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Journal articles on the topic 'DEAH-box ATPase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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1

Schmitt, Andreas, Florian Hamann, Piotr Neumann, and Ralf Ficner. "Crystal structure of the spliceosomal DEAH-box ATPase Prp2." Acta Crystallographica Section D Structural Biology 74, no. 7 (2018): 643–54. http://dx.doi.org/10.1107/s2059798318006356.

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The DEAH-box ATPase Prp2 plays a key role in the activation of the spliceosome as it promotes the transition from the Bactto the catalytically active B* spliceosome. Here, four crystal structures of Prp2 are reported: one of the nucleotide-free state and three different structures of the ADP-bound state. The overall conformation of the helicase core, formed by two RecA-like domains, does not differ significantly between the ADP-bound and the nucleotide-free states. However, intrinsic flexibility of Prp2 is observed, varying the position of the C-terminal domains with respect to the RecA domain
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2

Mayas, R. M., H. Maita, D. R. Semlow, and J. P. Staley. "Spliceosome discards intermediates via the DEAH box ATPase Prp43p." Proceedings of the National Academy of Sciences 107, no. 22 (2010): 10020–25. http://dx.doi.org/10.1073/pnas.0906022107.

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3

Chen, Hsin-Chou, Chi-Kang Tseng, Rong-Tzong Tsai, Che-Sheng Chung, and Soo-Chen Cheng. "Link of NTR-Mediated Spliceosome Disassembly with DEAH-Box ATPases Prp2, Prp16, and Prp22." Molecular and Cellular Biology 33, no. 3 (2012): 514–25. http://dx.doi.org/10.1128/mcb.01093-12.

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ABSTRACTThe DEAH-box ATPase Prp43 is required for disassembly of the spliceosome after the completion of splicing or after the discard of the spliceosome due to a splicing defect. Prp43 associates with Ntr1 and Ntr2 to form the NTR complex and is recruited to the spliceosome via the interaction of Ntr2 and U5 component Brr2. Ntr2 alone can bind to U5 and to the spliceosome. To understand how NTR might mediate the disassembly of spliceosome intermediates, we arrested the spliceosome at various stages of the assembly pathway and assessed its susceptibility to disassembly. We found that NTR could
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4

Hamann, Florian, Lars C. Zimmerningkat, Robert A. Becker, et al. "The structure of Prp2 bound to RNA and ADP-BeF3−reveals structural features important for RNA unwinding by DEAH-box ATPases." Acta Crystallographica Section D Structural Biology 77, no. 4 (2021): 496–509. http://dx.doi.org/10.1107/s2059798321001194.

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Noncoding intron sequences present in precursor mRNAs need to be removed prior to translation, and they are excisedviathe spliceosome, a multimegadalton molecular machine composed of numerous protein and RNA components. The DEAH-box ATPase Prp2 plays a crucial role during pre-mRNA splicing as it ensures the catalytic activation of the spliceosome. Despite high structural similarity to other spliceosomal DEAH-box helicases, Prp2 does not seem to function as an RNA helicase, but rather as an RNA-dependent ribonucleoprotein particle-modifying ATPase. Recent crystal structures of the spliceosomal
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5

Leeds, Nina B., Eliza C. Small, Shawna L. Hiley, Timothy R. Hughes, and Jonathan P. Staley. "The Splicing Factor Prp43p, a DEAH Box ATPase, Functions in Ribosome Biogenesis." Molecular and Cellular Biology 26, no. 2 (2006): 513–22. http://dx.doi.org/10.1128/mcb.26.2.513-522.2006.

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ABSTRACT Biogenesis of the small and large ribosomal subunits requires modification, processing, and folding of pre-rRNA to yield mature rRNA. Here, we report that efficient biogenesis of both small- and large-subunit rRNAs requires the DEAH box ATPase Prp43p, a pre-mRNA splicing factor. By steady-state analysis, a cold-sensitive prp43 mutant accumulates 35S pre-rRNA and depletes 20S, 27S, and 7S pre-rRNAs, precursors to the small- and large-subunit rRNAs. By pulse-chase analysis, the prp43 mutant is defective in the formation of 20S and 27S pre-rRNAs and in the accumulation of 18S and 25S mat
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6

Tsugeki, Ryuji, and Shiho Terada. "The Arabidopsis ortholog of the DEAH-box ATPase Prp16 influences auxin-mediated development." Plant Signaling & Behavior 10, no. 10 (2015): e1074369. http://dx.doi.org/10.1080/15592324.2015.1074369.

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7

Ma, Yupo, Tammy Barnett, Li Chai, et al. "DEAH-Box Splicing Factor Gene, Prp16 Amplification in Acute Myeloid Leukemia." Blood 108, no. 11 (2006): 4479. http://dx.doi.org/10.1182/blood.v108.11.4479.4479.

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Abstract Aberrant mRNA splicing has been observed frequently in solid tumors and shown to play a functionally significant role in tumorgenesis. Here we demonstrate that the DEAH-Box splicing factor gene, Prp16, is amplified in fresh human acute myeloid leukemia (AML) and in established AML cell lines. Prp16, an RNA-dependent ATPase required for pre-mRNA splicing, maps to chromosome 16q22, a region frequently altered in AML. Amplification of the Prp16 gene was initially detected using digital karyotyping, a powerful technique for analyzing genome-wide alterations in DNA copy number and verified
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8

Gencheva, Marieta, Mitsuo Kato, Alain N. S. Newo, and Ren-Jang Lin. "Contribution of DEAH-box protein DHX16 in human pre-mRNA splicing." Biochemical Journal 429, no. 1 (2010): 25–32. http://dx.doi.org/10.1042/bj20100266.

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Studies of mammalian splicing factors are often focused on small nuclear ribonucleoproteins or regulatory RNA-binding proteins, such as hnRNP (heterogeneous nuclear ribonucleoprotein) and SR proteins (serine/arginine-rich proteins); however, much less is known about the contribution of DExD/H-box proteins or RNA helicases in mammalian pre-mRNA splicing. The human DEAH-box protein DHX16 [also known as DBP2 (DEAD-box protein 2)], is homologous with Caenorhabditis elegans Mog-4, Schizosaccharomyces pombe Prp8 and Saccharomyces cerevisiae Prp2. In the present study, we show that DHX16 is required
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9

Tseng, C. K., H. L. Liu, and S. C. Cheng. "DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps." RNA 17, no. 1 (2010): 145–54. http://dx.doi.org/10.1261/rna.2459611.

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10

Campodonico, Eva, and Beate Schwer. "ATP-Dependent Remodeling of the Spliceosome: Intragenic Suppressors of Release-Defective Mutants of Saccharomyces cerevisiae Prp22." Genetics 160, no. 2 (2002): 407–15. http://dx.doi.org/10.1093/genetics/160.2.407.

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Abstract The essential splicing factor Prp22 is a DEAH-box helicase that catalyzes the release of mRNA from the spliceosome. ATP hydrolysis by Prp22 is necessary but not sufficient for spliceosome disassembly. Previous work showed that mutations in motif III (635SAT637) of Prp22 that uncouple ATP hydrolysis from spliceosome disassembly lead to severe cold-sensitive (cs) growth defects and to impaired RNA unwinding activity in vitro. The cs phenotype of S635A (635AAT) can be suppressed by intragenic mutations that restore RNA unwinding. We now report the isolation and characterization of new in
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11

Hamann, Florian, Andreas Schmitt, Filippo Favretto, et al. "Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2." Proceedings of the National Academy of Sciences 117, no. 6 (2020): 2948–56. http://dx.doi.org/10.1073/pnas.1907960117.

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The spliceosome consists of five small RNAs and more than 100 proteins. Almost 50% of the human spliceosomal proteins were predicted to be intrinsically disordered or to contain disordered regions, among them the G-patch protein Spp2. The G-patch region of Spp2 binds to the DEAH-box ATPase Prp2, and both proteins together are essential for promoting the transition from the Bact to the catalytically active B* spliceosome. Here we show by circular dichroism and nuclear magnetic resonance (NMR) spectroscopy that Spp2 is intrinsically disordered in solution. Crystal structures of a complex consist
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12

Kudlinzki, Denis, Andreas Schmitt, Henning Christian, and Ralf Ficner. "Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22." Biological Chemistry 393, no. 10 (2012): 1131–40. http://dx.doi.org/10.1515/hsz-2012-0158.

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Abstract Splicing of pre-mRNA requires the activity of at least eight different DEAD/H-box proteins that are involved in distinct steps of the splicing process. These proteins are driving the spliceosomal machinery by ATP-dependent unwinding of dsRNA and/or disrupting protein-RNA complexes. The spliceosomal DEAH-box proteins Prp2, Prp16, Prp22 and Prp43 share homologous C-terminal domains (CTD). We have determined the crystal structure of the CTD of human Prp22 by means of MAD. The fold of the human Prp22-CTD closely resembles that of the yeast Prp43-CTD. The similarity of these helicase-assoc
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13

Wagner, J. D. O. "The DEAH-box protein PRP22 is an ATPase that mediates ATP-dependent mRNA release from the spliceosome and unwinds RNA duplexes." EMBO Journal 17, no. 10 (1998): 2926–37. http://dx.doi.org/10.1093/emboj/17.10.2926.

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14

Silverman, Edward J., Ayaka Maeda, Janet Wei, Paul Smith, Jean D. Beggs, and Ren-Jang Lin. "Interaction between a G-Patch Protein and a Spliceosomal DEXD/H-Box ATPase That Is Critical for Splicing." Molecular and Cellular Biology 24, no. 23 (2004): 10101–10. http://dx.doi.org/10.1128/mcb.24.23.10101-10110.2004.

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ABSTRACT Prp2 is an RNA-dependent ATPase that activates the spliceosome before the first transesterification reaction of pre-mRNA splicing. Prp2 has extensive homology throughout the helicase domain characteristic of DEXD/H-box helicases and a conserved carboxyl-terminal domain also found in the spliceosomal helicases Prp16, Prp22, and Prp43. Despite the extensive homology shared by these helicases, each has a distinct, sequential role in splicing; thus, uncovering the determinants of specificity becomes crucial to the understanding of Prp2 and the other DEAH-splicing helicases. Mutations in a
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15

Lundgren, K., S. Allan, S. Urushiyama, et al. "A connection between pre-mRNA splicing and the cell cycle in fission yeast: cdc28+ is allelic with prp8+ and encodes an RNA-dependent ATPase/helicase." Molecular Biology of the Cell 7, no. 7 (1996): 1083–94. http://dx.doi.org/10.1091/mbc.7.7.1083.

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The fission-yeast gene cdc28+ was originally identified in a screen for temperature-sensitive mutants that exhibit a cell-division cycle arrest and was found to be required for mitosis. We undertook a study of this gene to understand more fully the general requirements for entry into mitosis. Cells carrying the conditional lethal cdc28-P8 mutation divide once and arrest in G2 after being shifted to the restrictive temperature. We cloned the cdc28+ gene by complementation of the temperature-sensitive growth arrest in cdc28-P8. DNA sequence analysis indicated that cdc28+ encodes a member of the
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16

Warkocki, Zbigniew, Cornelius Schneider, Sina Mozaffari-Jovin, et al. "The G-patch protein Spp2 couples the spliceosome-stimulated ATPase activity of the DEAH-box protein Prp2 to catalytic activation of the spliceosome." Genes & Development 29, no. 1 (2015): 94–107. http://dx.doi.org/10.1101/gad.253070.114.

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17

Li, Quan, Xiangyang Li, and Hui Lin. "Proteomic Analysis Reveals Growth Inhibition of Coriolus versicolor by Methanol Extracts of Cinnamomum camphora Xylem." International Journal of Polymer Science 2021 (August 21, 2021): 1–9. http://dx.doi.org/10.1155/2021/6337906.

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The extracts of decay-resistant tree species are important research objects for the future development of wood preservatives. To understand the antifungal mechanisms of Coriolus versicolor inhibition with methanol extracts of C. camphora xylem, the protein profiles of C. versicolor were analyzed using 2-DE followed by MALDI-TOF/MS and bioinformatic analyses. The results showed that 41 protein spots were obviously changed among the 366-385 protein spots of C. versicolor treated with methanol extracts of C. camphora xylem. Twenty-one protein spots were upregulated, and 20 protein spots were down
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18

Hamann, Florian, Andreas Schmitt, Filippo Favretto, Markus Zweckstetter, and Ralf Ficner. "RNA translocation mechanism of spliceosomal DEAH-box ATPases." Acta Crystallographica Section A Foundations and Advances 75, a2 (2019): e100-e100. http://dx.doi.org/10.1107/s2053273319094567.

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19

Hamann, Florian, Marieke Enders, and Ralf Ficner. "Structural basis for RNA translocation by DEAH-box ATPases." Nucleic Acids Research 47, no. 8 (2019): 4349–62. http://dx.doi.org/10.1093/nar/gkz150.

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20

Semlow, Daniel R., Mario R. Blanco, Nils G. Walter, and Jonathan P. Staley. "Spliceosomal DEAH-Box ATPases Remodel Pre-mRNA to Activate Alternative Splice Sites." Cell 164, no. 5 (2016): 985–98. http://dx.doi.org/10.1016/j.cell.2016.01.025.

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21

Koodathingal, Prakash, Thaddeus Novak, Joseph A. Piccirilli, and Jonathan P. Staley. "The DEAH Box ATPases Prp16 and Prp43 Cooperate to Proofread 5′ Splice Site Cleavage during Pre-mRNA Splicing." Molecular Cell 39, no. 3 (2010): 385–95. http://dx.doi.org/10.1016/j.molcel.2010.07.014.

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