Molecular Evolution and Functional Diversification of Replication Protein A1 in Plants
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Novel Roles of Replication Protein a Phosphorylation in Cellular Response to DNA Damage Moises A
East Tennessee State University Digital Commons @ East Tennessee State University Electronic Theses and Dissertations Student Works 8-2013 Novel Roles of Replication Protein A Phosphorylation in Cellular Response to DNA Damage Moises A. Serrano East Tennessee State University Follow this and additional works at: https://dc.etsu.edu/etd Part of the Biochemistry, Biophysics, and Structural Biology Commons, and the Laboratory and Basic Science Research Commons Recommended Citation Serrano, Moises A., "Novel Roles of Replication Protein A Phosphorylation in Cellular Response to DNA Damage" (2013). Electronic Theses and Dissertations. Paper 1206. https://dc.etsu.edu/etd/1206 This Dissertation - Open Access is brought to you for free and open access by the Student Works at Digital Commons @ East Tennessee State University. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of Digital Commons @ East Tennessee State University. For more information, please contact [email protected]. Novel Roles of Replication Protein A Phosphorylation in the Cellular Response to DNA Damage _____________________________ A dissertation presented to the faculty of the Department of Biomedical Science East Tennessee State University In partial fulfillment of the requirements for the degree Doctor of Philosophy in Biomedical Science _____________________________ by Moises Alejandro Serrano August 2013 _____________________________ Yue Zou, Ph.D., Chair Phillip R. Musich, Ph.D. Antonio E. Rusiñol, Ph.D. Michelle M. Duffourc, Ph.D. William L. Stone, Ph.D. Keywords: DNA Repair, DNA Damage Responses, RPA, p53, Apoptosis ABSTRACT Novel Roles of Replication Protein A Phosphorylation in Cellular Response to DNA Damage by Moises Alejandro Serrano Human replication protein A (RPA) is an eukaryotic single-stranded DNA binding protein directly involved in a variety of DNA metabolic pathways including replication, recombination, DNA damage checkpoints and signaling, as well as all DNA repair pathways. -
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. -
Gene Section Review
Atlas of Genetics and Cytogenetics in Oncology and Haematology OPEN ACCESS JOURNAL AT INIST-CNRS Gene Section Review RPA2 (replication protein A2, 32kDa) Anar KZ Murphy, James A Borowiec Dept of Biochemistry and New York University Cancer Institute, New York University School of Medicine, New York, New York 10016, USA (AKZM, JAB) Published in Atlas Database: April 2010 Online updated version : http://AtlasGeneticsOncology.org/Genes/RPA2ID42146ch1p35.html DOI: 10.4267/2042/44940 This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence. © 2011 Atlas of Genetics and Cytogenetics in Oncology and Haematology The coding sequence is contained within nine exons. Identity There is no confirmed alternative splicing of the RPA2 Other names: REPA2, RPA32 gene, or differential promoter usage. HGNC (Hugo): RPA2 Transcription Location: 1p35.3 The RPA2 mRNA transcript is 1.5 kb. The RPA2 Local order: The human RPA2 gene maps on 1p35.3 promoter contains four E2F consensus sequences between the SMPDL3B (sphingomyelin within the region about 400 bp upstream of the mRNA phosphodiesterase, acid-like 3B) and C1orf38 start site, and putative binding sites for ATF-1 and SP-1 (interferon-gamma inducible gene ICB-1 (induced by transcription factors. Expression is upregulated 2 to 3- contact to basement membrane)). fold by E2F, with mutation of the three start site- proximal E2F sites causing a loss of E2F DNA/RNA responsiveness (Kalma et al., 2001). Description Pseudogene The RPA2 gene is contained within 24.5 kb of RPA2 does not have known pseudogenes. chromosome 1. The sequence numbering corresponds to EMBL locus DQ001128 (26.6 kb). -
Identification of Novel Rpa-Protein Interactions Using the Yeast
IDENTIFICATION OF NOVEL RPA-PROTEIN INTERACTIONS USING THE YEAST TWO-HYBRID ASSAY AND IDENTIFICATION OF REGIONS IMPORTANT FOR INTERACTION BETWEEN RPA AND RAD24 A Thesis Submitted to the Graduate Faculty of the North Dakota State University of Agriculture and Applied Science By Gunjan Piya In Partial Fulfillment for the Degree of MASTER OF SCIENCE Major Department: Chemistry and Biochemistry July 2013 Fargo, North Dakota North Dakota State University Graduate School Title Identification of novel RPA-protein interactions using the yeast two-hybrid assay and identification of regions important for interaction between RPA and Rad24 By Gunjan Piya The Supervisory Committee certifies that this disquisition complies with North Dakota State University’s regulations and meets the accepted standards for the degree of MASTER OF SCIENCE SUPERVISORY COMMITTEE: Stuart J. Haring Chair Erika G. Offerdahl Glenn P. Dorsam Kendra J. Greenlee Approved: 7/25/2013 Gergory R. Cook Date Department Chair ABSTRACT Replication Protein A (RPA) [Replication Factor A (RFA) in yeast] is an ssDNA binding protein composed of Rpa1, Rpa2, and Rpa3 and involved in numerous DNA processing pathways such as Replication, Recombination, and Repair. It participates in such diverse pathways by its ability to interact with numerous proteins. The goal of my project was to find novel RPA-protein interactions using the yeast two hybrid assay. Using this method, we identified several known and unknown proteins that interact with Rfa1 and showed that these interactions were dependent on the phosphorylation state of Rfa2. Next, we determine the region important for interaction between Rfa1 and Rad24. Rad24 is a checkpoint protein important for initiation of the DNA damage checkpoint signaling. -
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 -
Replication Protein A2 Phosphorylation After DNA Damage by the Coordinated Action of Ataxia Telangiectasia-Mutated and DNA-Dependent Protein Kinase 1
[CANCER RESEARCH 61, 8554–8563, December 1, 2001] Replication Protein A2 Phosphorylation after DNA Damage by the Coordinated Action of Ataxia Telangiectasia-Mutated and DNA-dependent Protein Kinase 1 Hongyan Wang, Jun Guan, Huichen Wang, Ange Ronel Perrault, Ya Wang, and George Iliakis2 Department of Radiation Oncology, Kimmel Cancer Center, Jefferson Medical College, Philadelphia, Pennsylvania 19107 ABSTRACT RPA2 becomes hyperphosphorylated after exposure to IR, UV, certain chemotherapeutic agents, or inhibitors of DNA replication, Replication protein A (RPA, also known as human single-stranded implicating RPA modification in the cellular responses to DNA dam- DNA-binding protein) is a trimeric, multifunctional protein complex in- age (9–17). Identification of the kinases that phosphorylate RPA2 volved in DNA replication, DNA repair, and recombination. Phosphoryl- ation of the RPA2 subunit is observed after exposure of cells to ionizing after DNA damage as well as throughout the cell cycle is important radiation (IR) and other DNA-damaging agents, which implicates the for an understanding of the functions and the putative regulatory modified protein in the regulation of DNA replication after DNA damage properties of the protein. Evidence exists that certain cdk-cyclin or in DNA repair. Although ataxia telangiectasia-mutated (ATM) and complexes mediate some of the modifications observed during the DNA-dependent protein kinase (DNA-PK) phosphorylate RPA2 in vitro, progression of cells through the cell cycle (6, 7, 18–22). Other kinases their role in vivo remains uncertain, and contradictory results have been have been implicated in the phosphorylation of RPA2 after DNA reported. Here we show that RPA2 phosphorylation is delayed in cells damage. -
A Conserved but Plant-Specific CDK-Mediated Regulation of DNA Replication Protein A2 in the Precise Control of Stomatal Terminal Division
A conserved but plant-specific CDK-mediated regulation of DNA replication protein A2 in the precise control of stomatal terminal division Kezhen Yanga, Lingling Zhua,b, Hongzhe Wanga, Min Jianga, Chunwang Xiaoc,d, Xiangyang Hue, Steffen Vannestef,g,h, Juan Dongi, and Jie Lea,b,1 aKey Laboratory of Plant Molecular Physiology, CAS Center for Excellence in Molecular Plant Sciences, Institute of Botany, Chinese Academy of Sciences, 100093 Beijing, China; bUniversity of Chinese Academy of Sciences, 100049 Beijing, China; cCollege of Life and Environmental Sciences, Minzu University of China, 100081 Beijing, China; dHulun Lake Reserve Grassland Ecology Research Station, Minzu University of China, 100081 Beijing, China; eShanghai Key Laboratory of Bio-Energy Crops, School of Life Sciences, Shanghai University, 200444 Shanghai, China; fCenter for Plant Systems Biology, VIB, 9052 Ghent, Belgium; gDepartment of Plant Biotechnology and Bioinformatics, Ghent University, 9052 Ghent, Belgium; hLaboratory of Plant Growth Analysis, Ghent University Global Campus, 21985 Incheon, Republic of Korea; and iWaksman Institute of Microbiology, Rutgers, The State University of New Jersey, Piscataway, NJ 08854 Edited by David C. Baulcombe, University of Cambridge, Cambridge, United Kingdom, and approved July 29, 2019 (received for review November 11, 2018) The R2R3-MYB transcription factor FOUR LIPS (FLP) controls the condition, RPA2 is hyperphosphorylated by the PIKK-family stomatal terminal division through transcriptional repression of kinases (ATM, ATR, and DNA-PK) that facilitates mitotic exit the cell cycle genes CYCLIN-DEPENDENT KINASE (CDK) B1s (CDKB1s), and the initiation of DNA repair (13–15). All known RPA2 CDKA;1,andCYCLIN A2s (CYCA2s). We mutagenized the weak mu- homologs have a conserved N-terminal phosphorylation domain, tant allele flp-1 seeds with ethylmethane sulfonate and screened although the specific residues may be not conserved in different out a flp-1 suppressor 1 (fsp1) that suppressed the flp-1 stomatal species (11). -
ROR1/RPA2A, a Putative Replication Protein A2, Functions in Epigenetic Gene Silencing and in Regulation of Meristem Development in Arabidopsis W
The Plant Cell, Vol. 18, 85–103, January 2006, www.plantcell.org ª 2005 American Society of Plant Biologists ROR1/RPA2A, a Putative Replication Protein A2, Functions in Epigenetic Gene Silencing and in Regulation of Meristem Development in Arabidopsis W Ran Xia,a,1 Junguo Wang,a,1 Chunyan Liu,b Yu Wang,a Youqun Wang,a Jixian Zhai,b Jun Liu,a Xuhui Hong,a Xiaofeng Cao,b Jian-Kang Zhu,c and Zhizhong Gonga,2 a State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing, 100094, China b Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China c Department of Botany and Plant Sciences, Institute of Integrative Genome Biology, University of California, Riverside, California 92521 We screened for suppressors of repressor of silencing1 (ros1) using the silenced 35S promoter-neomycin phosphotrans- ferase II (Pro35S:NPTII) gene as a marker and identified two allelic mutants, ror1-1 and ror1-2 (for suppressor of ros1). Map- based cloning revealed that ROR1 encodes a 31-kD protein similar to DNA replication protein A2 (RPA2A). Mutations in ROR1 reactivate the silenced Pro35S:NPTII gene but not RD29A promoter-luciferase in the ros1 mutant. DNA methylation in rDNA, centromeric DNA, and RD29A promoter regions is not affected by ror1. However, chromatin immunoprecipitation data suggest that histone H3 acetylation is increased and histone H3K9 dimethylation is decreased in the 35S promoter in the ror1 ros1 mutant compared with ros1. These results indicate that release of silenced Pro35S:NPTII by ror1 mutations is independent of DNA methylation. -
A Dynamic Model for Replication Protein a (RPA) Function in DNA Processing Pathways Ellen Fanning*, Vitaly Klimovich and Andrew R
4126–4137 Nucleic Acids Research, 2006, Vol. 34, No. 15 Published online 25 August 2006 doi:10.1093/nar/gkl550 SURVEY AND SUMMARY A dynamic model for replication protein A (RPA) function in DNA processing pathways Ellen Fanning*, Vitaly Klimovich and Andrew R. Nager Department of Biological Sciences, Vanderbilt University, VU Station B 351634, Nashville, TN 37235-1634, USA Received April 3, 2006; Revised June 23, 2006; Accepted July 14, 2006 ABSTRACT ssDNA that would interfere with DNA processing, but it also appears to actively coordinate the sequential assembly Processing of DNA in replication, repair and and disassembly of DNA processing proteins on ssDNA recombination pathways in cells of all organisms (16,17). The ability of RPA to guide DNA processing requires the participation of at least one major depends in large part on RPA interactions with other proteins single-stranded DNA (ssDNA)-binding protein. This in each pathway. Although these mechanisms are not yet well protein protects ssDNA from nucleolytic damage, understood, we will review here several examples and discuss prevents hairpin formation and blocks DNA rean- possible models for protein-mediated RPA conformation nealing until the processing pathway is successfully changes that may underlie its assembly and disassembly on completed. Many ssDNA-binding proteins interact ssDNA. physically and functionally with a variety of other DNA processing proteins. These interactions are thought to temporally order and guide the parade of RPA: A MODULAR PROTEIN WITH MULTIPLE proteins that ‘trade places’ on the ssDNA, a model CONFORMATIONS known as ‘hand-off’, as the processing pathway RPA is a stable complex of three subunits RPA70, RPA32 progresses. -
Supplementary Table 2
Supplementary Table 2. Differentially Expressed Genes following Sham treatment relative to Untreated Controls Fold Change Accession Name Symbol 3 h 12 h NM_013121 CD28 antigen Cd28 12.82 BG665360 FMS-like tyrosine kinase 1 Flt1 9.63 NM_012701 Adrenergic receptor, beta 1 Adrb1 8.24 0.46 U20796 Nuclear receptor subfamily 1, group D, member 2 Nr1d2 7.22 NM_017116 Calpain 2 Capn2 6.41 BE097282 Guanine nucleotide binding protein, alpha 12 Gna12 6.21 NM_053328 Basic helix-loop-helix domain containing, class B2 Bhlhb2 5.79 NM_053831 Guanylate cyclase 2f Gucy2f 5.71 AW251703 Tumor necrosis factor receptor superfamily, member 12a Tnfrsf12a 5.57 NM_021691 Twist homolog 2 (Drosophila) Twist2 5.42 NM_133550 Fc receptor, IgE, low affinity II, alpha polypeptide Fcer2a 4.93 NM_031120 Signal sequence receptor, gamma Ssr3 4.84 NM_053544 Secreted frizzled-related protein 4 Sfrp4 4.73 NM_053910 Pleckstrin homology, Sec7 and coiled/coil domains 1 Pscd1 4.69 BE113233 Suppressor of cytokine signaling 2 Socs2 4.68 NM_053949 Potassium voltage-gated channel, subfamily H (eag- Kcnh2 4.60 related), member 2 NM_017305 Glutamate cysteine ligase, modifier subunit Gclm 4.59 NM_017309 Protein phospatase 3, regulatory subunit B, alpha Ppp3r1 4.54 isoform,type 1 NM_012765 5-hydroxytryptamine (serotonin) receptor 2C Htr2c 4.46 NM_017218 V-erb-b2 erythroblastic leukemia viral oncogene homolog Erbb3 4.42 3 (avian) AW918369 Zinc finger protein 191 Zfp191 4.38 NM_031034 Guanine nucleotide binding protein, alpha 12 Gna12 4.38 NM_017020 Interleukin 6 receptor Il6r 4.37 AJ002942 -
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.