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Volumn 29, Issue 2, 2009, Pages 448-457

Crystal structure of CRN-4: Implications for Domain Function in Apoptotic DNA degradation

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DNA FRAGMENT; DOUBLE STRANDED DNA; MANGANESE; NUCLEASE; PROTEIN CRN 4; UNCLASSIFIED DRUG; ZINC;

EID: 58249107985     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01006-08     Document Type: Article
Times cited : (21)

References (51)
  • 1
    • 0035094982 scopus 로고    scopus 로고
    • Host defense, viruses, and apoptosis
    • Barber, G. N. 2001. Host defense, viruses, and apoptosis. Cell Death Differ. 8:113-126.
    • (2001) Cell Death Differ , vol.8 , pp. 113-126
    • Barber, G.N.1
  • 2
    • 0028949817 scopus 로고
    • Intracellular ionic variations in the apoptotic death of L cells by inhibitors of cell cycle progression
    • Barbiero, G., F. Duranti, G. Bonelli, J. S. Amenta, and F. M. Baccino. 1995. Intracellular ionic variations in the apoptotic death of L cells by inhibitors of cell cycle progression. Exp. Cell Res. 217:410-418.
    • (1995) Exp. Cell Res , vol.217 , pp. 410-418
    • Barbiero, G.1    Duranti, F.2    Bonelli, G.3    Amenta, J.S.4    Baccino, F.M.5
  • 3
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. 1974. The genetics of Caenorhabditis elegans. Genetics 77:71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 4
    • 0033664281 scopus 로고    scopus 로고
    • Structure of Escherichia coli exonuclease I suggests how processivity is achieved
    • Breyer, W. A., and B. W. Matthews. 2000. Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat. Struct. Biol. 7:1125-1128.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1125-1128
    • Breyer, W.A.1    Matthews, B.W.2
  • 5
    • 34250303902 scopus 로고    scopus 로고
    • Biochemical and cellular characteristics of the 3′ → 5′ exonuclease TREX2
    • Chen, M. J., S. M. Ma, L. C. Dumitrache, and P. Hasty. 2007. Biochemical and cellular characteristics of the 3′ → 5′ exonuclease TREX2. Nucleic Acids Res. 35:2682-2694.
    • (2007) Nucleic Acids Res , vol.35 , pp. 2682-2694
    • Chen, M.J.1    Ma, S.M.2    Dumitrache, L.C.3    Hasty, P.4
  • 6
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: An initial-stage protein-docking algorithm
    • Chen, R., L. Li, and Z. Weng. 2003. ZDOCK: an initial-stage protein-docking algorithm. Proteins 52:80-87.
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 7
    • 4644324017 scopus 로고    scopus 로고
    • Crystallographic structure of the nuclease domain of 3′hExo, a DEDDh family member, bound to rAMP
    • Cheng, Y., and D. J. Patel. 2004. Crystallographic structure of the nuclease domain of 3′hExo, a DEDDh family member, bound to rAMP. J. Mol. Biol. 343:305-312.
    • (2004) J. Mol. Biol , vol.343 , pp. 305-312
    • Cheng, Y.1    Patel, D.J.2
  • 8
    • 33751090084 scopus 로고    scopus 로고
    • Chin, K.-H., C.-Y. Yang, C.-C. Chou, A. H.-J. Wang, and S.-H. Chou. 2006. The crystal structure of XC847 from Xanthomonas campestris:a 3′-5′ oligo- ribonuclease of DnaQ fold family with a novel opposingly shifted helix. Proteins Struct. Funct. Bioinform. 65:1036-1040.
    • Chin, K.-H., C.-Y. Yang, C.-C. Chou, A. H.-J. Wang, and S.-H. Chou. 2006. The crystal structure of XC847 from Xanthomonas campestris:a 3′-5′ oligo- ribonuclease of DnaQ fold family with a novel opposingly shifted helix. Proteins Struct. Funct. Bioinform. 65:1036-1040.
  • 10
    • 0029036047 scopus 로고
    • Deoxyribonuclease induction in apoptotic cytotoxic T lymphocytes
    • Deng, G., and E. R. Podack. 1995. Deoxyribonuclease induction in apoptotic cytotoxic T lymphocytes. FASEB J. 9:665-669.
    • (1995) FASEB J , vol.9 , pp. 665-669
    • Deng, G.1    Podack, E.R.2
  • 11
    • 0021169997 scopus 로고
    • Ribonuclease T: New exoribonuclease possibly involved in end-turnover of tRNA
    • Deutscher, M. P., C. W. Marlor, and R. Zaniewski. 1984. Ribonuclease T: new exoribonuclease possibly involved in end-turnover of tRNA. Proc. Natl. Acad. Sci. USA 81:4290-4293.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4290-4293
    • Deutscher, M.P.1    Marlor, C.W.2    Zaniewski, R.3
  • 12
    • 0141888419 scopus 로고    scopus 로고
    • A3′ exonuclease that specifically interacts with the 3′ end of histone mRNA
    • Dominski, Z., X. C. Yang, H. Kaygun, M. Dadlez, and W. F. Marzluff. 2003. A3′ exonuclease that specifically interacts with the 3′ end of histone mRNA. Mol. Cell 12:295-305.
    • (2003) Mol. Cell , vol.12 , pp. 295-305
    • Dominski, Z.1    Yang, X.C.2    Kaygun, H.3    Dadlez, M.4    Marzluff, W.F.5
  • 13
    • 0026334738 scopus 로고
    • Spontaneous mutation
    • Drake, J. W. 1991. Spontaneous mutation. Annu. Rev. Genet. 25:125-146.
    • (1991) Annu. Rev. Genet , vol.25 , pp. 125-146
    • Drake, J.W.1
  • 14
    • 31044452870 scopus 로고    scopus 로고
    • Duchaine, T. F., J. A. Wohlschlegel, S. Kennedy, Y. Bei, D. Conte, Jr., K. Pang, D. R. Brownell, S. Harding, S. Mitani, G. Ruvkun, J. R. Yates III, and C. C. Mello. 2006. Functional proteomics reveals the biochemical niche of Caenorhabditis elegans DCR-1 in multiple small- RNA- mediated pathways. Cell 124:343-354.
    • Duchaine, T. F., J. A. Wohlschlegel, S. Kennedy, Y. Bei, D. Conte, Jr., K. Pang, D. R. Brownell, S. Harding, S. Mitani, G. Ruvkun, J. R. Yates III, and C. C. Mello. 2006. Functional proteomics reveals the biochemical niche of Caenorhabditis elegans DCR-1 in multiple small- RNA- mediated pathways. Cell 124:343-354.
  • 15
    • 0031888955 scopus 로고    scopus 로고
    • A caspase- activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari, M., H. Sakahira, H. Yokoyama, K. Okawa, A. Iwamatsu, and S. Nagata. 1998. A caspase- activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 16
    • 0343938842 scopus 로고    scopus 로고
    • Changes in elemental content during apoptotic cell death studied by electron probe X-ray microanalysis
    • Fernandez- Segura, E., F. J. Canizares, M. A. Cubero, A. Warley, and A. Campos. 1999. Changes in elemental content during apoptotic cell death studied by electron probe X-ray microanalysis. Exp. Cell Res. 253:454-462.
    • (1999) Exp. Cell Res , vol.253 , pp. 454-462
    • Fernandez- Segura, E.1    Canizares, F.J.2    Cubero, M.A.3    Warley, A.4    Campos, A.5
  • 18
    • 0036229246 scopus 로고    scopus 로고
    • Structural basis for proofreading during replication of the Escherichia coli chromosome
    • Hamdan, S., P. D. Carr, S. E. Brown, D. L. Ollis, and N. E. Dixon. 2002. Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure 10:535-546.
    • (2002) Structure , vol.10 , pp. 535-546
    • Hamdan, S.1    Carr, P.D.2    Brown, S.E.3    Ollis, D.L.4    Dixon, N.E.5
  • 19
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • Harrington, J. J., and M. R. Lieber. 1994. The characterization of a mammalian DNA structure-specific endonuclease. EMBO J. 13:1235-1246.
    • (1994) EMBO J , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 20
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L., and C. Sander. 1996. Mapping the protein universe. Science 273:595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 21
    • 0027980787 scopus 로고
    • The dpy-30 gene encodes an essential component of the Caenorhabditis elegans dosage compensation machinery
    • Hsu, D. R., and B. J. Meyer. 1994. The dpy-30 gene encodes an essential component of the Caenorhabditis elegans dosage compensation machinery. Genetics 137:999-1018.
    • (1994) Genetics , vol.137 , pp. 999-1018
    • Hsu, D.R.1    Meyer, B.J.2
  • 22
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M. D., M. Weil, and M. C. Raff. 1997. Programmed cell death in animal development. Cell 88:347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 23
    • 1342346710 scopus 로고    scopus 로고
    • A conserved siRNA-degrading RNase negatively regulates RNA interference in Caenorhabditis elegans
    • Kennedy, S., D. Wang, and G. Ruvkun. 2004. A conserved siRNA-degrading RNase negatively regulates RNA interference in Caenorhabditis elegans. Nature 427:645-649.
    • (2004) Nature , vol.427 , pp. 645-649
    • Kennedy, S.1    Wang, D.2    Ruvkun, G.3
  • 25
  • 26
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L. Y., X. Luo, and X. Wang. 2001. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 27
    • 0029151159 scopus 로고
    • The tRNA processing enzyme RNase T is essential for maturation of 5S RNA
    • Li, Z., and M. P. Deutscher. 1995. The tRNA processing enzyme RNase T is essential for maturation of 5S RNA. Proc. Natl. Acad. Sci. USA 92:6883-6886.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6883-6886
    • Li, Z.1    Deutscher, M.P.2
  • 28
    • 0032951885 scopus 로고    scopus 로고
    • Maturation of 23S rRNA requires the exoribonuclease RNase T
    • Li, Z., S. Pandit, and M. P. Deutscher. 1999. Maturation of 23S rRNA requires the exoribonuclease RNase T. RNA 5:139-146.
    • (1999) RNA , vol.5 , pp. 139-146
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 29
    • 0030021182 scopus 로고    scopus 로고
    • Escherichia coli RNase T functions in vivo as a dimer dependent on cysteine 168
    • Li, Z., L. Zhan, and M. P. Deutscher. 1996. Escherichia coli RNase T functions in vivo as a dimer dependent on cysteine 168. J. Biol. Chem. 271:1133-1137.
    • (1996) J. Biol. Chem , vol.271 , pp. 1133-1137
    • Li, Z.1    Zhan, L.2    Deutscher, M.P.3
  • 30
    • 0031104841 scopus 로고    scopus 로고
    • The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair
    • Lieber, M. R. 1997. The FEN-1 family of structure-specific nucleases in eukaryotic DNA replication, recombination and repair. Bioessays 19:233-240.
    • (1997) Bioessays , vol.19 , pp. 233-240
    • Lieber, M.R.1
  • 31
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu, X., H. Zou, C. Slaoghter, and X. Wang. 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaoghter, C.3    Wang, X.4
  • 32
    • 0035907239 scopus 로고    scopus 로고
    • Excision of 3′ termini by the Trex1 and TREX2 3′ → 5′ exonucleases. Characterization of the recombinant proteins
    • Mazur, D. J., and F. W. Perrino. 2001. Excision of 3′ termini by the Trex1 and TREX2 3′ → 5′ exonucleases. Characterization of the recombinant proteins. J. Biol. Chem. 276:17022-17029.
    • (2001) J. Biol. Chem , vol.276 , pp. 17022-17029
    • Mazur, D.J.1    Perrino, F.W.2
  • 33
    • 0025942107 scopus 로고
    • Efficient gene transfer in Caenorhabditis elegans: Extrachromosomal maintenance and integration of transforming sequences
    • Mello, C. C., J. M. Krame, D. Stinchcomb, and V. Ambros. 1991. Efficient gene transfer in Caenorhabditis elegans: extrachromosomal maintenance and integration of transforming sequences. EMBO J. 10:3959-3970.
    • (1991) EMBO J , vol.10 , pp. 3959-3970
    • Mello, C.C.1    Krame, J.M.2    Stinchcomb, D.3    Ambros, V.4
  • 35
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. 1997. Apoptosis by death factor. Cell 88:355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0035811511 scopus 로고    scopus 로고
    • Mito- chondrial endonuclease G is important for apoptosis in Caenorhabditis elegans
    • Parrish, J., L. Li, K. Klotz, D. Ledwich, X. Wang, and D. Xue. 2001. Mito- chondrial endonuclease G is important for apoptosis in Caenorhabditis elegans. Nature 412:90-94.
    • (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
  • 38
    • 33644999160 scopus 로고    scopus 로고
    • Cuts can kill: The roles of apoptotic nucleases in cell death and animal development
    • Parrish, J. Z., and D. Xue. 2006. Cuts can kill: the roles of apoptotic nucleases in cell death and animal development. Chromosoma 115:89-97.
    • (2006) Chromosoma , vol.115 , pp. 89-97
    • Parrish, J.Z.1    Xue, D.2
  • 39
    • 0038369994 scopus 로고    scopus 로고
    • Functional genomic analysis of apoptotic DNA degradation in Caenorhabditis elegans
    • Parrish, J. Z., and D. Xue. 2003. Functional genomic analysis of apoptotic DNA degradation in Caenorhabditis elegans. Mol. Cell 11:987-996.
    • (2003) Mol. Cell , vol.11 , pp. 987-996
    • Parrish, J.Z.1    Xue, D.2
  • 40
    • 17644407757 scopus 로고    scopus 로고
    • The human TREX2 3′ → 5′-exonuclease structure suggests a mechanism for efficient non- processive DNA catalysis
    • Perrino, F. W., S. Harvey, S. McMillin, and T. Hollis. 2005. The human TREX2 3′ → 5′-exonuclease structure suggests a mechanism for efficient non- processive DNA catalysis. J. Biol. Chem. 280:15212- 15218.
    • (2005) J. Biol. Chem , vol.280 , pp. 15212-15218
    • Perrino, F.W.1    Harvey, S.2    McMillin, S.3    Hollis, T.4
  • 42
    • 0030880598 scopus 로고    scopus 로고
    • Sheldrick, G., and T. 1997. Schneider. SHELXL: high-resolution refinement Methods Enzymol. 277:319-343.
    • Sheldrick, G., and T. 1997. Schneider. SHELXL: high-resolution refinement Methods Enzymol. 277:319-343.
  • 43
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz, T. A., and J. A. Steitz. 1993. A general two-metal-ion mechanism for catalytic RNA. Proc. Natl. Acad. Sci. USA 90:6498-6502.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 44
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF- mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang, X., C. Yang, J. Chai, Y. Shi, and D. Xue. 2002. Mechanisms of AIF- mediated apoptotic DNA degradation in Caenorhabditis elegans. Science 298:1587-1592.
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 45
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., M. N. Isupov, and G. N. Murshudov. 2001. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Cryst. D 57:122-133.
    • (2001) Acta Cryst. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 46
    • 28644436520 scopus 로고    scopus 로고
    • Structural insight into poly(A) binding and catalytic mechanism of human PARN
    • Wu, M., M. Reuter, H. Lilie, Y. Liu, E. Wahle, and H. Song. 2005. Structural insight into poly(A) binding and catalytic mechanism of human PARN. EMBO J. 24:4082-4093.
    • (2005) EMBO J , vol.24 , pp. 4082-4093
    • Wu, M.1    Reuter, M.2    Lilie, H.3    Liu, Y.4    Wahle, E.5    Song, H.6
  • 47
    • 0034162713 scopus 로고    scopus 로고
    • NUC-1, a Caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis
    • Wu, Y. C., G. M. Stanfield, and H. R. Horvitz. 2000. NUC-1, a Caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis. Genes Dev. 14:536-548.
    • (2000) Genes Dev , vol.14 , pp. 536-548
    • Wu, Y.C.1    Stanfield, G.M.2    Horvitz, H.R.3
  • 48
    • 33750044572 scopus 로고    scopus 로고
    • Characterization of 3′hExo, a 3′ exonuclease specifically interacting with the 3′ end of histone mRNA
    • Yang, X. C., M. Purdy, W. F. Marzluff, and Z. Dominski. 2006. Characterization of 3′hExo, a 3′ exonuclease specifically interacting with the 3′ end of histone mRNA. J. Biol. Chem. 281:30447-30454.
    • (2006) J. Biol. Chem , vol.281 , pp. 30447-30454
    • Yang, X.C.1    Purdy, M.2    Marzluff, W.F.3    Dominski, Z.4
  • 50
    • 0037147310 scopus 로고    scopus 로고
    • Mechanism of action of RNase T. II. A structural and functional model of the enzyme
    • Zuo, Y., and M. P. Deutscher. 2002. Mechanism of action of RNase T. II. A structural and functional model of the enzyme. J. Biol. Chem. 277:50160-50164.
    • (2002) J. Biol. Chem , vol.277 , pp. 50160-50164
    • Zuo, Y.1    Deutscher, M.P.2


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