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Volumn 23, Issue 6, 2011, Pages 2285-2301

Transcription factor-dependent chromatin remodeling at heat shock and copper-responsive promoters in chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS REINHARDTII; CHLOROPHYTA;

EID: 79960888467     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.111.085266     Document Type: Article
Times cited : (60)

References (73)
  • 1
    • 0034326355 scopus 로고    scopus 로고
    • What does 'chromatin remodeling' mean
    • Aalfs, J.D., and Kingston, R.E. (2000). What does 'chromatin remodeling' mean? Trends Biochem. Sci. 25: 548-555.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 548-555
    • Aalfs, J.D.1    Kingston, R.E.2
  • 2
    • 0021100706 scopus 로고
    • Acetylation and methylation patterns of core his-tones are modified after heat or arsenite treatment of Drosophila tissue culture cells
    • Arrigo, A.P. (1983). Acetylation and methylation patterns of core his-tones are modified after heat or arsenite treatment of Drosophila tissue culture cells. Nucleic Acids Res. 11: 1389-1404.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1389-1404
    • Arrigo, A.P.1
  • 5
    • 33746828109 scopus 로고    scopus 로고
    • Molecular recognition of histone H3 by the WD40 protein WDR5
    • Couture, J.F., Collazo, E., and Trievel, R.C. (2006). Molecular recognition of histone H3 by the WD40 protein WDR5. Nat. Struct. Mol. Biol. 13: 698-703.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 698-703
    • Couture, J.F.1    Collazo, E.2    Trievel, R.C.3
  • 6
    • 0024743663 scopus 로고
    • The argininosucci-nate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus
    • Debuchy, R., Purton, S., and Rochaix, J.D. (1989). The argininosucci-nate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus. EMBO J. 8: 2803-2809.
    • (1989) EMBO J , vol.8 , pp. 2803-2809
    • Debuchy, R.1    Purton, S.2    Rochaix, J.D.3
  • 8
    • 77952782916 scopus 로고    scopus 로고
    • Chloroplast DnaJ-like proteins 3 and 4 (CDJ3/4) from Chlamydomonas reinhardtii contain redox-active Fe-S clusters and interact with stromal HSP70B
    • Dorn, K.V., Willmund, F., Schwarz, C., Henselmann, C., Pohl, T., Hess, B., Veyel, D., Usadel, B., Friedrich, T., Nickelsen, J., and Schroda, M. (2010). Chloroplast DnaJ-like proteins 3 and 4 (CDJ3/4) from Chlamydomonas reinhardtii contain redox-active Fe-S clusters and interact with stromal HSP70B. Biochem. J. 427: 205-215.
    • (2010) Biochem. J , vol.427 , pp. 205-215
    • Dorn, K.V.1    Willmund, F.2    Schwarz, C.3    Henselmann, C.4    Pohl, T.5    Hess, B.6    Veyel, D.7    Usadel, B.8    Friedrich, T.9    Nickelsen, J.10    Schroda, M.11
  • 9
    • 8544234958 scopus 로고    scopus 로고
    • Genetic dissection of nutritional copper signaling in Chlamydomonas distinguishes regulatory and target genes
    • Eriksson, M., Moseley, J.L., Tottey, S., Del Campo, J.A., Quinn, J., Kim, Y., and Merchant, S. (2004). Genetic dissection of nutritional copper signaling in Chlamydomonas distinguishes regulatory and target genes. Genetics 168: 795-807.
    • (2004) Genetics , vol.168 , pp. 795-807
    • Eriksson, M.1    Moseley, J.L.2    Tottey, S.3    del Campo, J.A.4    Quinn, J.5    Kim, Y.6    Merchant, S.7
  • 10
    • 33749631536 scopus 로고    scopus 로고
    • Displacement of histones at promoters of Saccharomyces cerevisiae heat shock genes is differentially associated with histone H3 acetylation
    • Erkina, T.Y., and Erkine, A.M. (2006). Displacement of histones at promoters of Saccharomyces cerevisiae heat shock genes is differentially associated with histone H3 acetylation. Mol. Cell. Biol. 26: 7587-7600.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 7587-7600
    • Erkina, T.Y.1    Erkine, A.M.2
  • 11
    • 77950483916 scopus 로고    scopus 로고
    • Functional interplay between chromatin remodeling complexes RSC, SWI/SNF and ISWI in regulation of yeast heat shock genes
    • Erkina, T.Y., Zou, Y., Freeling, S., Vorobyev, V.I., and Erkine, A.M. (2010). Functional interplay between chromatin remodeling complexes RSC, SWI/SNF and ISWI in regulation of yeast heat shock genes. Nucleic Acids Res. 38: 1441-1449.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1441-1449
    • Erkina, T.Y.1    Zou, Y.2    Freeling, S.3    Vorobyev, V.I.4    Erkine, A.M.5
  • 13
    • 34250369627 scopus 로고    scopus 로고
    • FAIRE (Formaldehyde-Assisted Isolation of Regulatory Elements) isolates active regulatory elements from human chromatin
    • Giresi, P.G., Kim, J., McDaniell, R.M., Iyer, V.R., and Lieb, J.D. (2007). FAIRE (Formaldehyde-Assisted Isolation of Regulatory Elements) isolates active regulatory elements from human chromatin. Genome Res. 17: 877-885.
    • (2007) Genome Res , vol.17 , pp. 877-885
    • Giresi, P.G.1    Kim, J.2    McDaniell, R.M.3    Iyer, V.R.4    Lieb, J.D.5
  • 14
    • 0023042758 scopus 로고
    • Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii
    • Goldschmidt-Clermont, M., and Rahire, M. (1986). Sequence, evolution and differential expression of the two genes encoding variant small subunits of ribulose bisphosphate carboxylase/oxygenase in Chlamydomonas reinhardtii. J. Mol. Biol. 191: 421-432.
    • (1986) J. Mol. Biol , vol.191 , pp. 421-432
    • Goldschmidt-Clermont, M.1    Rahire, M.2
  • 16
    • 0036809333 scopus 로고    scopus 로고
    • SHsps and their role in the chaperone network
    • Haslbeck, M. (2002). sHsps and their role in the chaperone network. Cell. Mol. Life Sci. 59: 1649-1657.
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1649-1657
    • Haslbeck, M.1
  • 17
    • 34249744467 scopus 로고    scopus 로고
    • Mapping and characterization of DNase I hypersensitive sites in Arabidopsis chromatin
    • Kodama, Y., Nagaya, S., Shinmyo, A., and Kato, K. (2007). Mapping and characterization of DNase I hypersensitive sites in Arabidopsis chromatin. Plant Cell Physiol. 48: 459-470.
    • (2007) Plant Cell Physiol , vol.48 , pp. 459-470
    • Kodama, Y.1    Nagaya, S.2    Shinmyo, A.3    Kato, K.4
  • 18
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. (2007). Chromatin modifications and their function. Cell 128: 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 19
    • 70450277187 scopus 로고    scopus 로고
    • SAGA and Rpd3 chromatin modification complexes dynamically regulate heat shock gene structure and expression
    • Kremer, S.B., and Gross, D.S. (2009). SAGA and Rpd3 chromatin modification complexes dynamically regulate heat shock gene structure and expression. J. Biol. Chem. 284: 32914-32931.
    • (2009) J. Biol. Chem , vol.284 , pp. 32914-32931
    • Kremer, S.B.1    Gross, D.S.2
  • 21
    • 29444433851 scopus 로고    scopus 로고
    • A regulator of nutritional copper signaling in Chlamydomonas is an SBP domain protein that recognizes the GTAC core of copper response element
    • Kropat, J., Tottey, S., Birkenbihl, R.P., Depége, N., Huijser, P., and Merchant, S. (2005). A regulator of nutritional copper signaling in Chlamydomonas is an SBP domain protein that recognizes the GTAC core of copper response element. Proc. Natl. Acad. Sci. USA 102: 18730-18735.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18730-18735
    • Kropat, J.1    Tottey, S.2    Birkenbihl, R.P.3    Depége, N.4    Huijser, P.5    Merchant, S.6
  • 22
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M., and Jenuwein, T. (2002). The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14: 286-298.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 23
    • 3543023310 scopus 로고    scopus 로고
    • Evidence for nucleosome depletion at active regulatory regions genome-wide
    • Lee, C.K., Shibata, Y., Rao, B., Strahl, B.D., and Lieb, J.D. (2004). Evidence for nucleosome depletion at active regulatory regions genome-wide. Nat. Genet. 36: 900-905.
    • (2004) Nat. Genet , vol.36 , pp. 900-905
    • Lee, C.K.1    Shibata, Y.2    Rao, B.3    Strahl, B.D.4    Lieb, J.D.5
  • 24
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • Lee, J.H., Hübel, A., and Schöffl, F. (1995). Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant J. 8: 603-612.
    • (1995) Plant J , vol.8 , pp. 603-612
    • Lee, J.H.1    Hübel, A.2    Schöffl, F.3
  • 26
    • 33847070442 scopus 로고    scopus 로고
    • The role of chromatin during transcription
    • Li, B., Carey, M., and Workman, J.L. (2007). The role of chromatin during transcription. Cell 128: 707-719.
    • (2007) Cell , vol.128 , pp. 707-719
    • Li, B.1    Carey, M.2    Workman, J.L.3
  • 27
    • 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. (2006). Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442: 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
  • 28
    • 14844293494 scopus 로고    scopus 로고
    • J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1
    • Liu, C., Willmund, F., Whitelegge, J.P., Hawat, S., Knapp, B., Lodha, M., and Schroda, M. (2005). J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1. Mol. Biol. Cell 16: 1165-1177.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1165-1177
    • Liu, C.1    Willmund, F.2    Whitelegge, J.P.3    Hawat, S.4    Knapp, B.5    Lodha, M.6    Schroda, M.7
  • 29
    • 26844485822 scopus 로고    scopus 로고
    • Analysis of chromatin structure in the control regions of the Chlamydomonas HSP70A and RBCS2 genes
    • Lodha, M., and Schroda, M. (2005). Analysis of chromatin structure in the control regions of the Chlamydomonas HSP70A and RBCS2 genes. Plant Mol. Biol. 59: 501-513.
    • (2005) Plant Mol. Biol , vol.59 , pp. 501-513
    • Lodha, M.1    Schroda, M.2
  • 30
    • 40649109127 scopus 로고    scopus 로고
    • A new assay for promoter analysis in Chlamydomonas reveals roles for heat shock elements and the TATA box in HSP70A promoter-mediated activation of transgene expression
    • Lodha, M., Schulz-Raffelt, M., and Schroda, M. (2008). A new assay for promoter analysis in Chlamydomonas reveals roles for heat shock elements and the TATA box in HSP70A promoter-mediated activation of transgene expression. Eukaryot. Cell 7: 172-176.
    • (2008) Eukaryot. Cell , vol.7 , pp. 172-176
    • Lodha, M.1    Schulz-Raffelt, M.2    Schroda, M.3
  • 31
    • 0037381213 scopus 로고    scopus 로고
    • Structure and dynamic behavior of nucleosomes
    • Luger, K. (2003). Structure and dynamic behavior of nucleosomes. Curr. Opin. Genet. Dev. 13: 127-135.
    • (2003) Curr. Opin. Genet. Dev , vol.13 , pp. 127-135
    • Luger, K.1
  • 32
    • 0022641081 scopus 로고
    • Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi
    • Merchant, S., and Bogorad, L. (1986). Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi. Mol. Cell. Biol. 6: 462-469.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 462-469
    • Merchant, S.1    Bogorad, L.2
  • 33
    • 0023405243 scopus 로고
    • Metal ion regulated gene expression: Use of a plastocyanin-less mutant of Chlamydomonas reinhardtii to study the Cu(II)-dependent expression of cytochrome c-552
    • Merchant, S., and Bogorad, L. (1987). Metal ion regulated gene expression: Use of a plastocyanin-less mutant of Chlamydomonas reinhardtii to study the Cu(II)-dependent expression of cytochrome c-552. EMBO J. 6: 2531-2535.
    • (1987) EMBO J , vol.6 , pp. 2531-2535
    • Merchant, S.1    Bogorad, L.2
  • 35
    • 0034658505 scopus 로고    scopus 로고
    • The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii
    • Moseley, J., Quinn, J., Eriksson, M., and Merchant, S. (2000). The Crd1 gene encodes a putative di-iron enzyme required for photosystem I accumulation in copper deficiency and hypoxia in Chlamydomonas reinhardtii. EMBO J. 19: 2139-2151.
    • (2000) EMBO J , vol.19 , pp. 2139-2151
    • Moseley, J.1    Quinn, J.2    Eriksson, M.3    Merchant, S.4
  • 36
    • 0026608847 scopus 로고
    • Structure of a gene encoding heat-shock protein HSP70 from the unicellular alga Chla-mydomonas reinhardtii
    • Müller, F.W., Igloi, G.L., and Beck, C.F. (1992). Structure of a gene encoding heat-shock protein HSP70 from the unicellular alga Chla-mydomonas reinhardtii. Gene 111: 165-173.
    • (1992) Gene , vol.111 , pp. 165-173
    • Müller, F.W.1    Igloi, G.L.2    Beck, C.F.3
  • 37
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng, H.H., Robert, F., Young, R.A., and Struhl, K. (2003). Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell 11: 709-719.
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 38
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodo-main of histone acetyltransferase gcn5p
    • Owen, D.J., Ornaghi, P., Yang, J.C., Lowe, N., Evans, P.R., Ballario, P., Neuhaus, D., Filetici, P., and Travers, A.A. (2000). The structural basis for the recognition of acetylated histone H4 by the bromodo-main of histone acetyltransferase gcn5p. EMBO J. 19: 6141-6149.
    • (2000) EMBO J , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 39
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene
    • Pelham, H.R. (1982). A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell 30: 517-528.
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.1
  • 41
    • 23944462969 scopus 로고    scopus 로고
    • Genome-wide map of nucleosome acetylation and methylation in yeast
    • Pokholok, D.K., et al. (2005). Genome-wide map of nucleosome acetylation and methylation in yeast. Cell 122: 517-527.
    • (2005) Cell , vol.122 , pp. 517-527
    • Pokholok, D.K.1
  • 42
    • 0029294085 scopus 로고
    • Two copper-responsive elements associated with the Chlamydomonas Cyc6 gene function as targets for transcriptional activators
    • Quinn, J.M., and Merchant, S. (1995). Two copper-responsive elements associated with the Chlamydomonas Cyc6 gene function as targets for transcriptional activators. Plant Cell 7: 623-628.
    • (1995) Plant Cell , vol.7 , pp. 623-628
    • Quinn, J.M.1    Merchant, S.2
  • 43
    • 0031721060 scopus 로고    scopus 로고
    • Copper-responsive gene expression during adaptation to copper deficiency
    • Quinn, J.M., and Merchant, S. (1998). Copper-responsive gene expression during adaptation to copper deficiency. Methods Enzymol. 297: 263-279.
    • (1998) Methods Enzymol , vol.297 , pp. 263-279
    • Quinn, J.M.1    Merchant, S.2
  • 44
    • 0033553513 scopus 로고    scopus 로고
    • Induction of coproporphyrinogen oxidase in Chlamydomonas chloroplasts occurs via transcriptional regulation of Cpx1 mediated by copper response elements and increased translation from a copper deficiency-specific form of the transcript
    • Quinn, J.M., Nakamoto, S.S., and Merchant, S. (1999). Induction of coproporphyrinogen oxidase in Chlamydomonas chloroplasts occurs via transcriptional regulation of Cpx1 mediated by copper response elements and increased translation from a copper deficiency-specific form of the transcript. J. Biol. Chem. 274: 14444-14454.
    • (1999) J. Biol. Chem , vol.274 , pp. 14444-14454
    • Quinn, J.M.1    Nakamoto, S.S.2    Merchant, S.3
  • 45
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran, S.K., Haroun, R.I., Clos, J., Wisniewski, J., and Wu, C. (1993). Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper. Science 259: 230-234.
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 46
    • 0034515772 scopus 로고    scopus 로고
    • Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase
    • Reid, J.L., Iyer, V.R., Brown, P.O., and Struhl, K. (2000). Coordinate regulation of yeast ribosomal protein genes is associated with targeted recruitment of Esa1 histone acetylase. Mol. Cell 6: 1297-1307.
    • (2000) Mol. Cell , vol.6 , pp. 1297-1307
    • Reid, J.L.1    Iyer, V.R.2    Brown, P.O.3    Struhl, K.4
  • 47
    • 0038094502 scopus 로고    scopus 로고
    • Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter
    • Reinke, H., and Hörz, W. (2003). Histones are first hyperacetylated and then lose contact with the activated PHO5 promoter. Mol. Cell 11: 1599-1607.
    • (2003) Mol. Cell , vol.11 , pp. 1599-1607
    • Reinke, H.1    Hörz, W.2
  • 51
    • 77956182394 scopus 로고    scopus 로고
    • An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance
    • Schmollinger, S., Strenkert, D., and Schroda, M. (2010). An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance. Curr. Genet. 56: 383-389.
    • (2010) Curr. Genet , vol.56 , pp. 383-389
    • Schmollinger, S.1    Strenkert, D.2    Schroda, M.3
  • 53
    • 0036690768 scopus 로고    scopus 로고
    • Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas
    • Schroda, M., Beck, C.F., and Vallon, O. (2002). Sequence elements within an HSP70 promoter counteract transcriptional transgene silencing in Chlamydomonas. Plant J. 31: 445-455.
    • (2002) Plant J , vol.31 , pp. 445-455
    • Schroda, M.1    Beck, C.F.2    Vallon, O.3
  • 54
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • Schroda, M., Blöcker, D., and Beck, C.F. (2000). The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J. 21: 121-131.
    • (2000) Plant J , vol.21 , pp. 121-131
    • Schroda, M.1    Blöcker, D.2    Beck, C.F.3
  • 56
    • 35148813020 scopus 로고    scopus 로고
    • Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas
    • Schulz-Raffelt, M., Lodha, M., and Schroda, M. (2007). Heat shock factor 1 is a key regulator of the stress response in Chlamydomonas. Plant J. 52: 286-295.
    • (2007) Plant J , vol.52 , pp. 286-295
    • Schulz-Raffelt, M.1    Lodha, M.2    Schroda, M.3
  • 57
    • 45849153073 scopus 로고    scopus 로고
    • The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nu-cleosome eviction at the HTLV-1 promoter
    • Sharma, N., and Nyborg, J.K. (2008). The coactivators CBP/p300 and the histone chaperone NAP1 promote transcription-independent nu-cleosome eviction at the HTLV-1 promoter. Proc. Natl. Acad. Sci. USA 105: 7959-7963.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7959-7963
    • Sharma, N.1    Nyborg, J.K.2
  • 58
    • 33745868054 scopus 로고    scopus 로고
    • ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
    • Shi, X., et al. (2006). ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442: 96-99.
    • (2006) Nature , vol.442 , pp. 96-99
    • Shi, X.1
  • 59
    • 33751116960 scopus 로고    scopus 로고
    • Histone H3 Lys 4 methylation: Caught in a bind
    • Sims III R.J., and Reinberg, D. (2006). Histone H3 Lys 4 methylation: Caught in a bind? Genes Dev. 20: 2779-2786.
    • (2006) Genes Dev , vol.20 , pp. 2779-2786
    • Sims, R.J.1    Reinberg, D.2
  • 60
    • 79551650614 scopus 로고    scopus 로고
    • The CRR1 nutritional copper sensor in Chlamydomonas contains two distinct metal-responsive domains
    • Sommer, F., Kropat, J., Malasarn, D., Grossoehme, N.E., Chen, X., Giedroc, D.P., and Merchant, S.S. (2010). The CRR1 nutritional copper sensor in Chlamydomonas contains two distinct metal-responsive domains. Plant Cell 22: 4098-4113.
    • (2010) Plant Cell , vol.22 , pp. 4098-4113
    • Sommer, F.1    Kropat, J.2    Malasarn, D.3    Grossoehme, N.E.4    Chen, X.5    Giedroc, D.P.6    Merchant, S.S.7
  • 61
    • 0023643235 scopus 로고
    • Heat shock factor is regulated differently in yeast and HeLa cells
    • Sorger, P.K., Lewis, M.J., and Pelham, H.R. (1987). Heat shock factor is regulated differently in yeast and HeLa cells. Nature 329: 81-84.
    • (1987) Nature , vol.329 , pp. 81-84
    • Sorger, P.K.1    Lewis, M.J.2    Pelham, H.R.3
  • 62
    • 0024852809 scopus 로고
    • Trimerization of a yeast tran-scriptional activator via a coiled-coil motif
    • Sorger, P.K., and Nelson, H.C. (1989). Trimerization of a yeast tran-scriptional activator via a coiled-coil motif. Cell 59: 807-813.
    • (1989) Cell , vol.59 , pp. 807-813
    • Sorger, P.K.1    Nelson, H.C.2
  • 63
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger, P.K., and Pelham, H.R. (1988). Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54: 855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.2
  • 66
    • 33750210385 scopus 로고    scopus 로고
    • Identification of a plastid response element that acts as an enhancer within the Chlamydomonas HSP70A promoter
    • von Gromoff, E.D., Schroda, M., Oster, U., and Beck, C.F. (2006). Identification of a plastid response element that acts as an enhancer within the Chlamydomonas HSP70A promoter. Nucleic Acids Res. 34: 4767-4779.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4767-4779
    • von Gromoff, E.D.1    Schroda, M.2    Oster, U.3    Beck, C.F.4
  • 67
    • 0024722271 scopus 로고
    • Three light-inducible heat shock genes of Chlamydomonas reinhardtii
    • von Gromoff, E.D., Treier, U., and Beck, C.F. (1989). Three light-inducible heat shock genes of Chlamydomonas reinhardtii. Mol. Cell. Biol. 9: 3911-3918.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 3911-3918
    • von Gromoff, E.D.1    Treier, U.2    Beck, C.F.3
  • 68
    • 0029379757 scopus 로고
    • Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and methylation
    • Waterborg, J.H., Robertson, A.J., Tatar, D.L., Borza, C.M., and Davie, J.R. (1995). Histones of Chlamydomonas reinhardtii. Synthesis, acetylation, and methylation. Plant Physiol. 109: 393-407.
    • (1995) Plant Physiol , vol.109 , pp. 393-407
    • Waterborg, J.H.1    Robertson, A.J.2    Tatar, D.L.3    Borza, C.M.4    Davie, J.R.5
  • 69
    • 33644666048 scopus 로고    scopus 로고
    • HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamy-domonas reinhardtii
    • Willmund, F., and Schroda, M. (2005). HEAT SHOCK PROTEIN 90C is a bona fide Hsp90 that interacts with plastidic HSP70B in Chlamy-domonas reinhardtii. Plant Physiol. 138: 2310-2322.
    • (2005) Plant Physiol , vol.138 , pp. 2310-2322
    • Willmund, F.1    Schroda, M.2
  • 70
    • 0017899881 scopus 로고
    • Interchangeable copper and iron proteins in algal photosynthesis. Studies on plastocyanin and cytochrome c-552 in Chlamydomonas
    • Wood, P.M. (1978). Interchangeable copper and iron proteins in algal photosynthesis. Studies on plastocyanin and cytochrome c-552 in Chlamydomonas. Eur. J. Biochem. 87: 9-19.
    • (1978) Eur. J. Biochem , vol.87 , pp. 9-19
    • Wood, P.M.1
  • 71
    • 77954487796 scopus 로고    scopus 로고
    • Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
    • Zeng, L., Zhang, Q., Li, S., Plotnikov, A.N., Walsh, M.J., and Zhou, M.M. (2010). Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b. Nature 466: 258-262.
    • (2010) Nature , vol.466 , pp. 258-262
    • Zeng, L.1    Zhang, Q.2    Li, S.3    Plotnikov, A.N.4    Walsh, M.J.5    Zhou, M.M.6
  • 72
    • 0038148033 scopus 로고    scopus 로고
    • Heat stress-dependent DNA binding of Arabidopsis heat shock transcription factor HSF1 to heat shock gene promoters in Arabidopsis suspension culture cells in vivo
    • Zhang, L., Lohmann, C., Prändl, R., and Schöffl, F. (2003). Heat stress-dependent DNA binding of Arabidopsis heat shock transcription factor HSF1 to heat shock gene promoters in Arabidopsis suspension culture cells in vivo. Biol. Chem. 384: 959-963.
    • (2003) Biol. Chem , vol.384 , pp. 959-963
    • Zhang, L.1    Lohmann, C.2    Prändl, R.3    Schöffl, F.4
  • 73
    • 26444545490 scopus 로고    scopus 로고
    • Domain-wide displacement of histones by activated heat shock factor occurs independently of Swi/Snf and is not correlated with RNA polymerase II density
    • Zhao, J., Herrera-Diaz, J., and Gross, D.S. (2005). Domain-wide displacement of histones by activated heat shock factor occurs independently of Swi/Snf and is not correlated with RNA polymerase II density. Mol. Cell. Biol. 25: 8985-8999.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8985-8999
    • Zhao, J.1    Herrera-Diaz, J.2    Gross, D.S.3


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