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  • The American Association of Immunologists  (5)
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  • The American Association of Immunologists  (5)
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  • 1
    Online Resource
    Online Resource
    Pax5 control the B lineage specific gene expression program through association with the nuclear matrix (153.14)
    The American Association of Immunologists ; 2011
    In:  The Journal of Immunology Vol. 186, No. 1_Supplement ( 2011-04-01), p. 153.14-153.14
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 186, No. 1_Supplement ( 2011-04-01), p. 153.14-153.14
    Abstract: Accumulating studies indicate that the nuclear matrix provides a dynamic structural support for various biological reactions inside of nuclei such as DNA replication, RNA transcription, and RNA splicing. Pax5 is an important regulator for B lineage cell development, which controls the B lineage specific gene expression program involving hundreds of positive and negative target genes. Here, we show that majority of the endogenous Pax5 proteins in human and murine B lineage cells are associated with the nuclear matrix, where they occupy the centers for transcription on the nuclear matrix as indicated by co-localization with the RNA polymerase II or the TATA box binding protein (TBP). Detailed analyses identified that two different domains of Pax5 are required for its association with the nuclear matrix. Interestingly, lysine 67, 87, and 89 residues within the PRD domain of Pax5 are essential for its association with the nuclear matrix. Microarray analysis showed that mutation of these lysine residues compromise Pax5 mediated activation and repression of hundreds target genes. Furthermore, chromatin immunoprecipitation (ChIP) and nuclear matrix foot printing assays indicated that Pax5 is responsible for recruitment of Cd19 loci to the nuclear matrix bound RNA polymerase complex. These results demonstrate that association with the nuclear matrix is essential for Pax5 to control the B lineage specific gene expression program.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.186.Supp.153.14
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2011
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    The V(D)J recombination machinery is associated with the nuclear matrix (88.3)
    The American Association of Immunologists ; 2010
    In:  The Journal of Immunology Vol. 184, No. 1_Supplement ( 2010-04-01), p. 88.3-88.3
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 184, No. 1_Supplement ( 2010-04-01), p. 88.3-88.3
    Abstract: Somatic recombination of immunoglobulin or T cell antigen receptor genes occurs through recombination activating gene product (RAG)-mediated cleavage at recombination signal sequences (RSS) and subsequently, the broken DNA ends are repaired by non-homologue end joining (NHEJ) enzymes. Here, we show that RAG1, RAG2, and many NHEJ factors in B lineage cells are associated with the nuclear matrix. The core RAG1 and RAG2 proteins have their own nuclear matrix targeting regions. RAG-mediated double stranded DNA breaks at the Jκ4 RSS can be readily detected in the nuclear matrix fraction in Gleevec treated Abelson transformed murine B cells or mouse bone marrow cells, indicating that the recombination reaction is ongoing on the nuclear matrix. In the HEK 293 cell-based recombination system, artificial recombination substrates are recruited to the nuclear matrix for recombination. Moreover, nuclear matrix proteins purified from 293 cells expressing the core RAG proteins or human B lineage cells expressing endogenous RAG proteins support cleavage of RSS substrates in vitro. Based on these results, we propose that the V(D)J recombination machinery is associated with the nuclear matrix.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.184.Supp.88.3
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2010
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Regulation of VH Replacement by B Cell Receptor–Mediated Signaling in Human Immature B Cells
    The American Association of Immunologists ; 2013
    In:  The Journal of Immunology Vol. 190, No. 11 ( 2013-06-01), p. 5559-5566
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 190, No. 11 ( 2013-06-01), p. 5559-5566
    Abstract: VH replacement provides a unique RAG-mediated recombination mechanism to edit nonfunctional IgH genes or IgH genes encoding self-reactive BCRs and contributes to the diversification of Ab repertoire in the mouse and human. Currently, it is not clear how VH replacement is regulated during early B lineage cell development. In this article, we show that cross-linking BCRs induces VH replacement in human EU12 μHC+ cells and in the newly emigrated immature B cells purified from peripheral blood of healthy donors or tonsillar samples. BCR signaling–induced VH replacement is dependent on the activation of Syk and Src kinases but is inhibited by CD19 costimulation, presumably through activation of the PI3K pathway. These results show that VH replacement is regulated by BCR-mediated signaling in human immature B cells, which can be modulated by physiological and pharmacological treatments.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.1102503
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2013
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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    Online Resource
  • 4
    Online Resource
    Online Resource
    The V(D)J recombination machinery is organized as large complexes anchored on the nuclear matrix (62.1)
    The American Association of Immunologists ; 2011
    In:  The Journal of Immunology Vol. 186, No. 1_Supplement ( 2011-04-01), p. 62.1-62.1
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 186, No. 1_Supplement ( 2011-04-01), p. 62.1-62.1
    Abstract: V(D)J recombination provides the foundation for adaptive immunity. This complicated process involves the cleavage of specific recombination signal sequences (RSS) by the recombination activating gene products, RAG1 and RAG2, followed by repair of the DNA double-stranded breaks (DSBs) by the non-homologous end joining (NHEJ) factors, including DNA dependent protein kinase (DNA-PK), Artemis, Ku86, Ku70, DNA ligase IV, XRCC4, XLF, and HMGB1. Currently, it is not clear how these factors are organized inside of the nuclei for recombination. Accumulating studies indicate that the multiple-component DNA replication and RNA transcription machineries are organized as large complexes on the nuclear matrix (NM). Here we show that RAG1, RAG2, and many NHEJ factors are associated with the NM, where they appear to form large complexes and are distributed closely at discrete foci. Ongoing RSS cleavage mainly occurs on the NM in developing B, T lineage cells and HEK293 cells with an artificial recombination system; Purified NMs containing RAG and NHEJ proteins possess the entire enzymatically active recombination system to cleave RSS substrates and generate coding joints in vitro. These results support a novel model that the V(D)J recombination machinery is organized as large complexes anchored on the NM to conduct recombination.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.186.Supp.62.1
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2011
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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    Online Resource
  • 5
    Online Resource
    Online Resource
    Molecular regulation of BCL2 to IGH translocation in follicular lymphoma (165.38)
    The American Association of Immunologists ; 2011
    In:  The Journal of Immunology Vol. 186, No. 1_Supplement ( 2011-04-01), p. 165.38-165.38
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 186, No. 1_Supplement ( 2011-04-01), p. 165.38-165.38
    Abstract: The hallmark of Follicular lymphoma (FL) is the aberrant translocation t(14; 18)(q32; q21) involving the IgH locus on chromosome 14 and BCL2 gene on chromosome 18. Previous analysis showed that approximately 70% of the BCL2/IgH translocations involve the BCL2 major break point region, known as the BCL2-MBR. Accumulating studies suggested that the BCL2-MBR to IgH translocation may be mechanistically similar to IgH DH to JH or VH to DJH recombination. Our analysis of 42 BCL2/IgH break points showed that 60% of them contain clearly identifiable DH genes, suggesting their origin from VH to DJH recombination. Our recent studies showed that the B lineage specific transcriptional factor Pax5 activates IgH VH to DJH recombination through binding to VH gene coding regions and recruiting RAG complexes. Based on this finding, we hypothesize that Pax5 also controls BCL2 to IgH chromosomal translocations. Our initial sequence analyses identified multiple potential Pax5 binding sites within the 150 bp BCL2-MBR. Electrophoresis Mobility Shift Assay (EMSA) demonstrated that Pax5 binds to the individual Pax5 binding sites as well as the full length BCL2-MBR. The BCL2-MBR displays Pax5-dependent enhancer activity when artificially placed in front of a minimal CMV promoter driven luciferase reporter gene. We also found that purified GST-RAG1 and RAG2 core proteins bind to and cleave at the BCL2-MBR. We speculate that Pax5 binding to the BCL2 MBR may enhance BCL2 to IgH recombination.
    Type of Medium: Online Resource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.186.Supp.165.38
    RVK:
    XA 54100
    RVK:
    XA 10000
    Language: English
    Publisher: The American Association of Immunologists
    Publication Date: 2011
    detail.hit.zdb_id: 1475085-5
    Location Call Number Limitation Availability
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    Online Resource
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