메뉴 건너뛰기




Volumn 54, Issue 8, 1998, Pages 880-891

The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis

Author keywords

propeller; Hydrophobic cluster analysis; Kelch motif; PHD motif; RAG2; V(D)J recombination; Zinc binding

Indexed keywords

DNA BINDING PROTEIN;

EID: 0031712128     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050216     Document Type: Article
Times cited : (103)

References (71)
  • 1
    • 0027087077 scopus 로고
    • Molecular analysis of V(D)J recombination
    • Gellert M. (1492) Molecular analysis of V(D)J recombination. Annu. Rev. Genet. 22: 425-446
    • (1492) Annu. Rev. Genet. , vol.22 , pp. 425-446
    • Gellert, M.1
  • 2
    • 0028048275 scopus 로고
    • The mechanism of V(D)J joining: Lessons from molecular, immunological and comparative analyses
    • Lewis S. M. (1494) The mechanism of V(D)J joining: lessons from molecular, immunological and comparative analyses. Adv. Immunol. 56: 27-150
    • (1494) Adv. Immunol. , vol.56 , pp. 27-150
    • Lewis, S.M.1
  • 3
    • 0030966099 scopus 로고    scopus 로고
    • Recent advances in understanding V(D)J recombination
    • Gellert M. (1997) Recent advances in understanding V(D)J recombination. Adv. Immunol. 64: 39-64
    • (1997) Adv. Immunol. , vol.64 , pp. 39-64
    • Gellert, M.1
  • 4
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa S. (1983) Somatic generation of antibody diversity. Nature 302: 575-581
    • (1983) Nature , vol.302 , pp. 575-581
    • Tonegawa, S.1
  • 5
    • 0027491330 scopus 로고
    • Characterization of broken DNA molecules associated with V(D)J recombination
    • Roth D. B., Zhu C. M. and Gellert M. (1993) Characterization of broken DNA molecules associated with V(D)J recombination. Proc. Natl. Acad. Sci. USA 90: 10788-10792
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10788-10792
    • Roth, D.B.1    Zhu, C.M.2    Gellert, M.3
  • 6
    • 0026792892 scopus 로고
    • V(D)J recombination: Broken DNA molecules with covalently sealed (hairpin) coding ends in scid mouse thmocytes
    • Roth D. B., Menetski J. P., Nakajima P. B., Bosma M. J. and Gellert M. (1992) V(D)J recombination: broken DNA molecules with covalently sealed (hairpin) coding ends in scid mouse thmocytes. Cell 70: 983-991
    • (1992) Cell , vol.70 , pp. 983-991
    • Roth, D.B.1    Menetski, J.P.2    Nakajima, P.B.3    Bosma, M.J.4    Gellert, M.5
  • 7
    • 0028801363 scopus 로고
    • Formation and resolution of double strand break intermediates in V(D)J rearrangement
    • Ramsden D. A. and Gellert M. (1995) Formation and resolution of double strand break intermediates in V(D)J rearrangement. Genes Dev. 9: 2409-2420
    • (1995) Genes Dev , vol.9 , pp. 2409-2420
    • Ramsden, D.A.1    Gellert, M.2
  • 8
    • 0028958942 scopus 로고
    • Characterization of coding ends in thymocytes of scid mice: Implications for the mechanism of V(D)J recombination
    • Zhu C. M. and Roth D. B. (1995) Characterization of coding ends in thymocytes of scid mice: implications for the mechanism of V(D)J recombination. Immunity 2: 101-112
    • (1995) Immunity , vol.2 , pp. 101-112
    • Zhu, C.M.1    Roth, D.B.2
  • 9
    • 0024846088 scopus 로고
    • The V(D)J recombination activating gene. RAG-1
    • Schatz D. G., Oettinger M. A. and Baltimore D. A. (1989) The V(D)J recombination activating gene. RAG-1. Cell 59: 1035-1048
    • (1989) Cell , vol.59 , pp. 1035-1048
    • Schatz, D.G.1    Oettinger, M.A.2    Baltimore, D.A.3
  • 10
    • 0025301095 scopus 로고
    • RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination
    • Oettinger M. A., Schatz D. G., Gorka C. and Baltimore D. (1990) RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248: 1517-1523
    • (1990) Science , vol.248 , pp. 1517-1523
    • Oettinger, M.A.1    Schatz, D.G.2    Gorka, C.3    Baltimore, D.4
  • 11
    • 0029864993 scopus 로고    scopus 로고
    • Initiation of V(D)J recombination in vitro obeying the 12-23 rule
    • Eastman Q. M., Leu T. M. J. and Schatz D. G. (1996) Initiation of V(D)J recombination in vitro obeying the 12-23 rule. Nature 380: 85-88
    • (1996) Nature , vol.380 , pp. 85-88
    • Eastman, Q.M.1    Leu, T.M.J.2    Schatz, D.G.3
  • 12
    • 0030009253 scopus 로고    scopus 로고
    • The RAG1 and RAG2 proteins establish the 12-23 rule in V(D)J recombination
    • van Gent D. C., Ramsden D. A. and Gellert M. (1996) The RAG1 and RAG2 proteins establish the 12-23 rule in V(D)J recombination. Cell 85: 107-113
    • (1996) Cell , vol.85 , pp. 107-113
    • Van Gent, D.C.1    Ramsden, D.A.2    Gellert, M.3
  • 13
    • 0028805853 scopus 로고
    • Cleavage at V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps
    • McBlane J. F., van Gent D. C., Ramsden D. A., Romeo C., Cuomo C. A., Gellert M. et al. (1995) Cleavage at V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps. Cell 83: 387-395
    • (1995) Cell , vol.83 , pp. 387-395
    • McBlane, J.F.1    Van Gent, D.C.2    Ramsden, D.A.3    Romeo, C.4    Cuomo, C.A.5    Gellert, M.6
  • 14
    • 0029967722 scopus 로고    scopus 로고
    • Similarities between initiation of V(D)J reeombination and retroviral integration
    • van Gent D. C., Mizuuchi K. and Gellert M. (1996) Similarities between initiation of V(D)J reeombination and retroviral integration. Science 271: 1592-1594
    • (1996) Science , vol.271 , pp. 1592-1594
    • Van Gent, D.C.1    Mizuuchi, K.2    Gellert, M.3
  • 15
    • 0030964130 scopus 로고    scopus 로고
    • A stable RAG1-RAG2-DNA complex that is active in V(D)J cleavage
    • Hiom K. and Gellert M. (1997) A stable RAG1-RAG2-DNA complex that is active in V(D)J cleavage. Cell 88: 65-72
    • (1997) Cell , vol.88 , pp. 65-72
    • Hiom, K.1    Gellert, M.2
  • 16
    • 0001265782 scopus 로고    scopus 로고
    • RAG1 mediates signal sequence recognition and recruitement of RAG2 in V(D)J recombination
    • Difilippantonio M. J., McMahan C. J., Eastman Q. M., Spanopoulou E. and Schatz D. G. (1996) RAG1 mediates signal sequence recognition and recruitement of RAG2 in V(D)J recombination. Cell 87: 253-262
    • (1996) Cell , vol.87 , pp. 253-262
    • Difilippantonio, M.J.1    McMahan, C.J.2    Eastman, Q.M.3    Spanopoulou, E.4    Schatz, D.G.5
  • 17
    • 0030592523 scopus 로고    scopus 로고
    • The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination
    • Spanopoulou E., Zaitseva F., Wang F.-H., Santagata S., Baltimore D. and Panayotou G. (1996) The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination. Cell 87: 263-276
    • (1996) Cell , vol.87 , pp. 263-276
    • Spanopoulou, E.1    Zaitseva, F.2    Wang, F.-H.3    Santagata, S.4    Baltimore, D.5    Panayotou, G.6
  • 18
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent D. C., Hiom K., Paull T. T. and Gellert M. (1997) Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J. 16: 2665-2670
    • (1997) EMBO J , vol.16 , pp. 2665-2670
    • Van Gent, D.C.1    Hiom, K.2    Paull, T.T.3    Gellert, M.4
  • 19
    • 0030887862 scopus 로고    scopus 로고
    • RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination
    • Agrawal A. and Schatz D. G. (1997) RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination. Cell 89: 43-53
    • (1997) Cell , vol.89 , pp. 43-53
    • Agrawal, A.1    Schatz, D.G.2
  • 20
    • 0029553231 scopus 로고
    • Localization, interaction and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2
    • Spanopoulou E., Cortes P., Shih C., Huang C.-M., Silver D. P., Svec P. et al. (1995) Localization, interaction and RNA binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2. Immunity 3: 715-726
    • (1995) Immunity , vol.3 , pp. 715-726
    • Spanopoulou, E.1    Cortes, P.2    Shih, C.3    Huang, C.-M.4    Silver, D.P.5    Svec, P.6
  • 21
    • 0029083695 scopus 로고
    • Rag-1 and rag-2 are components of a high molecular-weighl complex, and association of rag-2 with this complex is rag-1 dependent
    • Leu T. M. J. and Schatz D. G. (1995) Rag-1 and rag-2 are components of a high molecular-weighl complex, and association of rag-2 with this complex is rag-1 dependent. Mol. Cell. Biol. 15: 5657-5670
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5657-5670
    • Leu, T.M.J.1    Schatz, D.G.2
  • 22
    • 0030753633 scopus 로고    scopus 로고
    • Cell-free V(D)J recombination
    • Ramsden D. A., Paull T. T. and Gellert M. (1997) Cell-free V(D)J recombination. Nature 388: 488-491
    • (1997) Nature , vol.388 , pp. 488-491
    • Ramsden, D.A.1    Paull, T.T.2    Gellert, M.3
  • 23
    • 0027770854 scopus 로고
    • Expression and V(D)J recombination activity of mutated RAG-1 proteins
    • Sadofksy M. J., Hesse J. E., McBlane J. F. and Gellert M. (1993) Expression and V(D)J recombination activity of mutated RAG-1 proteins. Nucleic Acids Res. 21: 5644-5650
    • (1993) Nucleic Acids Res , vol.21 , pp. 5644-5650
    • Sadofksy, M.J.1    Hesse, J.E.2    McBlane, J.F.3    Gellert, M.4
  • 24
    • 0028237683 scopus 로고
    • Definition of a core region of RAG-2 that is functional in V(D)J recombination
    • Sadofsky M. J., Hesse J. E. and Gellert M. (1994) Definition of a core region of RAG-2 that is functional in V(D)J recombination. Nucleic Acids Res. 22: 1805-1809
    • (1994) Nucleic Acids Res , vol.22 , pp. 1805-1809
    • Sadofsky, M.J.1    Hesse, J.E.2    Gellert, M.3
  • 25
    • 0028307661 scopus 로고
    • Analysis of regions of RAG-2 important for V(D)J recombination
    • Cuomo C. A. and Ottinger M. A. (1994) Analysis of regions of RAG-2 important for V(D)J recombination. Nucleic Acids Res. 22: 1810-1814
    • (1994) Nucleic Acids Res , vol.22 , pp. 1810-1814
    • Cuomo, C.A.1    Ottinger, M.A.2
  • 26
    • 0027197151 scopus 로고
    • Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination
    • Silver D. P., Spanopoulou E., Mulligan R. C. and Baltimore D. (1993) Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination. Proc. Natl. Acad. Sci. USA 90: 6100-6104
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6100-6104
    • Silver, D.P.1    Spanopoulou, E.2    Mulligan, R.C.3    Baltimore, D.4
  • 28
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon S. F., Rodgers K. K., Schatz D. G., Coleman J. E. and Steitz T. A. (1997) Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat. Struct. Biol. 4: 586-591
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 30
    • 0031092628 scopus 로고    scopus 로고
    • Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2
    • McMahan C. J., Sadofsky M. J. and Schatz D. G. (1997) Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. J. Immunol. 158: 2202-2210
    • (1997) J. Immunol. , vol.158 , pp. 2202-2210
    • McMahan, C.J.1    Sadofsky, M.J.2    Schatz, D.G.3
  • 31
    • 0024997668 scopus 로고
    • The role of DNA topoisomerase in recombination and genome stability: A double-edge sword?
    • Wang J. C., Caron P. R. and Kim R. A. (1990) The role of DNA topoisomerase in recombination and genome stability: a double-edge sword? Cell 62: 403-406
    • (1990) Cell , vol.62 , pp. 403-406
    • Wang, J.C.1    Caron, P.R.2    Kim, R.A.3
  • 33
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis. An efficient new way to compare and analyse amino-acid sequences
    • Gaboriaud C., Bissery V., Benchetrit T. and Mornon J. P. (1987) Hydrophobic cluster analysis. An efficient new way to compare and analyse amino-acid sequences. FEBS Lett. 224: 149-155
    • (1987) FEBS Lett , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 34
    • 0030690133 scopus 로고    scopus 로고
    • Deciphering protein sequence information through hydrophobic cluster analysis: Current status and perspectives
    • Callebaut I., Labesse G., Durand P., Poupon A., Canard L., Chomilier J. et al. (1997) Deciphering protein sequence information through hydrophobic cluster analysis: current status and perspectives. Clell. Mol. Life Sci. 53: 621-645
    • (1997) Clell. Mol. Life Sci. , vol.53 , pp. 621-645
    • Callebaut, I.1    Labesse, G.2    Durand, P.3    Poupon, A.4    Canard, L.5    Chomilier, J.6
  • 36
    • 0031031787 scopus 로고    scopus 로고
    • From BRCA1 to RAPI: A widespread BRCT module closely associated to DNA repair
    • Callebaut I. and Mornon J.-P. (1997) From BRCA1 to RAPI: a widespread BRCT module closely associated to DNA repair. FEBS Lett. 400: 25-30
    • (1997) FEBS Lett , vol.400 , pp. 25-30
    • Callebaut, I.1    Mornon, J.-P.2
  • 37
    • 0031046294 scopus 로고    scopus 로고
    • A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins
    • Bork P., Hofmann K., Bucher P., Neuwald A. F., Altschul S. F. and Koonin E. V. (1997) A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins. FASEB J. 11: 68-76
    • (1997) FASEB J , vol.11 , pp. 68-76
    • Bork, P.1    Hofmann, K.2    Bucher, P.3    Neuwald, A.F.4    Altschul, S.F.5    Koonin, E.V.6
  • 38
    • 0031214080 scopus 로고    scopus 로고
    • Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV
    • Critchlow S. E., Bowater R. P. and Jackson S. P. (1997) Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV. Curr. Biol. 7: 588-598
    • (1997) Curr. Biol. , vol.7 , pp. 588-598
    • Critchlow, S.E.1    Bowater, R.P.2    Jackson, S.P.3
  • 39
    • 0030743386 scopus 로고    scopus 로고
    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
    • Grawunder U., Wilm M., Wu X., Kulesza P., Wilson T. E., Mann M. et al. (1997) Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature 388: 492-495
    • (1997) Nature , vol.388 , pp. 492-495
    • Grawunder, U.1    Wilm, M.2    Wu, X.3    Kulesza, P.4    Wilson, T.E.5    Mann, M.6
  • 40
    • 0027403024 scopus 로고
    • kelch encodes a component of intercellular bridges in Drosophila egg chambers
    • Xue F. and Cooley L. (1993) kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 72: 681-693
    • (1993) Cell , vol.72 , pp. 681-693
    • Xue, F.1    Cooley, L.2
  • 41
    • 0028231273 scopus 로고
    • Drosophila kelch motif is derived from a common enzyme fold
    • Bork P. and Doolittle R. F. (1994) Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 236: 1277-1282
    • (1994) J. Mol. Biol. , vol.236 , pp. 1277-1282
    • Bork, P.1    Doolittle, R.F.2
  • 42
    • 0028980644 scopus 로고
    • β-scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm
    • Way M., Sanders M., Chafel M., Tu Y.-H., Knight A. and Matsudaira P. (1995) β-scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm. J. Cell Sci. 108: 3155-3162
    • (1995) J. Cell Sci. , vol.108 , pp. 3155-3162
    • Way, M.1    Sanders, M.2    Chafel, M.3    Tu, Y.-H.4    Knight, A.5    Matsudaira, P.6
  • 43
    • 0028851246 scopus 로고
    • Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm
    • Way M., Sanders M., Garcia C., Sakai J. and Matsudaira P. (1995) Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm. J. Cell Biol. 128: 51-60
    • (1995) J. Cell Biol. , vol.128 , pp. 51-60
    • Way, M.1    Sanders, M.2    Garcia, C.3    Sakai, J.4    Matsudaira, P.5
  • 44
    • 0026084786 scopus 로고
    • Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase
    • Ito N., Philips S. E. V., Stevens C., Ogel Z. B., McPherson M. J., Keen J. N. et al. (1991) Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase. Nature 350: 87-90
    • (1991) Nature , vol.350 , pp. 87-90
    • Ito, N.1    Philips, S.E.V.2    Stevens, C.3    Ogel, Z.B.4    McPherson, M.J.5    Keen, J.N.6
  • 45
    • 0028290823 scopus 로고
    • Crystal structure of a free radical enzyme, galactose oxidase
    • Ito N., Philips S. E. V., Yadav K. D. S. and Knowles P. F. (1994) Crystal structure of a free radical enzyme, galactose oxidase. J. Mol. Biol. 238: 794-814
    • (1994) J. Mol. Biol. , vol.238 , pp. 794-814
    • Ito, N.1    Philips, S.E.V.2    Yadav, K.D.S.3    Knowles, P.F.4
  • 46
    • 0028813772 scopus 로고
    • 1.8 Å crystal structure of the C-terminal domain of rabbit serum haemopexin
    • Faber H. R., Groom C. R., Baker H. M., Morgan W. T., Smith A. and Baker E. N. (1995) 1.8 Å crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure 3: 551-559
    • (1995) Structure , vol.3 , pp. 551-559
    • Faber, H.R.1    Groom, C.R.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 47
    • 0026592054 scopus 로고
    • The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-Å resolution
    • Xia Z. X., Dai W. W., Xiong J. P., Hao Z. P., Davidson V. L., White S. et al. (1992) The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-Å resolution. J. Biol. Chem. 267: 22289-22297
    • (1992) J. Biol. Chem. , vol.267 , pp. 22289-22297
    • Xia, Z.X.1    Dai, W.W.2    Xiong, J.P.3    Hao, Z.P.4    Davidson, V.L.5    White, S.6
  • 48
    • 0026671355 scopus 로고
    • Structural principles for the propeller assembly of β-sheets: The preference for seven-fold symmetry
    • Murzin A. (1992) Structural principles for the propeller assembly of β-sheets: the preference for seven-fold symmetry. Proteins 14: 191-201
    • (1992) Proteins , vol.14 , pp. 191-201
    • Murzin, A.1
  • 53
    • 0032485075 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the regulator of chromosome condensation (RCCI) reveals a seven-bladed propeller
    • Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M. et al. (1998) The 1.7 Å crystal structure of the regulator of chromosome condensation (RCCI) reveals a seven-bladed propeller. Nature 392: 97-101
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1    Nassar, N.2    Vetter, I.3    Becker, J.4    Klebe, C.5    Roth, M.6
  • 54
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese J. N., Laver W. G. and Colman P. M. (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303: 35-40
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 55
    • 0027364312 scopus 로고
    • Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase
    • Crennell S. J., Garman E. F., Laver W. G., Vimr E. R. and Taylor G. L. (1993) Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase. Proc. Natl. Acad. Sci. USA 90: 9852-9856
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9852-9856
    • Crennell, S.J.1    Garman, E.F.2    Laver, W.G.3    Vimr, E.R.4    Taylor, G.L.5
  • 56
    • 0026458378 scopus 로고
    • Amino acids substitution matrices from proteins blocks
    • Henikoff S. and Henikoff J. G. (1992) Amino acids substitution matrices from proteins blocks. Proc. Natl. Acad. Sci. USA 89: 10915-10919
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 58
    • 0029148609 scopus 로고
    • Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton
    • von Bülow M., Heid H., Hess H. and Franke W. W. (1995) Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton. Exp. Cell Res. 219: 407-413
    • (1995) Exp. Cell Res. , vol.219 , pp. 407-413
    • Von Bülow, M.1    Heid, H.2    Hess, H.3    Franke, W.W.4
  • 59
    • 0030773728 scopus 로고    scopus 로고
    • Teal and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell
    • Mata J. and Nurse P. (1997) teal and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell. Cell 89: 939-949
    • (1997) Cell , vol.89 , pp. 939-949
    • Mata, J.1    Nurse, P.2
  • 60
    • 0028861418 scopus 로고
    • The PHD-finger: Implications for chromatin-mediated transcriptional regulation
    • Aasland R., Gibson T. J. and Stewart A. F. (1995) The PHD-finger: implications for chromatin-mediated transcriptional regulation. Trends Biochem. Sci. 20: 56-59
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 56-59
    • Aasland, R.1    Gibson, T.J.2    Stewart, A.F.3
  • 62
    • 0028857948 scopus 로고
    • The leukemia-associated-protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL. AF10, and MLLT6 proteins
    • Saha V., Chaplin T., Gregorini A., Ayton P. and Young B. D. (1995) The leukemia-associated-protein (LAP) domain, a cysteine-rich motif, is present in a wide range of proteins, including MLL. AF10, and MLLT6 proteins. Proc. Natl. Acad. Sci. USA 92: 9737-9741
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9737-9741
    • Saha, V.1    Chaplin, T.2    Gregorini, A.3    Ayton, P.4    Young, B.D.5
  • 63
    • 0030825790 scopus 로고    scopus 로고
    • Residues in the WD repeats of Tupl required for interaction with α2
    • Komachi K. and Johnson A. D. (1997) Residues in the WD repeats of Tupl required for interaction with α2. Mol. Cell. Biol. 17: 6023-6028
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6023-6028
    • Komachi, K.1    Johnson, A.D.2
  • 64
    • 9844236474 scopus 로고    scopus 로고
    • Identification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosome
    • Wang A., Forman-Kay J., Luo Y., Luo M., Chow Y.-H., Plumb J., et al. (1997) Identification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosome. Hum. Mol. Genet. 6: 2117-2126
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 2117-2126
    • Wang, A.1    Forman-Kay, J.2    Luo, Y.3    Luo, M.4    Chow, Y.-H.5    Plumb, J.6
  • 65
    • 0028291638 scopus 로고
    • Mutational analysis of the PRP4 protein of Saccharomyces cerevisiae suggests domain structure and sn-RNP interactions
    • Hu J., Xu Y., Schappert K., Harrington T., Wang A., Braga R. et al. (1994) Mutational analysis of the PRP4 protein of Saccharomyces cerevisiae suggests domain structure and sn-RNP interactions. Nucleic Acids Res. 22: 1724-1734
    • (1994) Nucleic Acids Res , vol.22 , pp. 1724-1734
    • Hu, J.1    Xu, Y.2    Schappert, K.3    Harrington, T.4    Wang, A.5    Braga, R.6
  • 66
    • 0029042690 scopus 로고
    • The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to actin-associated protein kelch and scruin
    • Varkey J. P., Muhlrad P. J., Minniti A. N., Do B. and Ward S. (1995) The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to actin-associated protein kelch and scruin. Genes Dev. 9: 1074-1086
    • (1995) Genes Dev , vol.9 , pp. 1074-1086
    • Varkey, J.P.1    Muhlrad, P.J.2    Minniti, A.N.3    Do, B.4    Ward, S.5
  • 67
    • 0029949657 scopus 로고    scopus 로고
    • A novel type of protein kinase phosphorylates actin in the actin-fragmin complex
    • Eichinger L., Bomblies L., Vandekerckhove J., Schleicher M. and Gettemans J. (1996) A novel type of protein kinase phosphorylates actin in the actin-fragmin complex. EMBO J. 15: 5547-5556
    • (1996) EMBO J , vol.15 , pp. 5547-5556
    • Eichinger, L.1    Bomblies, L.2    Vandekerckhove, J.3    Schleicher, M.4    Gettemans, J.5
  • 68
    • 0031000133 scopus 로고    scopus 로고
    • Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin
    • Sun S., Footer M. and Matsudaira P. (1997) Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin. Mol. Cell. Biol. 8: 421-430
    • (1997) Mol. Cell. Biol. , vol.8 , pp. 421-430
    • Sun, S.1    Footer, M.2    Matsudaira, P.3
  • 69
    • 0030863636 scopus 로고    scopus 로고
    • VP16 targets an amino-terminal domain of HCF involved in cell cycle progression
    • Wilson A. C., Freiman R. N., Goto H., Nishimoto T. and Herr W. (1997) VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. Mol. Cell. Biol. 17: 6139-6146
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6139-6146
    • Wilson, A.C.1    Freiman, R.N.2    Goto, H.3    Nishimoto, T.4    Herr, W.5
  • 70
    • 0030915297 scopus 로고    scopus 로고
    • A single-point mutation in HCF causes temperature-sensitive cell-cycle arrest and disrupts VP16 function
    • Goto H., Motomura S., Wilson A. C., Freiman R. N., Nakabeppu Y., Fukushima K. et al. (1997) A single-point mutation in HCF causes temperature-sensitive cell-cycle arrest and disrupts VP16 function. Genes Dev. 11: 726-737
    • (1997) Genes Dev. , vol.11 , pp. 726-737
    • Goto, H.1    Motomura, S.2    Wilson, A.C.3    Freiman, R.N.4    Nakabeppu, Y.5    Fukushima, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.