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Journal articles on the topic 'RuvB-like'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Kanemaki, Masato, Yumiko Kurokawa, Toru Matsu-ura, et al. "TIP49b, a New RuvB-like DNA Helicase, Is Included in a Complex Together with Another RuvB-like DNA Helicase, TIP49a." Journal of Biological Chemistry 274, no. 32 (1999): 22437–44. http://dx.doi.org/10.1074/jbc.274.32.22437.

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2

Qiu, Xiao-Bo, Yi-Ling Lin, Kelly C. Thome, et al. "An Eukaryotic RuvB-like Protein (RUVBL1) Essential for Growth." Journal of Biological Chemistry 273, no. 43 (1998): 27786–93. http://dx.doi.org/10.1074/jbc.273.43.27786.

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3

Kakugawa, Satoshi, Masayuki Shimojima, Gabriele Neumann, Hideo Goto, and Yoshihiro Kawaoka. "RuvB-Like Protein 2 Is a Suppressor of Influenza A Virus Polymerases." Journal of Virology 83, no. 13 (2009): 6429–34. http://dx.doi.org/10.1128/jvi.00293-09.

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ABSTRACT In pro- and eukaryotic cells, RuvB-like protein 2 (RBL2) resolves Holliday junction recombination intermediates. Here, we identified RBL2 as a suppressor of influenza A virus replication. Human RBL2 appears to interfere with the oligomerization of the viral nucleoprotein, a critical step in the assembly of viral replication complexes.

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4

Rodríguez, Carlos F., and Oscar Llorca. "RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes." Cells 9, no. 5 (2020): 1139. http://dx.doi.org/10.3390/cells9051139.

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The Rvb1-Rvb2-Tah1-Pih1 (R2TP) complex is a co-chaperone complex that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II (Pol II) and complexes of the phosphatidylinositol-3-kinase-like family of kinases (PIKKs), such as mTORC1 and ATR/ATRIP. R2TP is made of four subunits: RuvB-like protein 1 (RUVBL1) and RuvB-like 2 (RUVBL2) AAA-type ATPases, RNA polymerase II-associated protein 3 (RPAP3), and the Protein interacting with Hsp90 1 (PIH1) domain-containing protein 1 (PIH1D1). R2TP associates with other proteins as part of a

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5

Gospodinov, Anastas, and Boyka Anachkova. "Lack of Effect of RuvB-Like Proteins on DNA Damage Signaling Activation." Zeitschrift für Naturforschung C 65, no. 1-2 (2010): 148–52. http://dx.doi.org/10.1515/znc-2010-1-223.

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Ataxia telangiectasia mutated (ATM) kinase is a central player in cellular response to DNA damage. Phosphorylation of the histone H2AX by ATM is required for the accumulation of repair proteins at the sites of double-strand breaks. Recently, it was reported that the histone acetyltransferase Tat interactive protein-60 (TIP60) is required to acetylate ATM prior to its activation. The RuvB-like proteins TIP48 and TIP49 are known to be necessary for the assembly and functional activity of the TIP60 acetyltransferase complex. In the present communication, we investigated the requirements of TIP48

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6

Magalska, Adriana, Anna Katharina Schellhaus, Daniel Moreno-Andrés, et al. "RuvB-like ATPases Function in Chromatin Decondensation at the End of Mitosis." Developmental Cell 31, no. 3 (2014): 305–18. http://dx.doi.org/10.1016/j.devcel.2014.09.001.

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7

Niewiarowski, Andrew, Alison S. Bradley, Jayesh Gor, Adam R. McKay, Stephen J. Perkins, and Irina R. Tsaneva. "Oligomeric assembly and interactions within the human RuvB-like RuvBL1 and RuvBL2 complexes." Biochemical Journal 429, no. 1 (2010): 113–25. http://dx.doi.org/10.1042/bj20100489.

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The two closely related eukaryotic AAA+ proteins (ATPases associated with various cellular activities), RuvBL1 (RuvB-like 1) and RuvBL2, are essential components of large multi-protein complexes involved in diverse cellular processes. Although the molecular mechanisms of RuvBL1 and RuvBL2 function remain unknown, oligomerization is likely to be important for their function together or individually, and different oligomeric forms might underpin different functions. Several experimental approaches were used to investigate the molecular architecture of the RuvBL1–RuvBL2 complex and the role of th

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8

Mu, Xin, Yajing Fu, Yiping Zhu, et al. "HIV-1 Exploits the Host Factor RuvB-like 2 to Balance Viral Protein Expression." Cell Host & Microbe 18, no. 2 (2015): 233–42. http://dx.doi.org/10.1016/j.chom.2015.06.018.

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9

Makino, Yasutaka, Masato Kanemaki, Yumiko Kurokawa, Takehiko Koji, and Taka-aki Tamura. "A Rat RuvB-like Protein, TIP49a, Is a Germ Cell-enriched Novel DNA Helicase." Journal of Biological Chemistry 274, no. 22 (1999): 15329–35. http://dx.doi.org/10.1074/jbc.274.22.15329.

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10

Gorynia, Sabine, Pedro M. Matias, Susana Gonçalves, et al. "Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1." Acta Crystallographica Section F Structural Biology and Crystallization Communications 62, no. 1 (2005): 61–66. http://dx.doi.org/10.1107/s1744309105041400.

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11

Sawitzke, J. A., and F. W. Stahl. "Phage lambda has an analog of Escherichia coli recO, recR and recF genes." Genetics 130, no. 1 (1992): 7–16. http://dx.doi.org/10.1093/genetics/130.1.7.

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Abstract The RecF pathway catalyzes generalized recombination in Escherichia coli that is mutant for recBC, sbcB and sbcC. This pathway operating on conjugational recombination requires the recA, recF, recJ, recN, recO, recQ, recR, ruvA, ruvB and ruvC genes. In contrast, lambda mutant for its own recombination genes, int, red alpha and red beta, requires only the recA and recJ genes to recombine efficiently in recBC sbcB sbcC cells. Deletion of an open reading frame in the ninR region of lambda results in an additional requirement for recO, recR and recF in order to recombine in recBC sbcB sbc

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12

Rousseau, Benoît, Ludovic Ménard, Valérie Haurie, et al. "Overexpression and role of the ATPase and putative DNA helicase RuvB-like 2 in human hepatocellular carcinoma." Hepatology 46, no. 4 (2007): 1108–18. http://dx.doi.org/10.1002/hep.21770.

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13

Hong, Soomin, Junghyun Jo, Hyung Joon Kim, et al. "RuvB-Like Protein 2 (Ruvbl2) Has a Role in Directing the Neuroectodermal Differentiation of Mouse Embryonic Stem Cells." Stem Cells and Development 25, no. 18 (2016): 1376–85. http://dx.doi.org/10.1089/scd.2016.0076.

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14

Wang, Cheng-Wei, Wan-Chieh Chen, Li-Jing Lin, Chung-Tsai Lee, Tung-Hai Tseng, and Wei-Ming Leu. "OIP30, a RuvB-Like DNA Helicase 2, is a Potential Substrate for the Pollen-Predominant OsCPK25/26 in Rice." Plant and Cell Physiology 52, no. 9 (2011): 1641–56. http://dx.doi.org/10.1093/pcp/pcr094.

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15

Zimmermann, Fabian, Marina Serna, Artur Ezquerra, Rafael Fernandez-Leiro, Oscar Llorca та Jens Luders. "Assembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase". Science Advances 6, № 51 (2020): eabe0894. http://dx.doi.org/10.1126/sciadv.abe0894.

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The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has evaded in vitro reconstitution and thus detailed structure-function studies. Here, we show that a complex of RuvB-like protein 1 (RUVBL1) and RUVBL2 “RUVBL” controls assembly and composition of γTuRC in human cells. Likewise, RUVBL assembles γTuRC from a minimal set of core subunits in a heterologous coexpression system. RUVBL interacts with γTuRC subcomplexes but is not part of fully assembled γTuRC

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16

Gohshi, T., M. Shimada, S. Kawahire, et al. "Molecular Cloning of Mouse p47, a Second Group Mammalian RuvB DNA Helicase-Like Protein: Homology with Those from Human and Saccharomyces cerevisiae." Journal of Biochemistry 125, no. 5 (1999): 939–46. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022372.

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17

Wang, Yimeng, Jianhong Zhou, Samuel G. Mackintosh, and Yuchun Du. "RuvB-Like Protein 2 Interacts with the NS1 Protein of Influenza A Virus and Affects Apoptosis That Is Counterbalanced by Type I Interferons." Viruses 13, no. 6 (2021): 1038. http://dx.doi.org/10.3390/v13061038.

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The NS1 protein of influenza A virus (IAV) plays important roles in viral pathogenesis and host immune response. Through a proteomic approach, we have identified RuvB-like proteins 1 and 2 (RuvBL1 and RuvBL2) as interacting partners of the NS1 protein of IAVs. Infection of human lung A549 cells with A/PR/8/34 (PR8) virus resulted in reductions in the protein levels of RuvBL2 but not RuvBL1. Further studies with RuvBL2 demonstrated that the NS1-RuvBL2 interaction is RNA-independent, and RuvBL2 binds the RNA-binding domain of the NS1. Infection of interferon (IFN)-deficient Vero cells with wild-

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18

Ju, Dapeng, Wei Zhang, Jiawei Yan, et al. "Chemical perturbations reveal that RUVBL2 regulates the circadian phase in mammals." Science Translational Medicine 12, no. 542 (2020): eaba0769. http://dx.doi.org/10.1126/scitranslmed.aba0769.

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Transcriptional regulation lies at the core of the circadian clockwork, but how the clock-related transcription machinery controls the circadian phase is not understood. Here, we show both in human cells and in mice that RuvB-like ATPase 2 (RUVBL2) interacts with other known clock proteins on chromatin to regulate the circadian phase. Pharmacological perturbation of RUVBL2 with the adenosine analog compound cordycepin resulted in a rapid-onset 12-hour clock phase-shift phenotype at human cell, mouse tissue, and whole-animal live imaging levels. Using simple peripheral injection treatment, we f

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19

Ohdate, Hidezumi, Chun Ren Lim, Tetsuro Kokubo, Kenichi Matsubara, Yukio Kimata, and Kenji Kohno. "Impairment of the DNA Binding Activity of the TATA-binding Protein Renders the Transcriptional Function of Rvb2p/Tih2p, the Yeast RuvB-like Protein, Essential for Cell Growth." Journal of Biological Chemistry 278, no. 17 (2003): 14647–56. http://dx.doi.org/10.1074/jbc.m213220200.

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20

Doyon, Yannick, William Selleck, William S. Lane, Song Tan, and Jacques Côté. "Structural and Functional Conservation of the NuA4 Histone Acetyltransferase Complex from Yeast to Humans." Molecular and Cellular Biology 24, no. 5 (2004): 1884–96. http://dx.doi.org/10.1128/mcb.24.5.1884-1896.2004.

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ABSTRACT The NuA4 histone acetyltransferase (HAT) multisubunit complex is responsible for acetylation of histone H4 and H2A N-terminal tails in yeast. Its catalytic component, Esa1, is essential for cell cycle progression, gene-specific regulation and has been implicated in DNA repair. Almost all NuA4 subunits have clear homologues in higher eukaryotes, suggesting that the complex is conserved throughout evolution to metazoans. We demonstrate here that NuA4 complexes are indeed present in human cells. Tip60 and its splice variant Tip60b/PLIP were purified as stable HAT complexes associated wit

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21

Castorena, Carlos M., James G. MacKrell, Jonathan S. Bogan, Makoto Kanzaki, and Gregory D. Cartee. "Clustering of GLUT4, TUG, and RUVBL2 protein levels correlate with myosin heavy chain isoform pattern in skeletal muscles, but AS160 and TBC1D1 levels do not." Journal of Applied Physiology 111, no. 4 (2011): 1106–17. http://dx.doi.org/10.1152/japplphysiol.00631.2011.

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Skeletal muscle is a heterogeneous tissue. To further elucidate this heterogeneity, we probed relationships between myosin heavy chain (MHC) isoform composition and abundance of GLUT4 and four other proteins that are established or putative GLUT4 regulators [Akt substrate of 160 kDa (AS160), Tre-2/Bub2/Cdc 16-domain member 1 (TBC1D1), Tethering protein containing an UBX-domain for GLUT4 (TUG), and RuvB-like protein two (RUVBL2)] in 12 skeletal muscles or muscle regions from Wistar rats [adductor longus, extensor digitorum longus, epitrochlearis, gastrocnemius (mixed, red, and white), plantaris

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22

Gorynia, Sabine. "RuvB-like 1 - [Isoform 1]." Targeted Protein Database, May 19, 2008. http://dx.doi.org/10.2970/tpdb.2008.144.

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23

Haurie, V., A. Grigoletto, and J. Rosenbaum. "RUVBL1 (RuvB-like 1 (E. coli))." Atlas of Genetics and Cytogenetics in Oncology and Haematology, no. 3 (November 2011). http://dx.doi.org/10.4267/2042/44703.

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24

Grigoletto, A., V. Haurie, and J. Rosenbaum. "RUVBL2 (RuvB-like 2 (E. coli))." Atlas of Genetics and Cytogenetics in Oncology and Haematology, no. 3 (November 2011). http://dx.doi.org/10.4267/2042/44704.

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25

Silva, Sara T. N., José A. Brito, Rocío Arranz, et al. "X-ray structure of full-length human RuvB-Like 2 – mechanistic insights into coupling between ATP binding and mechanical action." Scientific Reports 8, no. 1 (2018). http://dx.doi.org/10.1038/s41598-018-31997-z.

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26

Yan, Tao, Fang Liu, Jiajia Gao, et al. "Multilevel regulation of RUVBL2 expression predicts poor prognosis in hepatocellular carcinoma." Cancer Cell International 19, no. 1 (2019). http://dx.doi.org/10.1186/s12935-019-0974-z.

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Abstract Background Hepatocellular carcinoma (HCC) is the second-most lethal cancer worldwide with a complex pathogenesis. RuvB-like 2 (RUVBL2) was previously found to contribute to hepatocarcinogenesis. However, its expression, regulation and clinical significance have not been systematically evaluated in a large number of clinical samples. Methods Here, we performed a comprehensive analysis of RUVBL2 based on multiple datasets from 371 liver cancer patients of The Cancer Genome Atlas (TCGA) and on immunohistochemical staining in 153 subjects. In addition, the aberrant signaling pathways caus

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27

Liu, Qi, Wei Jiang, Yun Chen, Manyu Zhang, Xiaoling Geng, and Quan Wang. "Study on Circulating Antigens in Serum of Mice With Experimental Acute Toxoplasmosis." Frontiers in Microbiology 11 (January 18, 2021). http://dx.doi.org/10.3389/fmicb.2020.612252.

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Toxoplasma gondii is a ubiquitous apicomplexan protozoan parasite that can infect all warm-blooded animals, causing toxoplasmosis. Thus, efficient diagnosis methods for acute T. gondii infection are essential for its management. Circulating antigens (CAgs) are reliable diagnostic indicators of acute infection. In this study, we established a mouse model of acute T. gondii infection and explored new potential diagnostic factors. CAgs levels peaked 60 h after T. gondii inoculation and 31 CAgs were identified by immunoprecipitation-liquid chromatography-tandem mass spectrometry, among which RuvB-

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28

Zang, Xupeng, Ting Gu, Qun Hu, et al. "Global Transcriptomic Analyses Reveal Genes Involved in Conceptus Development During the Implantation Stages in Pigs." Frontiers in Genetics 12 (February 24, 2021). http://dx.doi.org/10.3389/fgene.2021.584995.

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Prenatal mortality remains a significant concern to the pig farming industry around the world. Spontaneous fetal loss ranging from 20 to 45% by term occur after fertilization, with most of the loss happening during the implantation period. Since the factors regulating the high mortality rates of early conceptus during implantation phases are poorly understood, we sought to analyze the overall gene expression changes during this period, and identify the molecular mechanisms involved in conceptus development. This work employed Illumina’s next-generation sequencing (RNA-Seq) and quantitative rea

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