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Volumn 450, Issue 7172, 2007, Pages 1106-1110

RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; HOMEODOMAIN PROTEIN; LYMPHOCYTE ANTIGEN RECEPTOR; LYSINE; RAG2 PROTEIN; RECOMBINASE; TRYPTOPHAN;

EID: 37249041657     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06431     Document Type: Article
Times cited : (390)

References (41)
  • 1
    • 0035997348 scopus 로고    scopus 로고
    • (D)J recombination: RAG proteins, repair factors, and regulation
    • Gellert, M. V(D)J recombination: RAG proteins, repair factors, and regulation. Annu. Rev. Biochem. 71, 101-132 (2002).
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 101-132
    • Gellert, M.V.1
  • 2
    • 3242886299 scopus 로고    scopus 로고
    • How to keep V(D)J recombination under control
    • Oettinger, M. A. How to keep V(D)J recombination under control. Immunol. Rev. 200, 165-181 (2004).
    • (2004) Immunol. Rev , vol.200 , pp. 165-181
    • Oettinger, M.A.1
  • 3
    • 0035890244 scopus 로고    scopus 로고
    • Stepwise activation of the immunoglobulin m heavy chain gene locus
    • Chowdhury, D. & Sen, R. Stepwise activation of the immunoglobulin m heavy chain gene locus. EMBO J. 20, 6394-6403 (2001).
    • (2001) EMBO J , vol.20 , pp. 6394-6403
    • Chowdhury, D.1    Sen, R.2
  • 5
    • 0141705373 scopus 로고    scopus 로고
    • Antigen receptor loci poised for V(D)J rearrangement are broadly associated with BRG1 and flanked by peaks of histone H3 dimethylated at lysine 4
    • Morshead, K. B., Ciccone, D. N., Taverna, S. D., Allis, C. D. & Oettinger, M. A. Antigen receptor loci poised for V(D)J rearrangement are broadly associated with BRG1 and flanked by peaks of histone H3 dimethylated at lysine 4. Proc. Natl Acad. Sci. USA 100, 11577-11582 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 11577-11582
    • Morshead, K.B.1    Ciccone, D.N.2    Taverna, S.D.3    Allis, C.D.4    Oettinger, M.A.5
  • 6
    • 0031712128 scopus 로고    scopus 로고
    • The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis
    • Callebaut, I. & Mornon, J. P. The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis. Cell. Mol. Life Sci. 54, 880-891 (1998).
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 880-891
    • Callebaut, I.1    Mornon, J.P.2
  • 7
    • 23344453198 scopus 로고    scopus 로고
    • A PHD finger motif in the C terminus of RAG2 modulates recombination activity
    • Elkin, S. K. et al. A PHD finger motif in the C terminus of RAG2 modulates recombination activity. J. Biol. Chem. 280, 28701-28710 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 28701-28710
    • Elkin, S.K.1
  • 8
    • 12144286656 scopus 로고    scopus 로고
    • Nucleosome binding by the bromodomain and PHD finger of the transcriptional cofactor p300
    • Ragvin, A. et al. Nucleosome binding by the bromodomain and PHD finger of the transcriptional cofactor p300. J. Mol. Biol. 337, 773-788 (2004).
    • (2004) J. Mol. Biol , vol.337 , pp. 773-788
    • Ragvin, A.1
  • 9
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442, 96-99 (2006).
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1
  • 10
    • 33745839365 scopus 로고    scopus 로고
    • A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka, J. et al. A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442, 86-90 (2006).
    • (2006) Nature , vol.442 , pp. 86-90
    • Wysocka, J.1
  • 11
    • 23844471918 scopus 로고    scopus 로고
    • A direct interaction between the RAG2 C terminus and the core histones is required for efficient V(D)J recombination
    • West, K. L. et al. A direct interaction between the RAG2 C terminus and the core histones is required for efficient V(D)J recombination. Immunity 23, 203-212 (2005).
    • (2005) Immunity , vol.23 , pp. 203-212
    • West, K.L.1
  • 12
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li, H. et al. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442, 91-95 (2006).
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1
  • 13
    • 33745818717 scopus 로고    scopus 로고
    • Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
    • Pena, P. V. et al. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442, 100-103 (2006).
    • (2006) Nature , vol.442 , pp. 100-103
    • Pena, P.V.1
  • 14
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna, S. D. et al. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs. Mol. Cell 24, 785-796 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 785-796
    • Taverna, S.D.1
  • 15
    • 33846019277 scopus 로고    scopus 로고
    • Methylation of lysine 4 on histone H3: Intricacy of writing and reading a single epigenetic mark
    • Ruthenburg, A. J., Allis, C. D. & Wysocka, J. Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. Mol. Cell 25, 15-30 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 15-30
    • Ruthenburg, A.J.1    Allis, C.D.2    Wysocka, J.3
  • 16
    • 37649026007 scopus 로고    scopus 로고
    • The PHD finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2
    • doi:10.1073/pnas.0709170104 in the press
    • Ramon-Maiques, S. et al. The PHD finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2. Proc. Natl Acad. Sci. USA. doi:10.1073/pnas.0709170104 (in the press).
    • Proc. Natl Acad. Sci. USA
    • Ramon-Maiques, S.1
  • 17
    • 34047248383 scopus 로고    scopus 로고
    • Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36
    • Shi, X. et al. Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. J. Biol. Chem. 282, 2450-2455 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 2450-2455
    • Shi, X.1
  • 18
    • 0033942616 scopus 로고    scopus 로고
    • Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies
    • Gomez, C. A. et al. Mutations in conserved regions of the predicted RAG2 kelch repeats block initiation of V(D)J recombination and result in primary immunodeficiencies. Mol. Cell. Biol. 20, 5653-5664 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5653-5664
    • Gomez, C.A.1
  • 19
    • 0032577548 scopus 로고    scopus 로고
    • Partial V(D)J recombination activity leads to Omenn syndrome
    • Villa, A. et al. Partial V(D)J recombination activity leads to Omenn syndrome. Cell 93, 885-896 (1998).
    • (1998) Cell , vol.93 , pp. 885-896
    • Villa, A.1
  • 20
    • 0141753136 scopus 로고    scopus 로고
    • Regulation of V(D)J recombination by nucleosome positioning at recombination signal sequences
    • Baumann, M., Mamais, A., McBlane, F., Xiao, H. & Boyes, J. Regulation of V(D)J recombination by nucleosome positioning at recombination signal sequences. EMBO J. 22, 5197-5207 (2003).
    • (2003) EMBO J , vol.22 , pp. 5197-5207
    • Baumann, M.1    Mamais, A.2    McBlane, F.3    Xiao, H.4    Boyes, J.5
  • 21
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: Caught in a bind?
    • Sims, R. J. III & Reinberg, D. Histone H3 Lys 4 methylation: caught in a bind? Genes Dev. 20, 2779-2786 (2006).
    • (2006) Genes Dev , vol.20 , pp. 2779-2786
    • Sims III, R.J.1    Reinberg, D.2
  • 22
    • 33947302685 scopus 로고    scopus 로고
    • The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases
    • Iwase, S. et al. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell 128, 1077-1088 (2007).
    • (2007) Cell , vol.128 , pp. 1077-1088
    • Iwase, S.1
  • 23
    • 3042750473 scopus 로고    scopus 로고
    • Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition
    • Perkins, E. J., Kee, B. L. & Ramsden, D. A. Histone 3 lysine 4 methylation during the pre-B to immature B-cell transition. Nucleic Acids Res. 32, 1942-1947 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. 1942-1947
    • Perkins, E.J.1    Kee, B.L.2    Ramsden, D.A.3
  • 24
    • 0037417795 scopus 로고    scopus 로고
    • Deletion of the RAG2 C terminus leads to impaired lymphoid development in mice
    • Akamatsu, Y. et al. Deletion of the RAG2 C terminus leads to impaired lymphoid development in mice. Proc. Natl Acad. Sci. USA 100, 1209-1214 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1209-1214
    • Akamatsu, Y.1
  • 25
    • 34848843525 scopus 로고    scopus 로고
    • Rag mutations reveal robust alternative end joining
    • Corneo, B. et al. Rag mutations reveal robust alternative end joining. Nature 449, 483-486 (2007).
    • (2007) Nature , vol.449 , pp. 483-486
    • Corneo, B.1
  • 26
    • 0032541328 scopus 로고    scopus 로고
    • Dual role of RAG2 in V(D)J recombination: Catalysis and regulation of ordered Ig gene assembly
    • Kirch, S. A., Rathbun, G. A. & Oettinger, M. A. Dual role of RAG2 in V(D)J recombination: catalysis and regulation of ordered Ig gene assembly. EMBO J. 17, 4881-4886 (1998).
    • (1998) EMBO J , vol.17 , pp. 4881-4886
    • Kirch, S.A.1    Rathbun, G.A.2    Oettinger, M.A.3
  • 27
    • 0036850786 scopus 로고    scopus 로고
    • The "dispensable" portion of RAG2 is necessary for efficient V-to-DJ rearrangement during B and T cell development
    • Liang, H. E. et al. The "dispensable" portion of RAG2 is necessary for efficient V-to-DJ rearrangement during B and T cell development. Immunity 17, 639-651 (2002).
    • (2002) Immunity , vol.17 , pp. 639-651
    • Liang, H.E.1
  • 28
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi, Y. & Whetstine, J. R. Dynamic regulation of histone lysine methylation by demethylases. Mol. Cell 25, 1-14 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 29
    • 22544468602 scopus 로고    scopus 로고
    • COMPASS in the voyage of defining the role of trithorax/MLL-containing complexes: Linking leukemogensis to covalent modifications of chromatin
    • Tenney, K. & Shilatifard, A. A. COMPASS in the voyage of defining the role of trithorax/MLL-containing complexes: linking leukemogensis to covalent modifications of chromatin. J. Cell. Biochem. 95, 429-436 (2005).
    • (2005) J. Cell. Biochem , vol.95 , pp. 429-436
    • Tenney, K.1    Shilatifard, A.A.2
  • 30
    • 35349024178 scopus 로고    scopus 로고
    • A plant homeodomainin Rag-2 that binds hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement
    • Liu, Y., Subrahmanyam, R., Chakraborty, T., Sen, R. & Desiderio, S. A plant homeodomainin Rag-2 that binds hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement. Immunity 4, 561-571 (2007).
    • (2007) Immunity , vol.4 , pp. 561-571
    • Liu, Y.1    Subrahmanyam, R.2    Chakraborty, T.3    Sen, R.4    Desiderio, S.5
  • 31
    • 1842472070 scopus 로고    scopus 로고
    • Ordered DNA release and target capture in RAG transposition
    • Matthews, A. G., Elkin, S. K. & Oettinger, M. A. Ordered DNA release and target capture in RAG transposition. EMBO J. 23, 1198-1206 (2004).
    • (2004) EMBO J , vol.23 , pp. 1198-1206
    • Matthews, A.G.1    Elkin, S.K.2    Oettinger, M.A.3
  • 32
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260 (1997).
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Ottinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Ottinowski, Z.1    Minor, W.2
  • 34
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 35
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 36
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 37
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. M. & Schneider, T. R. SHELXL: High-resolution refinement. Methods Enzymol. 277, 319-343 (1997).
    • (1997) Methods Enzymol , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 38
    • 0037447338 scopus 로고    scopus 로고
    • The C-terminal portion of RAG2 protects against transposition in vitro
    • Elkin, S. K., Matthews, A. G. & Oettinger, M. A. The C-terminal portion of RAG2 protects against transposition in vitro. EMBO J. 22, 1931-1938 (2003).
    • (2003) EMBO J , vol.22 , pp. 1931-1938
    • Elkin, S.K.1    Matthews, A.G.2    Oettinger, M.A.3
  • 39
    • 0345505218 scopus 로고    scopus 로고
    • Nonhomologous end joining and V(D)J recombination require an additional factor
    • Dai, Y. et al. Nonhomologous end joining and V(D)J recombination require an additional factor. Proc. Natl Acad. Sci. USA 100, 2462-2467 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2462-2467
    • Dai, Y.1
  • 40
    • 0027158024 scopus 로고
    • Unequal signal and coding joint formation in human V(D)J recombination
    • Gauss, G. H. & Lieber, M. R. Unequal signal and coding joint formation in human V(D)J recombination. Mol. Cell. Biol. 13, 3900-3906 (1993).
    • (1993) Mol. Cell. Biol , vol.13 , pp. 3900-3906
    • Gauss, G.H.1    Lieber, M.R.2
  • 41
    • 0026032665 scopus 로고
    • Virus-transformed pre-B cells show ordered activation but not inactivation of immunoglobulin gene rearrangement and transcription
    • Schlissel, M. S., Corcoran, L. M. & Baltimore, D. Virus-transformed pre-B cells show ordered activation but not inactivation of immunoglobulin gene rearrangement and transcription. J. Exp. Med. 173, 711-720 (1991).
    • (1991) J. Exp. Med , vol.173 , pp. 711-720
    • Schlissel, M.S.1    Corcoran, L.M.2    Baltimore, D.3


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