Functional Diversification of Replication Protein A
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How Shelterin Protects Mammalian Telomeres 303 ANRV361-GE42-15 ARI 3 October 2008 10:10 (See 3' 5' TRF2 S Mplex
ANRV361-GE42-15 ARI 3 October 2008 10:10 ANNUAL How Shelterin Protects REVIEWS Further Click here for quick links to Annual Reviews content online, Mammalian Telomeres including: • Other articles in this volume 1 • Top cited articles Wilhelm Palm and Titia de Lange • Top downloaded articles • Our comprehensive search Laboratory for Cell Biology and Genetics, The Rockefeller University, New York, NY 10021; email: [email protected] 1Current address: Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany Annu. Rev. Genet. 2008. 42:301–34 Key Words First published online as a Review in Advance on ATM, ATR, cancer, NHEJ, HR August 4, 2008 by Rockefeller University on 10/13/09. For personal use only. The Annual Review of Genetics is online at Abstract genet.annualreviews.org The genomes of prokaryotes and eukaryotic organelles are usually cir- This article’s doi: cular as are most plasmids and viral genomes. In contrast, the nuclear Annu. Rev. Genet. 2008.42:301-334. Downloaded from arjournals.annualreviews.org 10.1146/annurev.genet.41.110306.130350 genomes of eukaryotes are organized on linear chromosomes, which Copyright c 2008 by Annual Reviews. require mechanisms to protect and replicate DNA ends. Eukaryotes All rights reserved navigate these problemswith the advent of telomeres, protective nucle- 0066-4197/08/1201-0301$20.00 oprotein complexes at the ends of linear chromosomes, and telomerase, the enzyme that maintains the DNA in these structures. Mammalian telomeres contain a specific protein complex, shelterin, that functions to protect chromosome ends from all aspects of the DNA damage re- sponse and regulates telomere maintenance by telomerase. -
Ailanthone Inhibits Non-Small Cell Lung Cancer Cell Growth Through Repressing DNA Replication Via Downregulating RPA1
FULL PAPER British Journal of Cancer (2017) 117, 1621–1630 | doi: 10.1038/bjc.2017.319 Keywords: ailanthone; non-small cell lung cancer; DNA replication; RPA1; Chinese medicine Ailanthone inhibits non-small cell lung cancer cell growth through repressing DNA replication via downregulating RPA1 Zhongya Ni1, Chao Yao1, Xiaowen Zhu1, Chenyuan Gong1, Zihang Xu2, Lixin Wang3, Suyun Li4, Chunpu Zou2 and Shiguo Zhu*,1,3 1Laboratory of Integrative Medicine, School of Basic Medical Sciences, Shanghai University of Traditional Chinese Medicine, 1200 Cai Lun Rd, Shanghai 201203, PR China; 2Department of Internal Classic of Medicine, School of Basic Medical Sciences, Shanghai University of Traditional Chinese Medicine, 1200 Cai Lun Rd, Shanghai 201203, PR China; 3Department of Immunology and Pathogenic Biology, School of Basic Medical Sciences, Shanghai University of Traditional Chinese Medicine, 1200 Cai Lun Rd, Shanghai 201203, PR China and 4Department of Pathology, School of Basic Medical Sciences, Shanghai University of Traditional Chinese Medicine, 1200 Cai Lun Rd, Shanghai 201203, PR China Background: The identification of bioactive compounds from Chinese medicine plays a crucial role in the development of novel reagents against non-small cell lung cancer (NSCLC). Methods: High throughput screening assay and analyses of cell growth, cell cycle, apoptosis, cDNA microarray, BrdU incorporation and gene expression were performed. Results: Ailanthone (Aila) suppressed NSCLC cell growth and colony formation in vitro and inhibited NSCLC tumour growth in subcutaneously xenografted and orthotopic lung tumour models, leading to prolonged survival of tumour-bearing mice. Moreover, Aila induced cell cycle arrest in a dose-independent manner but did not induce apoptosis in all NSCLC cells. -
Dyskerin Mutations Present in Dyskeratosis Congenita Patients Increase Oxidative Stress and DNA Damage Signalling in Dictyostelium Discoideum
cells Article Dyskerin Mutations Present in Dyskeratosis Congenita Patients Increase Oxidative Stress and DNA Damage Signalling in Dictyostelium Discoideum Javier Rodriguez-Centeno, Rosario Perona and Leandro Sastre * Instituto de Investigaciones Biomedicas, CSIC/UAM and Centro de Investigación Biomédica en Red de Enfermedades Raras, CIBERER, 28029 Madrid, Spain; [email protected] (J.R.-C.); [email protected] (R.P.) * Correspondence: [email protected]; Tel.: +3491-585-4437 Received: 11 October 2019; Accepted: 5 November 2019; Published: 8 November 2019 Abstract: Dyskerin is a protein involved in the formation of small nucleolar and small Cajal body ribonucleoproteins. These complexes participate in RNA pseudouridylation and are also components of the telomerase complex required for telomere elongation. Dyskerin mutations cause a rare disease, X-linked dyskeratosis congenita, with no curative treatment. The social amoeba Dictyostelium discoideum contains a gene coding for a dyskerin homologous protein. In this article D. discoideum mutant strains that have mutations corresponding to mutations found in dyskeratosis congenita patients are described. The phenotype of the mutant strains has been studied and no alterations were observed in pseudouridylation activity and telomere structure. Mutant strains showed increased proliferation on liquid culture but reduced growth feeding on bacteria. The results obtained indicated the existence of increased DNA damage response and reactive oxygen species, as also reported in human Dyskeratosis congenita cells and some other disease models. These data, together with the haploid character of D. discoideum vegetative cells, that resemble the genomic structure of the human dyskerin gene, located in the X chromosome, support the conclusion that D. discoideum can be a good model system for the study of this disease. -
Transcription-Replication Collisions—A Series of Unfortunate Events
biomolecules Review Transcription-Replication Collisions—A Series of Unfortunate Events Commodore St Germain 1,2,*, Hongchang Zhao 2 and Jacqueline H. Barlow 2,* 1 School of Mathematics and Science, Solano Community College, 4000 Suisun Valley Road, Fairfield, CA 94534, USA 2 Department of Microbiology and Molecular Genetics, University of California Davis, One Shields Avenue, Davis, CA 95616, USA; [email protected] * Correspondence: [email protected] (C.S.G.); [email protected] (J.H.B.) Abstract: Transcription-replication interactions occur when DNA replication encounters genomic regions undergoing transcription. Both replication and transcription are essential for life and use the same DNA template making conflicts unavoidable. R-loops, DNA supercoiling, DNA secondary structure, and chromatin-binding proteins are all potential obstacles for processive replication or transcription and pose an even more potent threat to genome integrity when these processes co-occur. It is critical to maintaining high fidelity and processivity of transcription and replication while navigating through a complex chromatin environment, highlighting the importance of defining cellular pathways regulating transcription-replication interaction formation, evasion, and resolution. Here we discuss how transcription influences replication fork stability, and the safeguards that have evolved to navigate transcription-replication interactions and maintain genome integrity in mammalian cells. Keywords: DNA replication; transcription; R-loops; replication stress Citation: St Germain, C.; Zhao, H.; Barlow, J.H. Transcription-Replication Collisions—A Series of Unfortunate Events. Biomolecules 2021, 11, 1249. 1. Introduction https://doi.org/10.3390/ From bacteria to humans, transcription has been identified as a source of genome biom11081249 instability, initially observed as spontaneous recombination referred to as transcription- associated recombination (TAR) [1]. -
Clipped Histone H3 Is Integrated Into Nucleosomes of DNA Replication
Clipped histone H3 is integrated into nucleosomes of DNA replication genes in the human malaria parasite Plasmodium falciparum Abril Marcela Herrera-solorio, Shruthi Sridhar Vembar, Cameron Ross Macpherson, Daniela Lozano-amado, Gabriela Romero Meza, Beatriz Xoconostle-cazares, Rafael Miyazawa Martins, Patty Chen, Miguel Vargas, Artur Scherf, et al. To cite this version: Abril Marcela Herrera-solorio, Shruthi Sridhar Vembar, Cameron Ross Macpherson, Daniela Lozano- amado, Gabriela Romero Meza, et al.. Clipped histone H3 is integrated into nucleosomes of DNA replication genes in the human malaria parasite Plasmodium falciparum. EMBO Reports, EMBO Press, 2019, 20 (4), pp.e46331. 10.15252/embr.201846331. hal-02321832 HAL Id: hal-02321832 https://hal.archives-ouvertes.fr/hal-02321832 Submitted on 9 Sep 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution| 4.0 International License Scientific Report Clipped histone H3 is integrated into nucleosomes of DNA replication genes in the human malaria parasite -
Anti-RPA1 Monoclonal Antibody, Clone 3I21 (DCABH-3680) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-RPA1 Monoclonal antibody, clone 3I21 (DCABH-3680) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Mouse monoclonal to RPA70 Antigen Description Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange. Immunogen Purified Human RPA70 protein Isotype IgG1 Source/Host Mouse Species Reactivity Human Clone 3I21 Purity Protein G purified Conjugate Unconjugated Applications WB, IP Positive Control HeLa cells Format Liquid Size 500 μl Buffer pH: 7.40; Preservative: 0.09% Sodium azide; Constituents: 99% PBS, 0.02% BSA Preservative 0.09% Sodium Azide Storage Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle. 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics -
Single-Molecule Analysis of the Human Telomerase RNA Center Dot Dyskerin Interaction and the Effect of Dyskeratosis Congenita Mu
Single-Molecule Analysis of the Human Telomerase RNA center dot Dyskerin Interaction and the Effect of Dyskeratosis Congenita Mutations Ashbridge, B; Orte, A; Yeoman, JA; Kirwan, M; Vulliamy, T; Dokal, I; Klenerman, D; Balasubramanian, S © 2009 American Chemical Society http://pubs.acs.org/page/policy/authorchoice_termsofuse.html For additional information about this publication click this link. http://qmro.qmul.ac.uk/xmlui/handle/123456789/14851 Information about this research object was correct at the time of download; we occasionally make corrections to records, please therefore check the published record when citing. For more information contact [email protected] 10858 Biochemistry 2009, 48, 10858–10865 DOI: 10.1021/bi901373e Single-Molecule Analysis of the Human Telomerase RNA 3 Dyskerin Interaction and the Effect of Dyskeratosis Congenita Mutations† Beth Ashbridge,‡,^ Angel Orte,‡,^,@ Justin A. Yeoman,‡,^,# Michael Kirwan, ) Tom Vulliamy, ) Inderjeet Dokal, ) David Klenerman,*,‡,r and Shankar Balasubramanian*,‡,§,r ‡University Chemical Laboratories, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., §School of Clinical Medicine, University of Cambridge, Cambridge CB2 0SP, U.K., and Centre) for Paediatrics, Institute of Cell and Molecular Science, Barts and The London School of Medicine and Dentistry, Queen Mary, University of London, London E1 2AT, U.K. ^These authors contributed equally to this work. @Present address: Department of Physical Chemistry, Faculty of Pharmacy, Campus Cartuja, Granada 18071, Spain. #Present address: National Centre for Biological Sciences, Tata Institute of Fundamental Research, UAS GKVK, Bellary Road, Bangalore 560 065, India. rJoint senior authorship. Received August 7, 2009; Revised Manuscript Received October 1, 2009 ABSTRACT: It has been proposed that human telomerase RNA (hTR) interacts with dyskerin, prior to assembly of the telomerase holoenzyme. -
Transcriptome-Wide Profiling of Multiple RNA Modifications Simultaneously at Single-Base Resolution,” by Vahid Khoddami, Archana Yerra, Timothy L
Correction BIOCHEMISTRY, CHEMISTRY Correction for “Transcriptome-wide profiling of multiple RNA modifications simultaneously at single-base resolution,” by Vahid Khoddami, Archana Yerra, Timothy L. Mosbruger, Aaron M. Fleming, Cynthia J. Burrows, and Bradley R. Cairns, which was first published March 14, 2019; 10.1073/pnas.1817334116 (Proc Natl Acad Sci USA 116:6784–6789). The authors note that the following statement should be added to the Acknowledgments: “This work was also supported by Grant R01 GM093099 from the NIH/National Institute of General Medical Sciences (to C.J.B.).” Published under the PNAS license. Published online April 22, 2019. www.pnas.org/cgi/doi/10.1073/pnas.1905628116 9136 | PNAS | April 30, 2019 | vol. 116 | no. 18 www.pnas.org Downloaded by guest on October 2, 2021 Transcriptome-wide profiling of multiple RNA modifications simultaneously at single-base resolution Vahid Khoddamia,b,c,1,2, Archana Yerrab,c,1, Timothy L. Mosbrugerd, Aaron M. Fleminge, Cynthia J. Burrowse,3, and Bradley R. Cairnsb,c,3 aDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115; bHoward Hughes Medical Institute, University of Utah School of Medicine, Salt Lake City, UT 84112; cDepartment of Oncological Sciences, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112; dBioinformatics Shared Resource, Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City, UT 84112; and eDepartment of Chemistry, University of Utah, Salt Lake City, UT 84112 Contributed by Cynthia J. Burrows, January 25, 2019 (sent for review October 9, 2018; reviewed by Juan D. Alfonzo, Thomas Carell, and Peter C. -
CHK1 Inhibition Is Synthetically Lethal with Loss of B-Family DNA Polymerase Function in Human Lung and Colorectal Cancer Cells
Author Manuscript Published OnlineFirst on March 11, 2020; DOI: 10.1158/0008-5472.CAN-19-1372 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. 1 Title: CHK1 inhibition is synthetically lethal with loss of B-family DNA polymerase function in human lung and colorectal cancer cells. Author List: Rebecca F. Rogers1, Mike I. Walton1, Daniel L. Cherry2, Ian Collins1, Paul A. Clarke1, Michelle D. Garrett2* and Paul Workman1* Affiliations: 1Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London, SM2 5NG, UK 2 School of Biosciences, Stacey Building, University of Kent, Canterbury, Kent, CT2 7NJ, UK Running title: Synthetic lethality of CHK1 and DNA polymerase inhibition *Corresponding authors: Michelle D Garrett and Paul Workman Corresponding Author Information Michelle D Garrett School of Biosciences, Stacey Building, University of Kent, Canterbury, Kent, CT2 7NJ, UK. Email: [email protected] Phone: +44 (0)1227 816140 Paul Workman Cancer Research UK Cancer Therapeutics Unit, The Institute of Cancer Research, London, SM2 5NG, UK. Email: [email protected] Phone: +44 (0)20 7153 5209 Conflict of interest statement: IC, MDG, MIW, RFR, PC and PW are current or past employees of The Institute of Cancer Research, which has a commercial interest in the discovery and development of CHK1 inhibitors, including SRA737, and operates a rewards-to- inventors scheme. IC, MDG and MIW have been involved in a commercial collaboration on CHK1 inhibitors with Sareum Ltd and intellectual property arising from the program, including SRA737, was licensed to Sierra Oncology. IC is a consultant for Sierra Oncology, Adorx Ltd, Epidarex LLP and Enterprise Therapeutics Ltd and holds equity in Monte Rosa Therapeutics AG. -
Qt38n028mr Nosplash A3e1d84
! ""! ACKNOWLEDGEMENTS I dedicate this thesis to my parents who inspired me to become a scientist through invigorating scientific discussions at the dinner table even when I was too young to understand what the hippocampus was. They also prepared me for the ups and downs of science and supported me through all of these experiences. I would like to thank my advisor Dr. Elizabeth Blackburn and my thesis committee members Dr. Eric Verdin, and Dr. Emmanuelle Passegue. Liz created a nurturing and supportive environment for me to explore my own ideas, while at the same time teaching me how to love science, test my questions, and of course provide endless ways to think about telomeres and telomerase. Eric and Emmanuelle both gave specific critical advice about the proper experiments for T cells and both volunteered their lab members for further critical advice. I always felt inspired with a sense of direction after thesis committee meetings. The Blackburn lab is full of smart and dedicated scientists whom I am thankful for their support. Specifically Dr. Shang Li and Dr. Brad Stohr for their stimulating scientific debates and “arguments.” Dr. Jue Lin, Dana Smith, Kyle Lapham, Dr. Tet Matsuguchi, and Kyle Jay for their friendships and discussions about what my data could possibly mean. Dr. Eva Samal for teaching me molecular biology techniques and putting up with my late night lab exercises. Beth Cimini for her expertise with microscopy, FACs, singing, and most of all for being a caring and supportive friend. Finally, I would like to thank Dr. Imke Listerman, my scientific partner for most of the breast cancer experiments. -
Expression of an Ortholog of Replication Protein A1 (RPA1)
Proc. Natl. Acad. Sci. USA Vol. 94, pp. 9979–9983, September 1997 Plant Biology Expression of an ortholog of replication protein A1 (RPA1) is induced by gibberellin in deepwater rice (cell divisionyintercalary meristemyinternodal growthyOryza sativa) ESTHER VAN DER KNAAP*, SANDRINE JAGOUEIX*†, AND HANS KENDE‡ Michigan State University–Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824-1312 Contributed by Hans Kende, July 16, 1997 ABSTRACT Internodes of deepwater rice are induced to antagonist of GA action in rice (6). Growth of the internode grow rapidly when plants become submerged. This adaptation is, ultimately, promoted by GA (5). enables deepwater rice to keep part of its foliage above the The primary target tissue of GA is the intercalary meristem rising flood waters during the monsoon season and to avoid of the internode, where GA enhances cell division activity and drowning. This growth response is, ultimately, elicited by the cell elongation (5, 7, 8). The intercalary meristem is a zone of plant hormone gibberellin (GA). The primary target tissue for about 3 mm in length and is located at the base of the internode GA action is the intercalary meristem of the internode. Using (9). Cells are displaced from the intercalary meristem into the differential display of mRNA, we have isolated a number of elongation zone, where they reach their final size. In GA- genes whose expression in the intercalary meristem is regu- treated internodes, the final cell length is about three to four lated by GA. The product of one of these genes was identified times longer than in control internodes (5, 7). -
Monitoring Replication Protein a (RPA) Dynamics in Homologous
Marquette University e-Publications@Marquette Biological Sciences Faculty Research and Biological Sciences, Department of Publications 9-19-2017 Monitoring Replication Protein A (RPA) Dynamics in Homologous Recombination Through Site-specific ncorI poration of Non- canonical Amino Acids Nilisha Pokhrel Marquette University Sofia Origanti Marquette University, [email protected] Eric Parker Davenport Marquette University Disha M. Gandhi Marquette University Kyle Kaniecki Columbia University See next page for additional authors Published version. Nucleic Acids Research, Vol. 45, No. 16 (September 19, 2017): 9413-9426. DOI. Authors Nilisha Pokhrel, Sofia Origanti, Eric Parker Davenport, Disha M. Gandhi, Kyle Kaniecki, Ryan A. Mehl, Eric C. Greene, Chris Dockendorff, and Edwin Antony This article is available at e-Publications@Marquette: https://epublications.marquette.edu/bio_fac/603 Published online 12 July 2017 Nucleic Acids Research, 2017, Vol. 45, No. 16 9413–9426 doi: 10.1093/nar/gkx598 Monitoring Replication Protein A (RPA) dynamics in homologous recombination through site-specific incorporation of non-canonical amino acids Nilisha Pokhrel1, Sofia Origanti1, Eric Parker Davenport1, Disha Gandhi2, Kyle Kaniecki3,4, Ryan A. Mehl5, Eric C. Greene3, Chris Dockendorff2 and Edwin Antony1,* 1Department of Biological Sciences, Marquette University, Milwaukee, WI 53201, USA, 2Department of Chemistry, Marquette University, Milwaukee, WI 53201, USA, 3Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY