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Volumn 54, Issue 2, 2007, Pages 204-211

Tri-cistronic cloning, overexpression and purification of human Rad9, Rad1, Hus1 protein complex

Author keywords

Affinity purification; ASEC; Cell cycle checkpoint control; DLS; DNA damage and repair; Heterologous expression; Hus1; Rad1; Rad9; Tri protein complex

Indexed keywords

CELL CYCLE PROTEIN; EXONUCLEASE; HUS1B PROTEIN, HUMAN; PROTEIN RAD9; RAD1 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

EID: 34249102243     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.03.011     Document Type: Article
Times cited : (4)

References (45)
  • 1
    • 2342527027 scopus 로고    scopus 로고
    • DNA damage checkpoint and repair centers
    • Lisby M., and Rothstein R. DNA damage checkpoint and repair centers. Curr. Opin. Cell. Biol. 16 (2004) 328-334
    • (2004) Curr. Opin. Cell. Biol. , vol.16 , pp. 328-334
    • Lisby, M.1    Rothstein, R.2
  • 2
    • 9244251125 scopus 로고    scopus 로고
    • Cell-cycle checkpoints and cancer
    • Kastan M.B., and Bartek J. Cell-cycle checkpoints and cancer. Nature 432 (2004) 316-323
    • (2004) Nature , vol.432 , pp. 316-323
    • Kastan, M.B.1    Bartek, J.2
  • 3
    • 0035797444 scopus 로고    scopus 로고
    • Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint
    • Tercero J.A., and Diffley J.F. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412 (2001) 553-557
    • (2001) Nature , vol.412 , pp. 553-557
    • Tercero, J.A.1    Diffley, J.F.2
  • 4
    • 0029835850 scopus 로고    scopus 로고
    • A meiotic recombination checkpoint controlled by mitotic checkpoint genes
    • Lydall D., Nikolsky Y., Bishop D.K., and Weinert T. A meiotic recombination checkpoint controlled by mitotic checkpoint genes. Nature 383 (1996) 840-843
    • (1996) Nature , vol.383 , pp. 840-843
    • Lydall, D.1    Nikolsky, Y.2    Bishop, D.K.3    Weinert, T.4
  • 5
    • 0030699088 scopus 로고    scopus 로고
    • Role of Schizosaccharomyces pombe RecQ homolog, recombination, and checkpoint genes in UV damage tolerance
    • Murray J.M., Lindsay H.D., Munday C.A., and Carr A.M. Role of Schizosaccharomyces pombe RecQ homolog, recombination, and checkpoint genes in UV damage tolerance. Mol. Cell. Biol. 17 (1997) 6868-6875
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6868-6875
    • Murray, J.M.1    Lindsay, H.D.2    Munday, C.A.3    Carr, A.M.4
  • 6
    • 2642706705 scopus 로고    scopus 로고
    • alters G2-M cell cycle checkpoint arrest following ionizing radiation
    • Davis T.W., et al. alters G2-M cell cycle checkpoint arrest following ionizing radiation. Cancer Res. 58 (1998) 767-778
    • (1998) Cancer Res. , vol.58 , pp. 767-778
    • Davis, T.W.1
  • 7
    • 0029143992 scopus 로고
    • Evidence for a connection between the mismatch repair system and the G2 cell cycle checkpoint
    • Hawn M.T., et al. Evidence for a connection between the mismatch repair system and the G2 cell cycle checkpoint. Cancer Res. 55 (1995) 3721-3725
    • (1995) Cancer Res. , vol.55 , pp. 3721-3725
    • Hawn, M.T.1
  • 8
    • 0026562544 scopus 로고
    • DNA repair mutants defining G2 checkpoint pathways in Schizosaccharomyces pombe
    • al-Khodairy F., and Carr A.M. DNA repair mutants defining G2 checkpoint pathways in Schizosaccharomyces pombe. EMBO J. 11 (1992) 1343-1350
    • (1992) EMBO J. , vol.11 , pp. 1343-1350
    • al-Khodairy, F.1    Carr, A.M.2
  • 9
    • 0028198383 scopus 로고
    • Identification and characterization of new elements involved in checkpoint and feedback controls in fission yeast
    • al-Khodairy F., et al. Identification and characterization of new elements involved in checkpoint and feedback controls in fission yeast. Mol. Biol. Cell. 5 (1994) 147-160
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 147-160
    • al-Khodairy, F.1
  • 10
    • 0026482601 scopus 로고
    • Fission yeast genes involved in coupling mitosis to completion of DNA replication
    • Enoch T., Carr A.M., and Nurse P. Fission yeast genes involved in coupling mitosis to completion of DNA replication. Genes Dev. 6 (1992) 2035-2046
    • (1992) Genes Dev. , vol.6 , pp. 2035-2046
    • Enoch, T.1    Carr, A.M.2    Nurse, P.3
  • 12
    • 0029057336 scopus 로고
    • A single ataxia telangiectasia gene with a product similar to PI-3 kinase
    • Savitsky K., et al. A single ataxia telangiectasia gene with a product similar to PI-3 kinase. Science 268 (1995) 1749-1753
    • (1995) Science , vol.268 , pp. 1749-1753
    • Savitsky, K.1
  • 13
    • 9244229490 scopus 로고    scopus 로고
    • cDNA cloning and gene mapping of a candidate human cell cycle checkpoint protein
    • Cimprich K.A., Shin R.B., Keith C.T., and Schreiber S.L. cDNA cloning and gene mapping of a candidate human cell cycle checkpoint protein. Proc. Natl. Acad. Sci. USA 93 (1996) 2850-2855
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2850-2855
    • Cimprich, K.A.1    Shin, R.B.2    Keith, C.T.3    Schreiber, S.L.4
  • 15
    • 0032842429 scopus 로고    scopus 로고
    • Genomic structure and histological expression pattern in normal testis and seminoma
    • von Deimling F., et al. Genomic structure and histological expression pattern in normal testis and seminoma. Hum. Genet. 105 (1999) 17-27
    • (1999) Hum. Genet. , vol.105 , pp. 17-27
    • von Deimling, F.1
  • 16
    • 0035941021 scopus 로고    scopus 로고
    • ATR and ATRIP: partners in checkpoint signaling
    • Cortez D., Guntuku S., Qin J., and Elledge S.J. ATR and ATRIP: partners in checkpoint signaling. Science 294 (2001) 1713-1716
    • (2001) Science , vol.294 , pp. 1713-1716
    • Cortez, D.1    Guntuku, S.2    Qin, J.3    Elledge, S.J.4
  • 17
    • 0032535726 scopus 로고    scopus 로고
    • cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster
    • Dean F.B., Lian L., and O'Donnell M. cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster. Genomics 54 (1998) 424-436
    • (1998) Genomics , vol.54 , pp. 424-436
    • Dean, F.B.1    Lian, L.2    O'Donnell, M.3
  • 18
    • 0034235463 scopus 로고    scopus 로고
    • Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes
    • Venclovas C., and Thelen M.P. Structure-based predictions of Rad1, Rad9, Hus1 and Rad17 participation in sliding clamp and clamp-loading complexes. Nucleic Acids Res. 28 (2000) 2481-2493
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2481-2493
    • Venclovas, C.1    Thelen, M.P.2
  • 19
    • 0033018634 scopus 로고    scopus 로고
    • The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1
    • St.Onge R.P., Udell C.M., Casselman R., and Davey S. The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1. Mol. Biol. Cell. 10 (1999) 1985-1995
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1985-1995
    • St.Onge, R.P.1    Udell, C.M.2    Casselman, R.3    Davey, S.4
  • 20
    • 0033534613 scopus 로고    scopus 로고
    • Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex
    • Volkmer E., and Karnitz L.M. Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. J. Biol. Chem. 274 (1999) 567-570
    • (1999) J. Biol. Chem. , vol.274 , pp. 567-570
    • Volkmer, E.1    Karnitz, L.M.2
  • 21
    • 0035854804 scopus 로고    scopus 로고
    • Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage-responsive checkpoint complex
    • Burtelow M.A., Roos-Mattjus P.M., Rauen M., Babendure J.R., and Karnitz L.M. Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage-responsive checkpoint complex. J. Biol. Chem. 276 (2001) 25903-25909
    • (2001) J. Biol. Chem. , vol.276 , pp. 25903-25909
    • Burtelow, M.A.1    Roos-Mattjus, P.M.2    Rauen, M.3    Babendure, J.R.4    Karnitz, L.M.5
  • 22
    • 0035658296 scopus 로고    scopus 로고
    • Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complex
    • Kaur R., Kostrub C.F., and Enoch T. Structure-function analysis of fission yeast Hus1-Rad1-Rad9 checkpoint complex. Mol. Biol. Cell. 12 (2001) 3744-3758
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 3744-3758
    • Kaur, R.1    Kostrub, C.F.2    Enoch, T.3
  • 23
    • 0035927713 scopus 로고    scopus 로고
    • ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses
    • Bao S., et al. ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses. Nature 411 (2001) 969-974
    • (2001) Nature , vol.411 , pp. 969-974
    • Bao, S.1
  • 24
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman G.D., O'Donnell M., and Kuriyan J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429 (2004) 724-730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 26
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure
    • Hendrickson W.A., Horton J.R., and LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9 (1990) 1665-1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 27
    • 0016829942 scopus 로고
    • Terminal-sequence analysis of bacterial ribosomal RNA. Correlation between the 3′-terminal-polypyrimidine sequence of 16-S RNA and translational specificity of the ribosome
    • Shine J., and Dalgarno L. Terminal-sequence analysis of bacterial ribosomal RNA. Correlation between the 3′-terminal-polypyrimidine sequence of 16-S RNA and translational specificity of the ribosome. Eur. J. Biochem. 57 (1975) 221-230
    • (1975) Eur. J. Biochem. , vol.57 , pp. 221-230
    • Shine, J.1    Dalgarno, L.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 27144466197 scopus 로고    scopus 로고
    • Production of recombinant proteins in Escherichia coli
    • Schumann W., and Ferreira L. Production of recombinant proteins in Escherichia coli. Genet. Mol. Biol. 17 (2004) 442-453
    • (2004) Genet. Mol. Biol. , vol.17 , pp. 442-453
    • Schumann, W.1    Ferreira, L.2
  • 30
    • 13844271129 scopus 로고    scopus 로고
    • From gene to protein: a review of new and enabling technologies for multi-parallel protein expression
    • Hunt I. From gene to protein: a review of new and enabling technologies for multi-parallel protein expression. Protein Express. Purif. 40 (2005) 1-22
    • (2005) Protein Express. Purif. , vol.40 , pp. 1-22
    • Hunt, I.1
  • 31
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sorensen H.P., and Mortensen K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell Fact. 4 (2005) 1
    • (2005) Microb. Cell Fact. , vol.4 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 32
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen H.P., and Mortensen K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotech. 115 (2005) 113-128
    • (2005) J. Biotech. , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.2
  • 33
    • 0030938085 scopus 로고    scopus 로고
    • Coexpression of nuclear receptor partners increase their solubility and biological activities
    • Li C., Schwabe J., Banayo E., and Evans R. Coexpression of nuclear receptor partners increase their solubility and biological activities. Proc. Natl. Acad. Sci. USA 94 (1997) 2278-2283
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2278-2283
    • Li, C.1    Schwabe, J.2    Banayo, E.3    Evans, R.4
  • 34
    • 0442292534 scopus 로고    scopus 로고
    • Genetically engineered bacterial cells co-expressing human cytochrome P450 with NADPH-cytochrome P450 reductase: Prediction of metabolism and toxicity of drugs in humans
    • Fujita K., and Kamataki T. Genetically engineered bacterial cells co-expressing human cytochrome P450 with NADPH-cytochrome P450 reductase: Prediction of metabolism and toxicity of drugs in humans. Drug Metab. Pharm. 17 (2002) 1-2
    • (2002) Drug Metab. Pharm. , vol.17 , pp. 1-2
    • Fujita, K.1    Kamataki, T.2
  • 36
    • 0028880896 scopus 로고
    • Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography
    • Elce J.S., Hegadorn C., Gauthier S., Vince J.W., and Davies P.L. Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography. Protein Eng. 8 (1995) 843-848
    • (1995) Protein Eng. , vol.8 , pp. 843-848
    • Elce, J.S.1    Hegadorn, C.2    Gauthier, S.3    Vince, J.W.4    Davies, P.L.5
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0027673618 scopus 로고
    • Affinity purification of histidine-tagged proteins
    • Schmitt J., Hess H., and Stunnenberg H.G. Affinity purification of histidine-tagged proteins. Mol. Biol. Reports 18 (1993) 223-230
    • (1993) Mol. Biol. Reports , vol.18 , pp. 223-230
    • Schmitt, J.1    Hess, H.2    Stunnenberg, H.G.3
  • 39
    • 0026333458 scopus 로고
    • Dynamic light scattering studies of the aggregation of lysozyme under crystallization conditions
    • Skouri M., Delsanti M., Munch J.P., Lorber B., and Giege R. Dynamic light scattering studies of the aggregation of lysozyme under crystallization conditions. FEBS Lett. 295 (1991) 84-88
    • (1991) FEBS Lett. , vol.295 , pp. 84-88
    • Skouri, M.1    Delsanti, M.2    Munch, J.P.3    Lorber, B.4    Giege, R.5
  • 41
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6 (1995) 494-500
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 43
    • 0033794367 scopus 로고    scopus 로고
    • High-throughput protein crystallization
    • Stevens R.C. High-throughput protein crystallization. Curr. Opin. Struct. Biol. 10 (2000) 558-563
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 558-563
    • Stevens, R.C.1
  • 44
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G., Shevchenko A., Rutz B., Wilm M., Mann M., and Séraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nature Biotech. 17 (1999) 1030-1032
    • (1999) Nature Biotech. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6


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