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histone ubiquitination

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https://www.readbyqxmd.com/read/29142133/human-adenovirus-infection-causes-the-cellular-mkrn1-e3-ubiquitin-ligase-degradation-involving-the-viral-core-protein-pvii
#1
Raviteja Inturi, Kwangchol Mun, Katrin Singethan, Sabrina Schreiner, Tanel Punga
Human adenoviruses (HAdVs) are common human pathogens encoding a highly abundant histone-like core protein VII, which is involved in nuclear delivery and protection of viral DNA as well as in sequestering immune danger signals in infected cells. The molecular details of how protein VII acts as a multifunctional protein have remained to a large extent enigmatic. Here we report the identification of several cellular proteins interacting with the precursor pVII protein. We show that the cellular E3 ubiquitin ligase MKRN1 is a novel precursor pVII interacting protein in HAdV-C5-infected cells...
November 15, 2017: Journal of Virology
https://www.readbyqxmd.com/read/29130659/-dna-repair-function-and-mutation-of-an-h2b-monoubiquitination-factor-wdr70-in-ovarian-cancer
#2
Zi-Zhi Tang, Hai-Bin Wang, Ming Zeng, Cong Liu, De-Hua Li
OBJECTIVE: To investigate the roles of enzyme DCAF proteinDNA damagebinding protein 1 (DDB1)/cullin4 (CRL4) complex family members CRL4WD40 repeat domain protein 70 (WDR70) in DNA repair process and its mutation in ovarian cancer. METHODS: Immunofluorescent assay was employed to measure H2AX (γH2AX) and phosphorylated replication protein A2 (RPA32) formed in siDDB1 or siWDR70 ovarian cancer cells after the treatments of chemical medicine and radioactive threapy...
September 2017: Sichuan da Xue Xue Bao. Yi Xue Ban, Journal of Sichuan University. Medical Science Edition
https://www.readbyqxmd.com/read/29127375/dna-damage-induced-histone-h1-ubiquitylation-is-mediated-by-huwe1-and-stimulates-the-rnf8-rnf168-pathway
#3
I K Mandemaker, L van Cuijk, R C Janssens, H Lans, K Bezstarosti, J H Hoeijmakers, J A Demmers, W Vermeulen, J A Marteijn
The DNA damage response (DDR), comprising distinct repair and signalling pathways, safeguards genomic integrity. Protein ubiquitylation is an important regulatory mechanism of the DDR. To study its role in the UV-induced DDR, we characterized changes in protein ubiquitylation following DNA damage using quantitative di-Gly proteomics. Interestingly, we identified multiple sites of histone H1 that are ubiquitylated upon UV-damage. We show that UV-dependent histone H1 ubiquitylation at multiple lysines is mediated by the E3-ligase HUWE1...
November 10, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29118980/sirt1-dependent-modulation-of-methylation-and-acetylation-of-histone-h3-on-lysine-9-h3k9-in-the-zygotic-pronuclei-improves-porcine-embryo-development
#4
Katerina Adamkova, Young-Joo Yi, Jaroslav Petr, Tereza Zalmanova, Kristyna Hoskova, Pavla Jelinkova, Jiri Moravec, Milena Kralickova, Miriam Sutovsky, Peter Sutovsky, Jan Nevoral
Background: The histone code is an established epigenetic regulator of early embryonic development in mammals. The lysine residue K9 of histone H3 (H3K9) is a prime target of SIRT1, a member of NAD(+)-dependent histone deacetylase family of enzymes targeting both histone and non-histone substrates. At present, little is known about SIRT1-modulation of H3K9 in zygotic pronuclei and its association with the success of preimplantation embryo development. Therefore, we evaluated the effect of SIRT1 activity on H3K9 methylation and acetylation in porcine zygotes and the significance of H3K9 modifications for early embryonic development...
2017: Journal of Animal Science and Biotechnology
https://www.readbyqxmd.com/read/29116388/the-evolutionarily-conserved-factor-sus1-eny2-plays-a-role-in-telomere-length-maintenance
#5
Amparo Galán, Encar García-Oliver, Carme Nuño-Cabanes, Linda Rubinstein, Martin Kupiec, Susana Rodríguez-Navarro
Sus1 is a conserved protein involved in histone H2B de-ubiquitination and mRNA export from the nucleus in eukaryotes. Previous studies implicated Sus1 partners in genome integrity including telomere homeostasis. However, the implication of Sus1 in telomere maintenance remains largely unknown. In this study, we found that yeast Sus1 interacts physically and genetically with factors involved in telomere maintenance and its absence leads to elongated telomeres. Deletion of several of Sus1's partners also leads to longer telomeres...
November 7, 2017: Current Genetics
https://www.readbyqxmd.com/read/29113987/bap1-is-a-novel-target-in-hpv-negative-head-and-neck-cancer
#6
Xiyou Liu, Liangpeng Yang, David P Molkentine, David Valdacanas, Shiying Yu, Manish Kumar, Raymond E Meyn, John Heymach, Heath D Skinner
PURPOSE: This study examined the potential role of the nuclear deubiquitinating enzyme BRCA1-associated protein-1 (BAP1) in radioresistance in head and neck squamous cell cancer (HNSCC). EXPERIMENTAL DESIGN: We overexpressed, knocked down, and rescued BAP1 expression in six HNSCC cell lines, three human papillomavirus (HPV) -negative and HPV-positive, and examined the effects on radiosensitivity in vitro and in HNSCC mouse xenograft models. Radiosensitivity was assessed by clonogenic cell survival and tumor growth delay assays; changes in protein expression were analyzed by immunofluorescence staining and western blotting...
November 7, 2017: Clinical Cancer Research: An Official Journal of the American Association for Cancer Research
https://www.readbyqxmd.com/read/29104064/a-chemical-proteomics-approach-to-reveal-direct-protein-protein-interactions-in-living-cells
#7
Ralph E Kleiner, Lisa E Hang, Kelly R Molloy, Brian T Chait, Tarun M Kapoor
Protein-protein interactions mediate essential cellular processes, however the detection of native interactions is challenging since they are often low affinity and context dependent. Here, we develop a chemical proteomics approach in vivo CLASPI [iCLASPI] (in vivo crosslinking-assisted and stable isotope labeling by amino acids in cell culture [SILAC]-based protein identification) relying upon photo-crosslinking, amber suppression, and SILAC-based quantitative proteomics to profile context-dependent protein-protein interactions in living cells...
October 25, 2017: Cell Chemical Biology
https://www.readbyqxmd.com/read/29099265/analysis-of-defective-protein-ubiquitylation-associated-to-adriamycin-resistant-cells
#8
Valérie Lang, Fabienne Aillet, Wendy Xolalpa, Sonia Serna, Laurie Ceccato, Rosa G Lopez-Reyes, Maria Paz Lopez-Mato, Radosław Januchowski, Niels-Christian Reichardt, Manuel S Rodriguez
DNA damage activated by Adriamycin (ADR) promotes ubiquitin-proteasome system-mediated proteolysis by stimulating both the activity of ubiquitylating enzymes and the proteasome. In ADR-resistant breast cancer MCF7 (MCF7(ADR)) cells, protein ubiquitylation is significantly reduced compared to the parental MCF7 cells. Here, we used tandem ubiquitin-binding entities (TUBEs) to analyze the ubiquitylation pattern observed in MCF7 or MCF7(ADR) cells. While in MCF7, the level of total ubiquitylation increased up to six-fold in response to ADR, in MCF7(ADR) cells only a two-fold response was found...
November 3, 2017: Cell Cycle
https://www.readbyqxmd.com/read/29097627/how-to-rewire-the-host-cell-a-home-improvement-guide-for-intracellular-bacteria
#9
REVIEW
Elias Cornejo, Philipp Schlaermann, Shaeri Mukherjee
Intracellular bacterial pathogens have developed versatile strategies to generate niches inside the eukaryotic cells that allow them to survive and proliferate. Making a home inside the host offers many advantages; however, intracellular bacteria must also overcome many challenges, such as disarming innate immune signaling and accessing host nutrient supplies. Gaining entry into the cell and avoiding degradation is only the beginning of a successful intracellular lifestyle. To establish these replicative niches, intracellular pathogens secrete various virulence proteins, called effectors, to manipulate host cell signaling pathways and subvert host defense mechanisms...
November 2, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/29095668/sumo-modification-system-facilitates-the-exchange-of-histone-variant-h2a-z-2-at-dna-damage-sites
#10
Atsuhiko Fukuto, Masae Ikura, Tsuyoshi Ikura, Jiying Sun, Yasunori Horikoshi, Hiroki Shima, Kazuhiko Igarashi, Masayuki Kusakabe, Masahiko Harata, Naoki Horikoshi, Hitoshi Kurumizaka, Yoshiaki Kiuchi, Satoshi Tashiro
Histone exchange and histone post-translational modifications play important roles in the regulation of DNA metabolism, by re-organizing the chromatin configuration. We previously demonstrated that the histone variant H2A.Z-2 is rapidly exchanged at damaged sites after DNA double strand break induction in human cells. In yeast, the small ubiquitin-like modifier (SUMO) modification of H2A.Z is involved in the DNA damage response. However, whether the SUMO modification regulates the exchange of human H2A.Z-2 at DNA damage sites remains unclear...
November 2, 2017: Nucleus
https://www.readbyqxmd.com/read/29089422/a-cryptic-tudor-domain-links-brwd2-phip-to-compass-mediated-histone-h3k4-methylation
#11
Marc A J Morgan, Ryan A Rickels, Clayton K Collings, Xiaolin He, Kaixiang Cao, Hans-Martin Herz, Kira A Cozzolino, Nebiyu A Abshiru, Stacy A Marshall, Emily J Rendleman, Christie C Sze, Andrea Piunti, Neil L Kelleher, Jeffrey N Savas, Ali Shilatifard
Histone H3 Lys4 (H3K4) methylation is a chromatin feature enriched at gene cis-regulatory sequences such as promoters and enhancers. Here we identify an evolutionarily conserved factor, BRWD2/PHIP, which colocalizes with histone H3K4 methylation genome-wide in human cells, mouse embryonic stem cells, and Drosophila Biochemical analysis of BRWD2 demonstrated an association with the Cullin-4-RING ubiquitin E3 ligase-4 (CRL4) complex, nucleosomes, and chromatin remodelers. BRWD2/PHIP binds directly to H3K4 methylation through a previously unidentified chromatin-binding module related to Royal Family Tudor domains, which we named the CryptoTudor domain...
October 1, 2017: Genes & Development
https://www.readbyqxmd.com/read/29070146/-research-progress-on-molecular-mechanisms-of-resistance-to-bortezomib-in-multiple-myeloma-review
#12
Ling-Ling Shi, Yong-Ping Zhai
Over the last decade, bortezomib(BTZ) has been extensively applied in the treatment of hematological malignancies, particularly in multiple myeloma and mantle cell lymphoma, however, the appearence of secondary resistance to BTZ has brought a huge challenge in MM treatment. In the present review, the mechanisms of resistance to bortezomib in MM are summarized, focusing on the action of ubiquitin-proteasome system(UPS), endoplasmin reticulum stress, antophagy, inducible pro-survival signalling and bone marrow microenvironment as well as exploration of the potential therapeutic strategies in the clinical perspective...
October 2017: Zhongguo Shi Yan Xue Ye Xue za Zhi
https://www.readbyqxmd.com/read/29069806/modulating-bap1-expression-affects-ros-homeostasis-cell-motility-and-mitochondrial-function
#13
Lucie Hebert, Dorine Bellanger, Chloé Guillas, Antoine Campagne, Florent Dingli, Damarys Loew, Alice Fievet, Virginie Jacquemin, Tatiana Popova, Didier Jean, Fatima Mechta-Grigoriou, Raphaël Margueron, Marc-Henri Stern
The tumor suppressor BAP1 associates with ASXL1/2 to form the core Polycomb complex PR-DUB, which catalyzes the removal of mono-ubiquitin from several substrates including histone H2A. This complex also mediates the poly-deubiquitination of HCFC1, OGT and PCG1-α, preventing them from proteasomal degradation. Surprisingly, considering its role in a Polycomb complex, no transcriptional signature was consistently found among BAP1-inactivated tumor types. It was hypothesized that BAP1 tumor suppressor activity could reside, at least in part, in stabilizing proteins through its poly-deubiquitinase activity...
September 22, 2017: Oncotarget
https://www.readbyqxmd.com/read/29061044/ubiquitin-conjugation-probed-by-inflammation-in-myeloid-derived-suppressor-cell-extracellular-vesicles
#14
Katherine R Adams, Sitara Chauhan, Divya B Patel, Virginia K Clements, Yan Wang, Steven M Jay, Nathan J Edwards, Suzanne Ostrand-Rosenberg, Catherine Fenselau
Ubiquitinated proteins carried by the extracellular vesicles (EV) released by myeloid-derived suppressor cells (MDSC) have been investigated using proteomic strategies to examine the effect of tumor-associated inflammation. EV were collected from MDSC directly following isolation from tumor-bearing mice with low and high inflammation. Among the 1092 proteins (high inflammation) and 925 proteins (low inflammation) identified, more than 50% were observed as ubiquitinated proteoforms. More than three ubiquitin-attachment sites were characterized per ubiquitinated protein, on average...
November 10, 2017: Journal of Proteome Research
https://www.readbyqxmd.com/read/29058668/e3-ubiquitin-ligase-bre1-couples-sister-chromatid-cohesion-establishment-to-dna-replication-in-saccharomyces-cerevisiae
#15
Wei Zhang, Clarence Hue Lok Yeung, Liwen Wu, Karen Wing Yee Yuen
Bre1, a conserved E3 ubiquitin ligase in Saccharomyces cerevisiae, together with its interacting partner Lge1, are responsible for histone H2B monoubiquitination, which regulates transcription, DNA replication, DNA damage response and repair, ensuring the structural integrity of the genome. Deletion of BRE1 or LGE1 also results in whole chromosome instability. We discovered a novel role for Bre1, Lge1 and H2Bub1 in chromosome segregation and sister chromatid cohesion. Bre1's function in G1 and S phases contributes to cohesion establishment, but it is not required for cohesion maintenance in G2 phase...
October 23, 2017: ELife
https://www.readbyqxmd.com/read/29055779/ubiquitome-analysis-reveals-pcna-associated-factor-15-paf15-as-a-specific-ubiquitination-target-of-uhrf1-in-embryonic-stem-cells
#16
Elisabeth Karg, Martha Smets, Joel Ryan, Ignasi Forné, Weihua Qin, Christopher B Mulholland, Georgia Kalideris, Axel Imhof, Sebastian Bultmann, Heinrich Leonhardt
Ubiquitination is a multifunctional posttranslational modification controlling the activity, subcellular localization and stability of proteins. The E3 ubiquitin ligase UHRF1 is an essential epigenetic factor that recognizes repressive histone marks as well as hemi-methylated DNA and recruits DNMT1. To explore enzymatic functions of UHRF1 beyond epigenetic regulation we conducted a comprehensive screen in mouse embryonic stem cells to identify novel ubiquitination targets of UHRF1 and its paralogue UHRF2. We found differentially ubiquitinated peptides associated with a variety of biological processes such as transcriptional regulation and DNA damage response...
October 18, 2017: Journal of Molecular Biology
https://www.readbyqxmd.com/read/29053958/structure-of-the-dnmt1-reader-module-complexed-with-a-unique-two-mono-ubiquitin-mark-on-histone-h3-reveals-the-basis-for-dna-methylation-maintenance
#17
Satoshi Ishiyama, Atsuya Nishiyama, Yasushi Saeki, Kei Moritsugu, Daichi Morimoto, Luna Yamaguchi, Naoko Arai, Rumie Matsumura, Toru Kawakami, Yuichi Mishima, Hironobu Hojo, Shintaro Shimamura, Fuyuki Ishikawa, Shoji Tajima, Keiji Tanaka, Mariko Ariyoshi, Masahiro Shirakawa, Mitsunori Ikeguchi, Akinori Kidera, Isao Suetake, Kyohei Arita, Makoto Nakanishi
The proper location and timing of Dnmt1 activation are essential for DNA methylation maintenance. We demonstrate here that Dnmt1 utilizes two-mono-ubiquitylated histone H3 as a unique ubiquitin mark for its recruitment to and activation at DNA methylation sites. The crystal structure of the replication foci targeting sequence (RFTS) of Dnmt1 in complex with H3-K18Ub/23Ub reveals striking differences to the known ubiquitin-recognition structures. The two ubiquitins are simultaneously bound to the RFTS with a combination of canonical hydrophobic and atypical hydrophilic interactions...
October 19, 2017: Molecular Cell
https://www.readbyqxmd.com/read/29051390/corrigendum-the-histone-h2b-specific-ubiquitin-ligase-rnf20-hbre1-acts-as-a-putative-tumor-suppressor-through-selective-regulation-of-gene-expression
#18
Efrat Shema, Itay Tirosh, Yael Aylon, Jing Huang, Chaoyang Ye, Neta Moskovits, Nina Raver-Shapira, Neri Minsky, Judith Pirngruber, Gabi Tarcic, Pavla Hublarova, Lilach Moyal, Mali Gana-Weisz, Yosef Shiloh, Yossef Yarden, Steven A Johnsen, Borivoj Vojtesek, Shelley L Berger, Moshe Oren
No abstract text is available yet for this article.
September 15, 2017: Genes & Development
https://www.readbyqxmd.com/read/29050267/reversible-regulation-of-orc2-sumoylation-by-pias4-and-senp2
#19
Ronghua Wang, Fangming Liu, Yongxu Zhao, Dan Wu, Lihan Chen, Edward T H Yeh, Chao Huang
The small ubiquitin-related modifier (SUMO) system is essential for smooth progression of cell cycle at the G2/M phase. Many centromeric proteins are reversibly SUMOylated to ensure proper chromosome segregation at the mitosis. SUMOylation of centromeric Origin Recognition Complex subunit 2 (ORC2) at the G2/M phase is essential in maintaining genome integrity. However, how ORC2 SUMOylation is regulated remains largely unclear. Here we show that ORC2 SUMOylation is reversibly controlled by SUMO E3 ligase PIAS4 and De-SUMOylase SENP2...
September 19, 2017: Oncotarget
https://www.readbyqxmd.com/read/29042515/structural-basis-for-regulation-of-the-nucleo-cytoplasmic-distribution-of-bag6-by-trc35
#20
Jee-Young Mock, Yue Xu, Yihong Ye, William M Clemons
The metazoan protein BCL2-associated athanogene cochaperone 6 (Bag6) forms a hetero-trimeric complex with ubiquitin-like 4A and transmembrane domain recognition complex 35 (TRC35). This Bag6 complex is involved in tail-anchored protein targeting and various protein quality-control pathways in the cytosol as well as regulating transcription and histone methylation in the nucleus. Here we present a crystal structure of Bag6 and its cytoplasmic retention factor TRC35, revealing that TRC35 is remarkably conserved throughout the opisthokont lineage except at the C-terminal Bag6-binding groove, which evolved to accommodate Bag6, a unique metazoan factor...
October 31, 2017: Proceedings of the National Academy of Sciences of the United States of America
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