메뉴 건너뛰기




Volumn 73, Issue 1, 2010, Pages 99-106

Production and characterization of recombinant protein preparations of Endonuclease G-homologs from yeast, C. elegans and humans

Author keywords

Apoptosis; DNA repair; Endonuclease; Exonuclease; Mitochondria; Refolding

Indexed keywords


EID: 77955365267     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.04.001     Document Type: Article
Times cited : (14)

References (27)
  • 1
    • 46549086527 scopus 로고    scopus 로고
    • Mitochondrial death pathways in yeast and mammalian cells
    • W.C. Cheng, K.M. Leach, J.M. Hardwick, Mitochondrial death pathways in yeast and mammalian cells, Biochim. Biophys. Acta 1783 (2008) 1272-1279.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1272-1279
    • Cheng, W.C.1    Leach, K.M.2    Hardwick, J.M.3
  • 2
    • 34247469791 scopus 로고    scopus 로고
    • The mitochondrial pathway in yeast apoptosis
    • T. Eisenberg, S. Buttner, G. Kroemer, F. Madeo, The mitochondrial pathway in yeast apoptosis, Apoptosis 12 (2007) 1011-1023.
    • (2007) Apoptosis , vol.12 , pp. 1011-1023
    • Eisenberg, T.1    Buttner, S.2    Kroemer, G.3    Madeo, F.4
  • 4
    • 0037343170 scopus 로고    scopus 로고
    • Mitochondrial Endonuclease G function in apoptosis and mtDNA metabolism: A historical perspective
    • R.L. Low, Mitochondrial Endonuclease G function in apoptosis and mtDNA metabolism: a historical perspective, Mitochondrion 2 (2003) 225-236.
    • (2003) Mitochondrion , vol.2 , pp. 225-236
    • Low, R.L.1
  • 5
    • 56549114782 scopus 로고    scopus 로고
    • Leishmania infantum expresses a mitochondrial nuclease homologous to EndoG that migrates to the nucleus in response to an apoptotic stimulus
    • E. Rico, J.F. Alzate, A.A. Arias, D. Moreno, J. Clos, F. Gago, I. Moreno, M. Dominguez, A. Jimenez-Ruiz, Leishmania infantum expresses a mitochondrial nuclease homologous to EndoG that migrates to the nucleus in response to an apoptotic stimulus, Mol. Biochem. Parasitol. 163 (2009) 28-38.
    • (2009) Mol. Biochem. Parasitol. , vol.163 , pp. 28-38
    • Rico, E.1    Alzate, J.F.2    Arias, A.A.3    Moreno, D.4    Clos, J.5    Gago, F.6    Moreno, I.7    M. Dominguez8    Jimenez-Ruiz, A.9
  • 6
    • 39449083014 scopus 로고    scopus 로고
    • Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites
    • S. Gannavaram, C. Vedvyas, A. Debrabant, Conservation of the pro-apoptotic nuclease activity of endonuclease G in unicellular trypanosomatid parasites, J. Cell Sci. 121 (2008) 99-109.
    • (2008) J. Cell Sci. , vol.121 , pp. 99-109
    • Gannavaram, S.1    Vedvyas, C.2    Debrabant, A.3
  • 8
    • 33846652860 scopus 로고    scopus 로고
    • Yeast endonuclease G: Complex matters of death, and of life
    • W.C. Burhans, M. Weinberger, Yeast endonuclease G: complex matters of death, and of life, Mol. Cell 25 (2007) 323-325.
    • (2007) Mol. Cell , vol.25 , pp. 323-325
    • Burhans, W.C.1    Weinberger, M.2
  • 9
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • X. Wang, C. Yang, J. Chai, Y. Shi, D. Xue, Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans, Science 298 (2002) 1587-1592.
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 10
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • J. Parrish, L. Li, K. Klotz, D. Ledwich, X. Wang, D. Xue, Mitochondrial endonuclease G is important for apoptosis in C. elegans, Nature 412 (2001) 90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 11
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • D. Arnoult, B. Gaume, M. Karbowski, J.C. Sharpe, F. Cecconi, R.J. Youle, Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization, EMBO J. 22 (2003) 4385-4399.
    • (2003) EMBO J. , vol.22 , pp. 4385-4399
    • Arnoult, D.1    Gaume, B.2    Karbowski, M.3    Sharpe, J.C.4    Cecconi, F.5    Youle, R.J.6
  • 13
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • L.Y. Li, X. Luo, X. Wang, Endonuclease G is an apoptotic DNase when released from mitochondria, Nature 412 (2001) 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 14
    • 33745171416 scopus 로고    scopus 로고
    • Endonuclease G: A role for the enzyme in recombination and cellular proliferation
    • K.J. Huang, C.C. Ku, I.R. Lehman, Endonuclease G: a role for the enzyme in recombination and cellular proliferation, Proc. Natl. Acad. Sci. USA 103 (2006) 8995-9000.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8995-9000
    • Huang, K.J.1    Ku, C.C.2    Lehman, I.R.3
  • 16
    • 0028012341 scopus 로고
    • Analysis of the role of the NUC1 endo/ exonuclease in yeast mitochondrial DNA recombination
    • H.P. Zassenhaus, G. Denniger, Analysis of the role of the NUC1 endo/ exonuclease in yeast mitochondrial DNA recombination, Curr. Genet. 25 (1994) 142-149.
    • (1994) Curr. Genet. , vol.25 , pp. 142-149
    • Zassenhaus, H.P.1    Denniger, G.2
  • 17
    • 0024278708 scopus 로고
    • Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae
    • E. Dake, T.J. Hofmann, S. McIntire, A. Hudson, H.P. Zassenhaus, Purification and properties of the major nuclease from mitochondria of Saccharomyces cerevisiae, J. Biol. Chem. 263 (1988) 7691-7702.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7691-7702
    • Dake, E.1    Hofmann, T.J.2    McIntire, S.3    Hudson, A.4    Zassenhaus, H.P.5
  • 18
    • 0023283902 scopus 로고
    • Endonuclease G: A (dG) n X (dC)n-specific DNase from higher eukaryotes
    • A. Ruiz-Carrillo, J. Renaud, Endonuclease G: a (dG)n X (dC)n-specific DNase from higher eukaryotes, EMBO J. 6 (1987) 401-407.
    • (1987) EMBO J. , vol.6 , pp. 401-407
    • Ruiz-Carrillo, A.1    Renaud, J.2
  • 19
    • 0024978057 scopus 로고
    • Recognition of (dG)n.(dC)n sequences by endonuclease G. Characterization of the calf thymus nuclease
    • J. Cote, J. Renaud, A. Ruiz-Carrillo, Recognition of (dG)n.(dC)n sequences by endonuclease G. Characterization of the calf thymus nuclease, J. Biol. Chem. 264 (1989) 3301-3310.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3301-3310
    • Cote, J.1    Renaud, J.2    Ruiz-Carrillo, A.3
  • 21
    • 0032006766 scopus 로고    scopus 로고
    • Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and its inhibitor NuiA
    • G. Meiss, I. Franke, O. Gimadutdinow, C. Urbanke, A. Pingoud, Biochemical characterization of Anabaena sp. strain PCC 7120 non-specific nuclease NucA and its inhibitor NuiA, Eur. J. Biochem. 251 (1998) 924-934.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 924-934
    • Meiss, G.1    Franke, I.2    Gimadutdinow, O.3    Urbanke, C.4    Pingoud, A.5
  • 23
    • 36148984593 scopus 로고    scopus 로고
    • 2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease
    • M. Saravanan, K. Vasu, S. Ghosh, V. Nagaraja, Dual role for Zn2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease, J. Biol. Chem. 282 (2007) 32320-32326.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32320-32326
    • Saravanan, M.1    Vasu, K.2    Ghosh, S.3    Nagaraja, V.4
  • 24
    • 75349114909 scopus 로고    scopus 로고
    • Crystal structure of the EndoG/ EndoGI complex: Mechanism of EndoG inhibition
    • B. Loll, M. Gebhardt, E. Wahle, A. Meinhart, Crystal structure of the EndoG/ EndoGI complex: mechanism of EndoG inhibition, Nucleic Acids Res. 37 (2009) 7312-7320.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7312-7320
    • Loll, B.1    Gebhardt, M.2    Wahle, E.3    Meinhart, A.4
  • 25
    • 0035930523 scopus 로고    scopus 로고
    • Action of recombinant human apoptotic endonuclease G on naked DNA and chromatin substrates: Cooperation with exonuclease and DNase I
    • P. Widlak, L.Y. Li, X. Wang, W.T. Garrard, Action of recombinant human apoptotic endonuclease G on naked DNA and chromatin substrates: cooperation with exonuclease and DNase I, J. Biol. Chem. 276 (2001) 48404-48409.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48404-48409
    • Widlak, P.1    Li, L.Y.2    Wang, X.3    Garrard, W.T.4
  • 26
    • 23944462470 scopus 로고    scopus 로고
    • Regulation of the human apoptotic DNase/RNase Endonuclease G: Involvement of Hsp70 and ATP
    • M. Kalinowska, W. Garncarz, M. Pietrowska, W.T. Garrard, P. Widlak, Regulation of the human apoptotic DNase/RNase Endonuclease G: involvement of Hsp70 and ATP, Apoptosis 10 (2005) 821-830.
    • (2005) Apoptosis , vol.10 , pp. 821-830
    • Kalinowska, M.1    Garncarz, W.2    Pietrowska, M.3    Garrard, W.T.4    Widlak, P.5
  • 27
    • 1842452746 scopus 로고    scopus 로고
    • Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis
    • P. Schafer, S.R. Scholz, O. Gimadutdinow, I.A. Cymerman, J.M. Bujnicki, A. Ruiz- Carrillo, A. Pingoud, G. Meiss, Structural and functional characterization of mitochondrial EndoG, a sugar non-specific nuclease which plays an important role during apoptosis, J. Mol. Biol. 338 (2004) 217-228.
    • (2004) J. Mol. Biol. , vol.338 , pp. 217-228
    • Schafer, P.1    Scholz, S.R.2    Gimadutdinow, O.3    Cymerman, I.A.4    Bujnicki, J.M.5    Ruiz- Carrillo, A.6    Pingoud, A.7    Meiss, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.