103. http://dx.doi.org/10.1093/biolre/ioaa058.

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Abstract MicroRNA-21 is expressed in bovine, murine, and human cumulus cells with its expression in murine and bovine cumulus cells correlated with oocyte developmental potential. The aim of this study was to assess the relationship between cumulus cell MIR-21 and human oocyte developmental potential. These studies revealed that both the immature and mature forms of MicroRNA-21 (MIR-21-5p) were elevated in cumulus cells of oocytes that developed into blastocysts compared to cumulus cells of oocytes that arrested prior to blastocyst formation. This increase in MicroRNA-21 was observed regardless of whether the oocytes developed into euploid or aneuploid blastocysts. Moreover, MIR-21-5p levels in cumulus cells surrounding oocytes that either failed to mature or matured to metaphase II but failed to fertilize, were ≈50% less than the MIR-21-5p levels associated with oocytes that arrested prior to blastocyst formation. Why cumulus cells associated with oocytes of reduced developmental potential expressed less MIR-21-5p is unknown. It is unlikely due to reduced expression of either the receptors of growth differentiation factor 9 or rosha Ribonuclease III (DROSHA) and Dicer Ribonuclease III (DICER) which sequentially promote the conversion of immature forms of MicroRNA-21 to mature MicroRNA-21. Furthermore, cultured cumulus cells treated with a MIR-21-5p inhibitor had an increase in apoptosis and a corresponding increase in the expression of PTEN, a gene known to inhibit the AKT-dependent survival pathway in cumulus cells. These studies provide evidence for a role of MicroRNA-21 in human cumulus cells that influences the developmental potential of human oocytes.

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49

Ciechanowska, Kinga, Maria Pokornowska, and Anna Kurzyńska-Kokorniak. "Genetic Insight into the Domain Structure and Functions of Dicer-Type Ribonucleases." International Journal of Molecular Sciences 22, no. 2 (January 9, 2021): 616. http://dx.doi.org/10.3390/ijms22020616.

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Abstract:

Ribonuclease Dicer belongs to the family of RNase III endoribonucleases, the enzymes that specifically hydrolyze phosphodiester bonds found in double-stranded regions of RNAs. Dicer enzymes are mostly known for their essential role in the biogenesis of small regulatory RNAs. A typical Dicer-type RNase consists of a helicase domain, a domain of unknown function (DUF283), a PAZ (Piwi-Argonaute-Zwille) domain, two RNase III domains, and a double-stranded RNA binding domain; however, the domain composition of Dicers varies among species. Dicer and its homologues developed only in eukaryotes; nevertheless, the two enzymatic domains of Dicer, helicase and RNase III, display high sequence similarity to their prokaryotic orthologs. Evolutionary studies indicate that a combination of the helicase and RNase III domains in a single protein is a eukaryotic signature and is supposed to be one of the critical events that triggered the consolidation of the eukaryotic RNA interference. In this review, we provide the genetic insight into the domain organization and structure of Dicer proteins found in vertebrate and invertebrate animals, plants and fungi. We also discuss, in the context of the individual domains, domain deletion variants and partner proteins, a variety of Dicers’ functions not only related to small RNA biogenesis pathways.

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Ciechanowska, Kinga, Maria Pokornowska, and Anna Kurzyńska-Kokorniak. "Genetic Insight into the Domain Structure and Functions of Dicer-Type Ribonucleases." International Journal of Molecular Sciences 22, no. 2 (January 9, 2021): 616. http://dx.doi.org/10.3390/ijms22020616.

Full text

Abstract:

Ribonuclease Dicer belongs to the family of RNase III endoribonucleases, the enzymes that specifically hydrolyze phosphodiester bonds found in double-stranded regions of RNAs. Dicer enzymes are mostly known for their essential role in the biogenesis of small regulatory RNAs. A typical Dicer-type RNase consists of a helicase domain, a domain of unknown function (DUF283), a PAZ (Piwi-Argonaute-Zwille) domain, two RNase III domains, and a double-stranded RNA binding domain; however, the domain composition of Dicers varies among species. Dicer and its homologues developed only in eukaryotes; nevertheless, the two enzymatic domains of Dicer, helicase and RNase III, display high sequence similarity to their prokaryotic orthologs. Evolutionary studies indicate that a combination of the helicase and RNase III domains in a single protein is a eukaryotic signature and is supposed to be one of the critical events that triggered the consolidation of the eukaryotic RNA interference. In this review, we provide the genetic insight into the domain organization and structure of Dicer proteins found in vertebrate and invertebrate animals, plants and fungi. We also discuss, in the context of the individual domains, domain deletion variants and partner proteins, a variety of Dicers’ functions not only related to small RNA biogenesis pathways.

APA, Harvard, Vancouver, ISO, and other styles

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