메뉴 건너뛰기




Volumn 369, Issue 2, 2007, Pages 334-342

Molecular Implications of Evolutionary Differences in CHD Double Chromodomains

Author keywords

CHD; double chromodomains; histone H3; lysine methylation; transcription

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; CHROMOADENOSINE TRIPHOSPHATASE HELICASE DNA BINDING PROTEIN; DNA BINDING PROTEIN; HISTONE H3; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 34247576687     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.03.024     Document Type: Article
Times cited : (48)

References (49)
  • 2
    • 33745122231 scopus 로고    scopus 로고
    • Identification of multiple distinct Snf2 subfamilies with conserved structural motifs
    • Flaus A., Martin D.M., Barton G.J., and Owen-Hughes T. Identification of multiple distinct Snf2 subfamilies with conserved structural motifs. Nucl. Acids Res. 34 (2006) 2887-2905
    • (2006) Nucl. Acids Res. , vol.34 , pp. 2887-2905
    • Flaus, A.1    Martin, D.M.2    Barton, G.J.3    Owen-Hughes, T.4
  • 3
    • 33745221438 scopus 로고    scopus 로고
    • Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes
    • Stockdale C., Flaus A., Ferreira H., and Owen-Hughes T. Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin remodeling complexes. J. Biol. Chem. 281 (2006) 16279-16288
    • (2006) J. Biol. Chem. , vol.281 , pp. 16279-16288
    • Stockdale, C.1    Flaus, A.2    Ferreira, H.3    Owen-Hughes, T.4
  • 4
    • 15544369061 scopus 로고    scopus 로고
    • Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly
    • Lusser A., Urwin D.L., and Kadonaga J.T. Distinct activities of CHD1 and ACF in ATP-dependent chromatin assembly. Nature Struct. Mol. Biol. 12 (2005) 160-166
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 160-166
    • Lusser, A.1    Urwin, D.L.2    Kadonaga, J.T.3
  • 5
    • 33646869229 scopus 로고    scopus 로고
    • Chromatin remodelling in mammalian differentiation: lessons from ATP-dependent remodellers
    • de la Serna I.L., Ohkawa Y., and Imbalzano A.N. Chromatin remodelling in mammalian differentiation: lessons from ATP-dependent remodellers. Nature Rev. Genet. 7 (2006) 461-473
    • (2006) Nature Rev. Genet. , vol.7 , pp. 461-473
    • de la Serna, I.L.1    Ohkawa, Y.2    Imbalzano, A.N.3
  • 7
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker P.B., and Horz W. ATP-dependent nucleosome remodeling. Annu. Rev. Biochem. 71 (2002) 247-273
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 8
    • 0037240878 scopus 로고    scopus 로고
    • The NuRD complex: linking histone modification to nucleosome remodeling
    • Feng Q., and Zhang Y. The NuRD complex: linking histone modification to nucleosome remodeling. Curr. Top. Microbiol. Immunol. 274 (2003) 269-290
    • (2003) Curr. Top. Microbiol. Immunol. , vol.274 , pp. 269-290
    • Feng, Q.1    Zhang, Y.2
  • 9
    • 19444366179 scopus 로고    scopus 로고
    • Genetic players in esophageal atresia and tracheoesophageal fistula
    • Brunner H.G., and van Bokhoven H. Genetic players in esophageal atresia and tracheoesophageal fistula. Curr. Opin. Genet. Dev. 15 (2005) 341-347
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 341-347
    • Brunner, H.G.1    van Bokhoven, H.2
  • 10
    • 33745906255 scopus 로고    scopus 로고
    • Oesophageal atresia, tracheo-oesophageal fistula, and the VACTERL association: review of genetics and epidemiology
    • Shaw-Smith C. Oesophageal atresia, tracheo-oesophageal fistula, and the VACTERL association: review of genetics and epidemiology. J. Med. Genet. 43 (2006) 545-554
    • (2006) J. Med. Genet. , vol.43 , pp. 545-554
    • Shaw-Smith, C.1
  • 11
    • 0345698603 scopus 로고    scopus 로고
    • Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes
    • Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J., Johnson A.D., Hartzog G.A., and Arndt K.M. Chromatin remodeling protein Chd1 interacts with transcription elongation factors and localizes to transcribed genes. EMBO J. 22 (2003) 1846-1856
    • (2003) EMBO J. , vol.22 , pp. 1846-1856
    • Simic, R.1    Lindstrom, D.L.2    Tran, H.G.3    Roinick, K.L.4    Costa, P.J.5    Johnson, A.D.6    Hartzog, G.A.7    Arndt, K.M.8
  • 13
    • 29244460109 scopus 로고    scopus 로고
    • Double chromodomains cooperate to recognize the methylated histone H3 tail
    • Flanagan J.F., Mi L.Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., et al. Double chromodomains cooperate to recognize the methylated histone H3 tail. Nature 438 (2005) 1181-1185
    • (2005) Nature , vol.438 , pp. 1181-1185
    • Flanagan, J.F.1    Mi, L.Z.2    Chruszcz, M.3    Cymborowski, M.4    Clines, K.L.5    Kim, Y.6
  • 14
    • 29644433964 scopus 로고    scopus 로고
    • Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains
    • Sims III R.J., Chen C.F., Santos-Rosa H., Kouzarides T., Patel S.S., and Reinberg D. Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains. J. Biol. Chem. 280 (2005) 41789-41792
    • (2005) J. Biol. Chem. , vol.280 , pp. 41789-41792
    • Sims III, R.J.1    Chen, C.F.2    Santos-Rosa, H.3    Kouzarides, T.4    Patel, S.S.5    Reinberg, D.6
  • 15
    • 33845760082 scopus 로고    scopus 로고
    • Structural polymorphism of chromodomains in Chd1
    • Okuda M., Horikoshi M., and Nishimura Y. Structural polymorphism of chromodomains in Chd1. J. Mol. Biol. 365 (2007) 1047-1062
    • (2007) J. Mol. Biol. , vol.365 , pp. 1047-1062
    • Okuda, M.1    Horikoshi, M.2    Nishimura, Y.3
  • 16
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin A.C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M., et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440 (2006) 631-636
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1    Aloy, P.2    Grandi, P.3    Krause, R.4    Boesche, M.5    Marzioch, M.6
  • 17
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • Krogan N.J., Cagney G., Yu H., Zhong G., Guo X., Ignatchenko A., et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440 (2006) 637-643
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5    Ignatchenko, A.6
  • 19
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
    • Pray-Grant M.G., Daniel J.A., Schieltz D., Yates III J.R., and Grant P.A. Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation. Nature 433 (2005) 434-438
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 21
    • 0037093537 scopus 로고    scopus 로고
    • The dMi-2 chromodomains are DNA binding modules important for ATP- dependent nucleosome mobilization
    • Bouazoune K., Mitterweger A., Langst G., Imhof A., Akhtar A., Becker P.B., and Brehm A. The dMi-2 chromodomains are DNA binding modules important for ATP- dependent nucleosome mobilization. EMBO J. 21 (2002) 2430-2440
    • (2002) EMBO J. , vol.21 , pp. 2430-2440
    • Bouazoune, K.1    Mitterweger, A.2    Langst, G.3    Imhof, A.4    Akhtar, A.5    Becker, P.B.6    Brehm, A.7
  • 22
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li H., Ilin S., Wang W., Duncan E.M., Wysocka J., Allis C.D., and Patel D.J. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442 (2006) 91-95
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 23
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T., et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature (2006)
    • (2006) Nature
    • Shi, X.1    Hong, T.2    Walter, K.L.3    Ewalt, M.4    Michishita, E.5    Hung, T.6
  • 27
    • 0034693158 scopus 로고    scopus 로고
    • A novel beta- catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation
    • Sakamoto I., Kishida S., Fukui A., Kishida M., Yamamoto H., Hino S., et al. A novel beta- catenin-binding protein inhibits beta-catenin-dependent Tcf activation and axis formation. J. Biol. Chem. 275 (2000) 32871-32878
    • (2000) J. Biol. Chem. , vol.275 , pp. 32871-32878
    • Sakamoto, I.1    Kishida, S.2    Fukui, A.3    Kishida, M.4    Yamamoto, H.5    Hino, S.6
  • 29
    • 0037015030 scopus 로고    scopus 로고
    • Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator
    • Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V., Kashireddy P., et al. Identification of a transcriptionally active peroxisome proliferator-activated receptor alpha -interacting cofactor complex in rat liver and characterization of PRIC285 as a coactivator. Proc. Natl Acad. Sci. USA 99 (2002) 11836-11841
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11836-11841
    • Surapureddi, S.1    Yu, S.2    Bu, H.3    Hashimoto, T.4    Yeldandi, A.V.5    Kashireddy, P.6
  • 31
    • 33746641324 scopus 로고    scopus 로고
    • Nucleosome displacement in transcription
    • Workman J.L. Nucleosome displacement in transcription. Genes Dev. 20 (2006) 2009-2017
    • (2006) Genes Dev. , vol.20 , pp. 2009-2017
    • Workman, J.L.1
  • 32
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: caught in a bind?
    • Sims III R.J., and Reinberg D. Histone H3 Lys 4 methylation: caught in a bind?. Genes Dev. 20 (2006) 2779-2786
    • (2006) Genes Dev. , vol.20 , pp. 2779-2786
    • Sims III, R.J.1    Reinberg, D.2
  • 33
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza M.J., Li B., Florens L., Suganuma T., Swanson S.K., Lee K.K., et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell 123 (2005) 581-592
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3    Suganuma, T.4    Swanson, S.K.5    Lee, K.K.6
  • 34
    • 27744587302 scopus 로고    scopus 로고
    • Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex
    • Keogh M.C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V., Collins S.R., et al. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Cell 123 (2005) 593-605
    • (2005) Cell , vol.123 , pp. 593-605
    • Keogh, M.C.1    Kurdistani, S.K.2    Morris, S.A.3    Ahn, S.H.4    Podolny, V.5    Collins, S.R.6
  • 35
    • 0029901861 scopus 로고    scopus 로고
    • CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes
    • Stokes D.G., Tartof K.D., and Perry R.P. CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes. Proc. Natl Acad. Sci. USA 93 (1996) 7137-7142
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7137-7142
    • Stokes, D.G.1    Tartof, K.D.2    Perry, R.P.3
  • 36
    • 17744371151 scopus 로고    scopus 로고
    • The Drosophila trithorax group protein Kismet facilitates 18an early step in transcriptional elongation by RNA Polymerase II
    • Srinivasan S., Armstrong J.A., Deuring R., Dahlsveen I.K., McNeill H., and Tamkun J.W. The Drosophila trithorax group protein Kismet facilitates 18an early step in transcriptional elongation by RNA Polymerase II. Development 132 (2005) 1623-1635
    • (2005) Development , vol.132 , pp. 1623-1635
    • Srinivasan, S.1    Armstrong, J.A.2    Deuring, R.3    Dahlsveen, I.K.4    McNeill, H.5    Tamkun, J.W.6
  • 37
    • 33750088144 scopus 로고    scopus 로고
    • CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA synthesis
    • Lutz T., Stoger R., and Nieto A. CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA synthesis. FEBS Letters 580 (2006) 5851-5857
    • (2006) FEBS Letters , vol.580 , pp. 5851-5857
    • Lutz, T.1    Stoger, R.2    Nieto, A.3
  • 38
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 419 (2002) 498-511
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3    White, O.4    Berriman, M.5    Hyman, R.W.6
  • 40
    • 33845386531 scopus 로고    scopus 로고
    • Dual infection with HIV and malaria fuels the spread of both diseases in Sub-Saharan Africa
    • Abu-Raddad L.J., Patnaik P., and Kublin J.G. Dual infection with HIV and malaria fuels the spread of both diseases in Sub-Saharan Africa. Science 314 (2006) 1603-1606
    • (2006) Science , vol.314 , pp. 1603-1606
    • Abu-Raddad, L.J.1    Patnaik, P.2    Kublin, J.G.3
  • 41
    • 1042276983 scopus 로고    scopus 로고
    • Assays for the determination of structure and dynamics of the interaction of the chromodomain with histone peptides
    • Jacobs S.A., Fischle W., and Khorasanizadeh S. Assays for the determination of structure and dynamics of the interaction of the chromodomain with histone peptides. Methods Enzymol. 376 (2004) 131-148
    • (2004) Methods Enzymol. , vol.376 , pp. 131-148
    • Jacobs, S.A.1    Fischle, W.2    Khorasanizadeh, S.3
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallog. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallog. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 44
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building with iterative structure refinement
    • Perrakis A., Morris R.J., and Lamzin V.S. Automated protein model building with iterative structure refinement. Nature Struct. Biol. 6 (1999) 458-468
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-468
    • Perrakis, A.1    Morris, R.J.2    Lamzin, V.S.3
  • 45
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P., and Cowtan K. COOT: Model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 49
    • 34247598269 scopus 로고    scopus 로고
    • Felsenstein, J. (2005). PHYLIP (Phylogeny Inference Package) version 3.65.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.