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  1. Article ; Online: Regulation of antigen receptor gene assembly by genetic-epigenetic crosstalk.

    Osipovich, Oleg / Oltz, Eugene M

    Seminars in immunology

    2010  Volume 22, Issue 6, Page(s) 313–322

    Abstract: Many aspects of gene function are coordinated by changes in the epigenome, which include dynamic revisions of chromatin modifications, genome packaging, subnuclear localization, and chromosome conformation. All of these mechanisms are used by developing ... ...

    Abstract Many aspects of gene function are coordinated by changes in the epigenome, which include dynamic revisions of chromatin modifications, genome packaging, subnuclear localization, and chromosome conformation. All of these mechanisms are used by developing lymphocytes to regulate the assembly of functional antigen receptor genes by V(D)J recombination. This somatic rearrangement of the genome must be tightly regulated to ensure proper B and T cell development and to avoid chromosomal translocations that cause lymphoid tumors. V(D)J recombination is controlled by a complex interplay between cis-acting regulatory elements that use transcription factors as liaisons to communicate with epigenetic pathways. Genetic-epigenetic crosstalk is a key strategy employed by precursor lymphocytes to modulate chromatin configurations at Ig and Tcr loci and thereby permit or deny access to a single V(D)J recombinase complex. This article describes our current knowledge of how genetic elements orchestrate crosstalk with epigenetic mechanisms to regulate recombinase accessibility via localized, regional, or long-range changes in chromatin.
    MeSH term(s) Animals ; Chromatin Assembly and Disassembly ; Epigenomics ; Gene Rearrangement, T-Lymphocyte ; Humans ; Receptors, Antigen, T-Cell/genetics
    Chemical Substances Receptors, Antigen, T-Cell
    Language English
    Publishing date 2010-09-15
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1018141-6
    ISSN 1096-3618 ; 1044-5323
    ISSN (online) 1096-3618
    ISSN 1044-5323
    DOI 10.1016/j.smim.2010.07.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Activation of Mouse

    Zhao, Jiang-Yang / Osipovich, Oleg / Koues, Olivia I / Majumder, Kinjal / Oltz, Eugene M

    Journal of immunology (Baltimore, Md. : 1950)

    2017  Volume 199, Issue 3, Page(s) 1131–1141

    Abstract: T lineage commitment requires the coordination of key transcription factors (TFs) in multipotent progenitors that transition them away from other lineages and cement T cell identity. Two important TFs for the multipotent progenitors to T lineage ... ...

    Abstract T lineage commitment requires the coordination of key transcription factors (TFs) in multipotent progenitors that transition them away from other lineages and cement T cell identity. Two important TFs for the multipotent progenitors to T lineage transition are RUNX1 and ETS1, which bind cooperatively to composite sites throughout the genome, especially in regulatory elements for genes involved in T lymphopoiesis. Activation of the TCR β (
    MeSH term(s) Animals ; Binding Sites/genetics ; Chromatin/immunology ; Chromatin/metabolism ; Core Binding Factor Alpha 2 Subunit/genetics ; Core Binding Factor Alpha 2 Subunit/metabolism ; Genome ; Mice ; Promoter Regions, Genetic ; Protein Binding ; Proto-Oncogene Protein c-ets-1/genetics ; Proto-Oncogene Protein c-ets-1/metabolism ; Receptors, Antigen, T-Cell, alpha-beta/immunology ; Receptors, Antigen, T-Cell, alpha-beta/metabolism ; Recombination, Genetic ; Thymocytes/immunology ; Thymocytes/metabolism
    Chemical Substances Chromatin ; Core Binding Factor Alpha 2 Subunit ; Ets1 protein, mouse ; Proto-Oncogene Protein c-ets-1 ; Receptors, Antigen, T-Cell, alpha-beta ; Runx1 protein, mouse
    Language English
    Publishing date 2017-06-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.1700146
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  3. Article: Accessibility control of V(D)J recombination.

    Cobb, Robin Milley / Oestreich, Kenneth J / Osipovich, Oleg A / Oltz, Eugene M

    Advances in immunology

    2006  Volume 91, Page(s) 45–109

    Abstract: Mammals contend with a universe of evolving pathogens by generating an enormous diversity of antigen receptors during lymphocyte development. Precursor B and T cells assemble functional immunoglobulin (Ig) and T cell receptor (TCR) genes via ... ...

    Abstract Mammals contend with a universe of evolving pathogens by generating an enormous diversity of antigen receptors during lymphocyte development. Precursor B and T cells assemble functional immunoglobulin (Ig) and T cell receptor (TCR) genes via recombination of numerous variable (V), diversity (D), and joining (J) gene segments. Although this combinatorial process generates significant diversity, genetic reorganization is inherently dangerous. Thus, V(D)J recombination must be tightly regulated to ensure proper lymphocyte development and avoid chromosomal translocations that cause lymphoid tumors. Each genomic rearrangement is mediated by a common V(D)J recombinase that recognizes sequences flanking all antigen receptor gene segments. The specificity of V(D)J recombination is due, in large part, to changes in the accessibility of chromatin at target gene segments, which either permits or restricts access to recombinase. The chromatin configuration of antigen receptor loci is governed by the concerted action of enhancers and promoters, which function as accessibility control elements (ACEs). In general, ACEs act as conduits for transcription factors, which in turn recruit enzymes that covalently modify or remodel nucleosomes. These ACE-mediated alterations are critical for activation of gene segment transcription and for opening chromatin associated with recombinase target sequences. In this chapter, we describe advances in understanding the mechanisms that control V(D)J recombination at the level of chromatin accessibility. The discussion will focus on cis-acting regulation by ACEs, the nuclear factors that control ACE function, and the epigenetic modifications that establish recombinase accessibility.
    MeSH term(s) Animals ; B-Lymphocytes/cytology ; Gene Rearrangement, B-Lymphocyte ; Gene Rearrangement, T-Lymphocyte ; Humans ; Receptors, Antigen, B-Cell/genetics ; Receptors, Antigen, T-Cell/genetics ; T-Lymphocytes/cytology ; VDJ Recombinases/genetics
    Chemical Substances Receptors, Antigen, B-Cell ; Receptors, Antigen, T-Cell ; VDJ Recombinases (EC 2.7.7.-)
    Language English
    Publishing date 2006
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 80226-8
    ISSN 1557-8445 ; 0065-2776
    ISSN (online) 1557-8445
    ISSN 0065-2776
    DOI 10.1016/S0065-2776(06)91002-5
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  4. Article ; Online: Cutting edge: SWI/SNF mediates antisense Igh transcription and locus-wide accessibility in B cell precursors.

    Osipovich, Oleg A / Subrahmanyam, Ramesh / Pierce, Steven / Sen, Ranjan / Oltz, Eugene M

    Journal of immunology (Baltimore, Md. : 1950)

    2009  Volume 183, Issue 3, Page(s) 1509–1513

    Abstract: The stepwise process of Ag receptor gene assembly, termed V(D)J recombination, is coordinated during lymphocyte development by sweeping changes in chromatin that permit or deny access to a single recombinase enzyme. We now show that switching/sucrose ... ...

    Abstract The stepwise process of Ag receptor gene assembly, termed V(D)J recombination, is coordinated during lymphocyte development by sweeping changes in chromatin that permit or deny access to a single recombinase enzyme. We now show that switching/sucrose nonfermenting (SWI/SNF) chromatin remodeling complexes are recruited to the Igh locus by an enhancer-dependent process and that these complexes are essential for generating recombinase accessibility throughout the locus. Depletion of SWI/SNF in pro-B cells also inhibits antisense transcription through all clusters of Igh gene segments, a pioneering process that has been implicated in the initial opening of chromatin. We conclude that SWI/SNF complexes play multiple roles in Igh gene assembly, ranging from initial locus activation to the spreading and maintenance of chromatin accessibility over large V(H), D(H), and J(H) domains.
    MeSH term(s) Animals ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/genetics ; DNA, Antisense/genetics ; Enhancer Elements, Genetic ; Genes, Immunoglobulin Heavy Chain/genetics ; Mice ; Precursor Cells, B-Lymphoid/metabolism ; Transcription Factors/genetics ; Transcription, Genetic ; VDJ Recombinases/metabolism
    Chemical Substances Chromosomal Proteins, Non-Histone ; DNA, Antisense ; SWI-SNF-B chromatin-remodeling complex ; Transcription Factors ; VDJ Recombinases (EC 2.7.7.-)
    Language English
    Publishing date 2009-07-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.0900896
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  5. Article: Targeting V(D)J recombinase: putting a PHD to work.

    Oltz, Eugene M / Osipovich, Oleg

    Immunity

    2007  Volume 27, Issue 4, Page(s) 539–541

    Abstract: In this issue of Immunity, Liu et al. (2007) show that V(D)J recombinase binds chromatin marked by H3K4 trimethylation. Because this mark associates with active promoters, the finding forges a new link between transcription, epigenetics, and recombinase ... ...

    Abstract In this issue of Immunity, Liu et al. (2007) show that V(D)J recombinase binds chromatin marked by H3K4 trimethylation. Because this mark associates with active promoters, the finding forges a new link between transcription, epigenetics, and recombinase targeting during lymphocyte development.
    MeSH term(s) Animals ; Epigenesis, Genetic ; Gene Rearrangement, T-Lymphocyte/genetics ; Genes, Immunoglobulin ; Humans ; Lymphocytes ; Models, Genetic ; Models, Immunological ; Transcription, Genetic ; VDJ Recombinases/metabolism
    Chemical Substances VDJ Recombinases (EC 2.7.7.-)
    Language English
    Publishing date 2007-10
    Publishing country United States
    Document type Comment ; Journal Article ; Review
    ZDB-ID 1217235-2
    ISSN 1097-4180 ; 1074-7613
    ISSN (online) 1097-4180
    ISSN 1074-7613
    DOI 10.1016/j.immuni.2007.10.001
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  6. Article ; Online: Functional intersection of ATM and DNA-dependent protein kinase catalytic subunit in coding end joining during V(D)J recombination.

    Lee, Baeck-Seung / Gapud, Eric J / Zhang, Shichuan / Dorsett, Yair / Bredemeyer, Andrea / George, Rosmy / Callen, Elsa / Daniel, Jeremy A / Osipovich, Oleg / Oltz, Eugene M / Bassing, Craig H / Nussenzweig, Andre / Lees-Miller, Susan / Hammel, Michal / Chen, Benjamin P C / Sleckman, Barry P

    Molecular and cellular biology

    2013  Volume 33, Issue 18, Page(s) 3568–3579

    Abstract: V(D)J recombination is initiated by the RAG endonuclease, which introduces DNA double-strand breaks (DSBs) at the border between two recombining gene segments, generating two hairpin-sealed coding ends and two blunt signal ends. ATM and DNA-dependent ... ...

    Abstract V(D)J recombination is initiated by the RAG endonuclease, which introduces DNA double-strand breaks (DSBs) at the border between two recombining gene segments, generating two hairpin-sealed coding ends and two blunt signal ends. ATM and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) are serine-threonine kinases that orchestrate the cellular responses to DNA DSBs. During V(D)J recombination, ATM and DNA-PKcs have unique functions in the repair of coding DNA ends. ATM deficiency leads to instability of postcleavage complexes and the loss of coding ends from these complexes. DNA-PKcs deficiency leads to a nearly complete block in coding join formation, as DNA-PKcs is required to activate Artemis, the endonuclease that opens hairpin-sealed coding ends. In contrast to loss of DNA-PKcs protein, here we show that inhibition of DNA-PKcs kinase activity has no effect on coding join formation when ATM is present and its kinase activity is intact. The ability of ATM to compensate for DNA-PKcs kinase activity depends on the integrity of three threonines in DNA-PKcs that are phosphorylation targets of ATM, suggesting that ATM can modulate DNA-PKcs activity through direct phosphorylation of DNA-PKcs. Mutation of these threonine residues to alanine (DNA-PKcs(3A)) renders DNA-PKcs dependent on its intrinsic kinase activity during coding end joining, at a step downstream of opening hairpin-sealed coding ends. Thus, DNA-PKcs has critical functions in coding end joining beyond promoting Artemis endonuclease activity, and these functions can be regulated redundantly by the kinase activity of either ATM or DNA-PKcs.
    MeSH term(s) Animals ; Ataxia Telangiectasia Mutated Proteins/chemistry ; Ataxia Telangiectasia Mutated Proteins/genetics ; Ataxia Telangiectasia Mutated Proteins/metabolism ; Catalytic Domain ; Cells, Cultured ; DNA Breaks, Double-Stranded ; DNA End-Joining Repair ; DNA-Activated Protein Kinase/chemistry ; DNA-Activated Protein Kinase/genetics ; DNA-Activated Protein Kinase/metabolism ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Endonucleases/metabolism ; Homeodomain Proteins/genetics ; Homeodomain Proteins/metabolism ; Mice ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Phosphorylation ; Precursor Cells, B-Lymphoid/metabolism ; Protein Interaction Domains and Motifs ; V(D)J Recombination
    Chemical Substances DNA-Binding Proteins ; Homeodomain Proteins ; Nuclear Proteins ; Rag2 protein, mouse ; RAG-1 protein (128559-51-3) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; Atm protein, mouse (EC 2.7.11.1) ; DNA-Activated Protein Kinase (EC 2.7.11.1) ; Prkdc protein, mouse (EC 2.7.11.1) ; Endonucleases (EC 3.1.-) ; Dclre1c protein, mouse (EC 3.1.-.-)
    Language English
    Publishing date 2013-07-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00308-13
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  7. Article: Targeted inhibition of V(D)J recombination by a histone methyltransferase.

    Osipovich, Oleg / Milley, Robin / Meade, Amber / Tachibana, Makoto / Shinkai, Yoichi / Krangel, Michael S / Oltz, Eugene M

    Nature immunology

    2004  Volume 5, Issue 3, Page(s) 309–316

    Abstract: The tissue- and stage-specific assembly of antigen receptor genes by V(D)J recombination is regulated by changes in the chromatin accessibility of target gene segments. This dynamic remodeling process is coordinated by cis-acting promoters and enhancers, ...

    Abstract The tissue- and stage-specific assembly of antigen receptor genes by V(D)J recombination is regulated by changes in the chromatin accessibility of target gene segments. This dynamic remodeling process is coordinated by cis-acting promoters and enhancers, which function as accessibility control elements. The basic epigenetic mechanisms that activate or repress chromatin accessibility to V(D)J recombinase remain unclear. We now demonstrate that a histone methyltransferase overrides accessibility control element function and cripples V(D)J recombination of chromosomal gene segments. The recruited histone methyltransferase induces extensive revisions in the local chromatin environment, including altered histone modifications and de novo methylation of DNA. These findings indicate a key function for histone methyltransferases in the tissue- and stage-specific suppression of antigen receptor gene assembly during lymphocyte development.
    MeSH term(s) Animals ; Cell Line ; Chromatin/enzymology ; DNA Methylation ; Gene Expression Regulation ; Gene Rearrangement, T-Lymphocyte ; Histone-Lysine N-Methyltransferase ; Histones/metabolism ; Immunoglobulin Fragments/genetics ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Variable Region/genetics ; Methyltransferases/physiology ; Mice ; Protein Methyltransferases ; Transcription, Genetic ; VDJ Recombinases/metabolism
    Chemical Substances Chromatin ; Histones ; Immunoglobulin Fragments ; Immunoglobulin Joining Region ; Immunoglobulin Variable Region ; Methyltransferases (EC 2.1.1.-) ; Protein Methyltransferases (EC 2.1.1.-) ; histone methyltransferase (EC 2.1.1.-) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; VDJ Recombinases (EC 2.7.7.-)
    Language English
    Publishing date 2004-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2016987-5
    ISSN 1529-2916 ; 1529-2908
    ISSN (online) 1529-2916
    ISSN 1529-2908
    DOI 10.1038/ni1042
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  8. Article: Synthesis, characterization, antifungal and anti-HIV activities of metal(II) complexes of 4,6-di-tert-butyl-3-[(2-hydroxyethyl)thio]benzene-1,2-diol.

    Loginova, Natalia V / Koval'chuk, Tat'yana V / Polozov, Genrikh I / Osipovich, Nikolai P / Rytik, Pyotr G / Kucherov, Igor I / Chernyavskaya, Anna A / Sorokin, Victor L / Shadyro, Oleg I

    European journal of medicinal chemistry

    2008  Volume 43, Issue 7, Page(s) 1536–1542

    Abstract: Co(II) and Ni(II) complexes with 4,6-di-tert-butyl-3-[(2-hydroxyethyl)thio]benzene-1,2-diol (L) have been synthesized and characterized by means of elemental analysis, TG/DTA, FT-IR, ESR, UV-vis, XRD, magnetic susceptibility, cyclic voltammetry and ... ...

    Abstract Co(II) and Ni(II) complexes with 4,6-di-tert-butyl-3-[(2-hydroxyethyl)thio]benzene-1,2-diol (L) have been synthesized and characterized by means of elemental analysis, TG/DTA, FT-IR, ESR, UV-vis, XRD, magnetic susceptibility, cyclic voltammetry and conductance measurements. According to the data obtained the organic compound acts as a bidentate O,S-coordinated ligand and yields Co(II) and Ni(II) complexes of the stoichiometry ML(2) which is characterized by square planar geometry. Antifungal and anti-HIV activities of the ligand and its metal(II) complexes were found to decrease in the sequence CuL(2)>CoL(2) ~ NiL(2)>HL, along with their reducing ability (determined electrochemically).
    MeSH term(s) Anti-HIV Agents/chemistry ; Anti-HIV Agents/pharmacology ; Antifungal Agents/chemistry ; Antifungal Agents/pharmacology ; Metals/chemistry ; Organometallic Compounds/chemical synthesis ; Organometallic Compounds/chemistry ; Organometallic Compounds/pharmacology ; Spectrum Analysis/methods
    Chemical Substances 4,6-di-tert-butyl-3-((2-hydroxyethyl)thio)benzene-1,2-diol-copper(II) ; Anti-HIV Agents ; Antifungal Agents ; Metals ; Organometallic Compounds
    Language English
    Publishing date 2008-07
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 188597-2
    ISSN 1768-3254 ; 0223-5234 ; 0009-4374
    ISSN (online) 1768-3254
    ISSN 0223-5234 ; 0009-4374
    DOI 10.1016/j.ejmech.2007.09.024
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  9. Article: Synthesis and biological evaluation of copper (II) complexes of sterically hindered o-aminophenol derivatives as antimicrobial agents.

    Loginova, Natalia V / Koval'chuk, Tat'yana V / Zheldakova, Rimma A / Osipovich, Nikolai P / Sorokin, Victor L / Polozov, Genrikh I / Ksendzova, Galina A / Glushonok, Gennady K / Chernyavskaya, Anna A / Shadyro, Oleg I

    Bioorganic & medicinal chemistry letters

    2006  Volume 16, Issue 20, Page(s) 5403–5407

    Abstract: Cu(II) complexes with 4,6-di(tert-butyl)-2-aminophenol (I) and 2-anilino-4,6-di(tert-butyl)phenol (II) have been synthesized and characterized by means of elemental analysis, TG/DTA, FT-IR, UV-vis, ESR, and conductance measurements. The compounds I and ... ...

    Abstract Cu(II) complexes with 4,6-di(tert-butyl)-2-aminophenol (I) and 2-anilino-4,6-di(tert-butyl)phenol (II) have been synthesized and characterized by means of elemental analysis, TG/DTA, FT-IR, UV-vis, ESR, and conductance measurements. The compounds I and II can coordinate in their singly deprotonated forms and behave as bidentate O,N-coordinated ligands; their CuL(2) complexes are characterized by CuN(2)O(2) coordination modes and square planar geometry. In vitro antimicrobial screening against Gram-positive and Gram-negative bacteria, yeasts, and moulds indicated that the compound I and its Cu(II) complex were more active than Questiomycin B, the compound II, and its Cu(II) complex.
    MeSH term(s) Aminophenols/chemistry ; Anti-Infective Agents/chemical synthesis ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/pharmacology ; Copper/chemistry ; In Vitro Techniques ; Microbial Sensitivity Tests ; Molecular Conformation ; Molecular Structure ; Organometallic Compounds/chemical synthesis ; Organometallic Compounds/chemistry ; Organometallic Compounds/pharmacology ; Structure-Activity Relationship
    Chemical Substances Aminophenols ; Anti-Infective Agents ; Organometallic Compounds ; 2-aminophenol (23RH73DZ65) ; Copper (789U1901C5)
    Language English
    Publishing date 2006-10-15
    Publishing country England
    Document type Journal Article
    ZDB-ID 1063195-1
    ISSN 1464-3405 ; 0960-894X
    ISSN (online) 1464-3405
    ISSN 0960-894X
    DOI 10.1016/j.bmcl.2006.07.065
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  10. Article ; Online: Functional Intersection of ATM and DNA-Dependent Protein Kinase Catalytic Subunit in Coding End Joining during V(D)J Recombination

    Lee, Baeck-Seung / Gapud, Eric J. / Zhang, Shichuan / Dorsett, Yair / Bredemeyer, Andrea / George, Rosmy / Callen, Elsa / Daniel, Jeremy A. / Osipovich, Oleg / Oltz, Eugene M. / Bassing, Craig H. / Nussenzweig, Andre / Lees-Miller, Susan / Hammel, Michal / Chen, Benjamin P. C. / Sleckman, Barry P.

    Molecular and Cellular Biology. 2013 Sept. 1, v. 33, no. 18 p.3568-3579

    2013  

    Abstract: V(D)J recombination is initiated by the RAG endonuclease, which introduces DNA double-strand breaks (DSBs) at the border between two recombining gene segments, generating two hairpin-sealed coding ends and two blunt signal ends. ATM and DNA-dependent ... ...

    Abstract V(D)J recombination is initiated by the RAG endonuclease, which introduces DNA double-strand breaks (DSBs) at the border between two recombining gene segments, generating two hairpin-sealed coding ends and two blunt signal ends. ATM and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) are serine-threonine kinases that orchestrate the cellular responses to DNA DSBs. During V(D)J recombination, ATM and DNA-PKcs have unique functions in the repair of coding DNA ends. ATM deficiency leads to instability of postcleavage complexes and the loss of coding ends from these complexes. DNA-PKcs deficiency leads to a nearly complete block in coding join formation, as DNA-PKcs is required to activate Artemis, the endonuclease that opens hairpin-sealed coding ends. In contrast to loss of DNA-PKcs protein, here we show that inhibition of DNA-PKcs kinase activity has no effect on coding join formation when ATM is present and its kinase activity is intact. The ability of ATM to compensate for DNA-PKcs kinase activity depends on the integrity of three threonines in DNA-PKcs that are phosphorylation targets of ATM, suggesting that ATM can modulate DNA-PKcs activity through direct phosphorylation of DNA-PKcs. Mutation of these threonine residues to alanine (DNA-PKcs³ᴬ) renders DNA-PKcs dependent on its intrinsic kinase activity during coding end joining, at a step downstream of opening hairpin-sealed coding ends. Thus, DNA-PKcs has critical functions in coding end joining beyond promoting Artemis endonuclease activity, and these functions can be regulated redundantly by the kinase activity of either ATM or DNA-PKcs.
    Keywords DNA ; alanine ; cell biology ; genes ; mutation ; phosphorylation ; protein kinases ; protein subunits ; threonine
    Language English
    Dates of publication 2013-0901
    Size p. 3568-3579.
    Publishing place Taylor & Francis
    Document type Article ; Online
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00308-13
    Database NAL-Catalogue (AGRICOLA)

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