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Volumn 1829, Issue 8, 2013, Pages 842-853

Yeast and human mitochondrial helicases

Author keywords

IRC3; Mitochondrial degradosome; MSS116; RNA degradation; Suv3 helicase (SUPV3L1 hSuv3p, hSuv3, Suv3p); Twinkle

Indexed keywords

C10ORF2 PROTEIN; DEAD BOX PROTEIN; HELICASE; IRC3P PROTEIN; MDDX28 PROTEIN; MESSENGER RNA; MITOCHONDRIAL RNA; MRH4P PROTEIN; MSS16P PROTEIN; PIF1 PROTEIN; RIBOSOME RNA; RNA HELICASE; SUPV3L1 PROTEIN; SUV3P PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; UNTRANSLATED RNA;

EID: 84877924367     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2013.02.009     Document Type: Review
Times cited : (27)

References (133)
  • 1
    • 77953799862 scopus 로고    scopus 로고
    • Maintenance and expression of the S. cerevisiae mitochondrial genome-from genetics to evolution and systems biology
    • Lipinski K.A., Kaniak-Golik A., Golik P. Maintenance and expression of the S. cerevisiae mitochondrial genome-from genetics to evolution and systems biology. Biochim. Biophys. Acta 2010, 1797:1086-1098.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1086-1098
    • Lipinski, K.A.1    Kaniak-Golik, A.2    Golik, P.3
  • 2
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: the driving forces behind RNA metabolism
    • Rocak S., Linder P. DEAD-box proteins: the driving forces behind RNA metabolism. Nat. Rev. Mol. Cell Biol. 2004, 5:232-241.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 3
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: from generic motors to specific dissociation functions
    • Tanner N.K., Linder P. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell 2001, 8:251-262.
    • (2001) Mol. Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 5
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: a family affair-active and passive players in RNP-remodeling
    • Linder P. Dead-box proteins: a family affair-active and passive players in RNP-remodeling. Nucleic Acids Res. 2006, 34:4168-4180.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4168-4180
    • Linder, P.1
  • 7
    • 0024961642 scopus 로고
    • Mitochondrial splicing requires a protein from a novel helicase family
    • Seraphin B., Simon M., Boulet A., Faye G. Mitochondrial splicing requires a protein from a novel helicase family. Nature 1989, 337:84-87.
    • (1989) Nature , vol.337 , pp. 84-87
    • Seraphin, B.1    Simon, M.2    Boulet, A.3    Faye, G.4
  • 9
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang H.R., Rowe C.E., Mohr S., Jiang Y., Lambowitz A.M., Perlman P.S. The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:163-168.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 163-168
    • Huang, H.R.1    Rowe, C.E.2    Mohr, S.3    Jiang, Y.4    Lambowitz, A.M.5    Perlman, P.S.6
  • 11
    • 84875171510 scopus 로고    scopus 로고
    • Toward a molecular understanding of RNA remodeling by DEAD-box proteins
    • Russell R., Jarmoskaite I., Lambowitz A.M. Toward a molecular understanding of RNA remodeling by DEAD-box proteins. RNA Biol. 2012, 10.
    • (2012) RNA Biol. , vol.10
    • Russell, R.1    Jarmoskaite, I.2    Lambowitz, A.M.3
  • 12
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls C., Mohr S., Del Campo M., Yang Q., Jankowsky E., Lambowitz A.M. Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J. Mol. Biol. 2007, 365:835-855.
    • (2007) J. Mol. Biol. , vol.365 , pp. 835-855
    • Halls, C.1    Mohr, S.2    Del Campo, M.3    Yang, Q.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 13
    • 33847652952 scopus 로고    scopus 로고
    • A DEAD protein that activates intron self-splicing without unwinding RNA
    • Solem A., Zingler N., Pyle A.M. A DEAD protein that activates intron self-splicing without unwinding RNA. Mol. Cell 2006, 24:611-617.
    • (2006) Mol. Cell , vol.24 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.3
  • 14
    • 52949136970 scopus 로고    scopus 로고
    • A DExH/D-box protein coordinates the two steps of splicing in a group I intron
    • Bifano A.L., Caprara M.G. A DExH/D-box protein coordinates the two steps of splicing in a group I intron. J. Mol. Biol. 2008, 383:667-682.
    • (2008) J. Mol. Biol. , vol.383 , pp. 667-682
    • Bifano, A.L.1    Caprara, M.G.2
  • 15
    • 33846637337 scopus 로고    scopus 로고
    • Group II intron folding under near-physiological conditions: collapsing to the near-native state
    • Fedorova O., Waldsich C., Pyle A.M. Group II intron folding under near-physiological conditions: collapsing to the near-native state. J. Mol. Biol. 2007, 366:1099-1114.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1099-1114
    • Fedorova, O.1    Waldsich, C.2    Pyle, A.M.3
  • 16
    • 78751664168 scopus 로고    scopus 로고
    • DEAD-box protein facilitated RNA folding in vivo
    • Liebeg A., Mayer O., Waldsich C. DEAD-box protein facilitated RNA folding in vivo. RNA Biol. 2010, 7:803-811.
    • (2010) RNA Biol. , vol.7 , pp. 803-811
    • Liebeg, A.1    Mayer, O.2    Waldsich, C.3
  • 18
    • 67349117103 scopus 로고    scopus 로고
    • Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones
    • Del Campo M., Mohr S., Jiang Y., Jia H., Jankowsky E., Lambowitz A.M. Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones. J. Mol. Biol. 2009, 389:674-693.
    • (2009) J. Mol. Biol. , vol.389 , pp. 674-693
    • Del Campo, M.1    Mohr, S.2    Jiang, Y.3    Jia, H.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 20
    • 79960910841 scopus 로고    scopus 로고
    • ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo
    • Potratz J.P., Del Campo M., Wolf R.Z., Lambowitz A.M., Russell R. ATP-dependent roles of the DEAD-box protein Mss116p in group II intron splicing in vitro and in vivo. J. Mol. Biol. 2011, 411:661-679.
    • (2011) J. Mol. Biol. , vol.411 , pp. 661-679
    • Potratz, J.P.1    Del Campo, M.2    Wolf, R.Z.3    Lambowitz, A.M.4    Russell, R.5
  • 21
    • 35348941874 scopus 로고    scopus 로고
    • DEAD-box proteins unwind duplexes by local strand separation
    • Yang Q., Del Campo M., Lambowitz A.M., Jankowsky E. DEAD-box proteins unwind duplexes by local strand separation. Mol. Cell 2007, 28:253-263.
    • (2007) Mol. Cell , vol.28 , pp. 253-263
    • Yang, Q.1    Del Campo, M.2    Lambowitz, A.M.3    Jankowsky, E.4
  • 22
    • 84865093422 scopus 로고    scopus 로고
    • The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate
    • Fedorova O., Pyle A.M. The brace for a growing scaffold: Mss116 protein promotes RNA folding by stabilizing an early assembly intermediate. J. Mol. Biol. 2012, 422:347-365.
    • (2012) J. Mol. Biol. , vol.422 , pp. 347-365
    • Fedorova, O.1    Pyle, A.M.2
  • 23
    • 77649337588 scopus 로고    scopus 로고
    • Protein-facilitated folding of group II intron ribozymes
    • Fedorova O., Solem A., Pyle A.M. Protein-facilitated folding of group II intron ribozymes. J. Mol. Biol. 2010, 397:799-813.
    • (2010) J. Mol. Biol. , vol.397 , pp. 799-813
    • Fedorova, O.1    Solem, A.2    Pyle, A.M.3
  • 24
    • 78049234242 scopus 로고    scopus 로고
    • Single-molecule analysis of Mss116-mediated group II intron folding
    • Karunatilaka K.S., Solem A., Pyle A.M., Rueda D. Single-molecule analysis of Mss116-mediated group II intron folding. Nature 2010, 467:935-939.
    • (2010) Nature , vol.467 , pp. 935-939
    • Karunatilaka, K.S.1    Solem, A.2    Pyle, A.M.3    Rueda, D.4
  • 26
    • 78049293801 scopus 로고    scopus 로고
    • Dual roles for the Mss116 cofactor during splicing of the ai5gamma group II intron
    • Zingler N., Solem A., Pyle A.M. Dual roles for the Mss116 cofactor during splicing of the ai5gamma group II intron. Nucleic Acids Res. 2010, 38:6602-6609.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6602-6609
    • Zingler, N.1    Solem, A.2    Pyle, A.M.3
  • 27
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F., Putnam A., Jankowsky E. ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:20209-20214.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 28
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the yeast DEAD box protein Mss116p reveals two wedges that crimp RNA
    • Del Campo M., Lambowitz A.M. Structure of the yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol. Cell 2009, 35:598-609.
    • (2009) Mol. Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 29
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • Mohr G., Del Campo M., Mohr S., Yang Q., Jia H., Jankowsky E., Lambowitz A.M. Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro. J. Mol. Biol. 2008, 375:1344-1364.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1344-1364
    • Mohr, G.1    Del Campo, M.2    Mohr, S.3    Yang, Q.4    Jia, H.5    Jankowsky, E.6    Lambowitz, A.M.7
  • 30
    • 0036053425 scopus 로고    scopus 로고
    • A novel mitochondrial DEAD box protein (Mrh4) required for maintenance of mtDNA in Saccharomyces cerevisiae
    • Schmidt U., Lehmann K., Stahl U. A novel mitochondrial DEAD box protein (Mrh4) required for maintenance of mtDNA in Saccharomyces cerevisiae. FEMS Yeast Res. 2002, 2:267-276.
    • (2002) FEMS Yeast Res. , vol.2 , pp. 267-276
    • Schmidt, U.1    Lehmann, K.2    Stahl, U.3
  • 31
    • 0034122608 scopus 로고    scopus 로고
    • Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast
    • Contamine V., Picard M. Maintenance and integrity of the mitochondrial genome: a plethora of nuclear genes in the budding yeast. Microbiol. Mol. Biol. Rev. 2000, 64:281-315.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 281-315
    • Contamine, V.1    Picard, M.2
  • 32
    • 0025281416 scopus 로고
    • The nuclear SUV3-1 mutation affects a variety of post-transcriptional processes in yeast mitochondria
    • Conrad-Webb H., Perlman P.S., Zhu H., Butow R.A. The nuclear SUV3-1 mutation affects a variety of post-transcriptional processes in yeast mitochondria. Nucleic Acids Res. 1990, 18:1369-1376.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1369-1376
    • Conrad-Webb, H.1    Perlman, P.S.2    Zhu, H.3    Butow, R.A.4
  • 33
    • 0026736197 scopus 로고
    • The yeast nuclear gene suv3 affecting mitochondrial post-transcriptional processes encodes a putative ATP-dependent RNA helicase
    • Stepien P.P., Margossian S.P., Landsman D., Butow R.A. The yeast nuclear gene suv3 affecting mitochondrial post-transcriptional processes encodes a putative ATP-dependent RNA helicase. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:6813-6817.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6813-6817
    • Stepien, P.P.1    Margossian, S.P.2    Landsman, D.3    Butow, R.A.4
  • 34
    • 0024505742 scopus 로고
    • Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene
    • Zhu H., Conrad-Webb H., Liao X.S., Perlman P.S., Butow R.A. Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene. Mol. Cell. Biol. 1989, 9:1507-1512.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1507-1512
    • Zhu, H.1    Conrad-Webb, H.2    Liao, X.S.3    Perlman, P.S.4    Butow, R.A.5
  • 35
    • 0037449772 scopus 로고    scopus 로고
    • The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism
    • Dziembowski A., Piwowarski J., Hoser R., Minczuk M., Dmochowska A., Siep M., van der Spek H., Grivell L.A., Stepien P.P. The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism. J. Biol. Chem. 2003, 278:1603-1611.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1603-1611
    • Dziembowski, A.1    Piwowarski, J.2    Hoser, R.3    Minczuk, M.4    Dmochowska, A.5    Siep, M.6    van der Spek, H.7    Grivell, L.A.8    Stepien, P.P.9
  • 36
    • 33644851218 scopus 로고    scopus 로고
    • Balance between transcription and RNA degradation is vital for Saccharomyces cerevisiae mitochondria: reduced transcription rescues the phenotype of deficient RNA degradation
    • Rogowska A.T., Puchta O., Czarnecka A.M., Kaniak A., Stepien P.P., Golik P. Balance between transcription and RNA degradation is vital for Saccharomyces cerevisiae mitochondria: reduced transcription rescues the phenotype of deficient RNA degradation. Mol. Biol. Cell 2006, 17:1184-1193.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1184-1193
    • Rogowska, A.T.1    Puchta, O.2    Czarnecka, A.M.3    Kaniak, A.4    Stepien, P.P.5    Golik, P.6
  • 38
    • 0031725399 scopus 로고    scopus 로고
    • The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA
    • Dziembowski A., Malewicz M., Minczuk M., Golik P., Dmochowska A., Stepien P.P. The yeast nuclear gene DSS1, which codes for a putative RNase II, is necessary for the function of the mitochondrial degradosome in processing and turnover of RNA. Mol. Gen. Genet. 1998, 260:108-114.
    • (1998) Mol. Gen. Genet. , vol.260 , pp. 108-114
    • Dziembowski, A.1    Malewicz, M.2    Minczuk, M.3    Golik, P.4    Dmochowska, A.5    Stepien, P.P.6
  • 39
    • 0030034498 scopus 로고    scopus 로고
    • The DExH box protein Suv3p is a component of a yeast mitochondrial 3'-to-5' exoribonuclease that suppresses group I intron toxicity
    • Margossian S.P., Li H., Zassenhaus H.P., Butow R.A. The DExH box protein Suv3p is a component of a yeast mitochondrial 3'-to-5' exoribonuclease that suppresses group I intron toxicity. Cell 1996, 84:199-209.
    • (1996) Cell , vol.84 , pp. 199-209
    • Margossian, S.P.1    Li, H.2    Zassenhaus, H.P.3    Butow, R.A.4
  • 40
    • 0027512243 scopus 로고
    • Isolation and characterization of an NTP-dependent 3'-exoribonuclease from mitochondria of Saccharomyces cerevisiae
    • Min J., Heuertz R.M., Zassenhaus H.P. Isolation and characterization of an NTP-dependent 3'-exoribonuclease from mitochondria of Saccharomyces cerevisiae. J. Biol. Chem. 1993, 268:7350-7357.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7350-7357
    • Min, J.1    Heuertz, R.M.2    Zassenhaus, H.P.3
  • 41
    • 0028963261 scopus 로고
    • The suv3 nuclear gene product is required for the in vivo processing of the yeast mitochondrial 21s rRNA transcripts containing the r1 intron
    • Stepien P.P., Kokot L., Leski T., Bartnik E. The suv3 nuclear gene product is required for the in vivo processing of the yeast mitochondrial 21s rRNA transcripts containing the r1 intron. Curr. Genet. 1995, 27:234-238.
    • (1995) Curr. Genet. , vol.27 , pp. 234-238
    • Stepien, P.P.1    Kokot, L.2    Leski, T.3    Bartnik, E.4
  • 42
    • 0029112165 scopus 로고
    • The S. cerevisiae nuclear gene SUV3 encoding a putative RNA helicase is necessary for the stability of mitochondrial transcripts containing multiple introns
    • Golik P., Szczepanek T., Bartnik E., Stepien P.P., Lazowska J. The S. cerevisiae nuclear gene SUV3 encoding a putative RNA helicase is necessary for the stability of mitochondrial transcripts containing multiple introns. Curr. Genet. 1995, 28:217-224.
    • (1995) Curr. Genet. , vol.28 , pp. 217-224
    • Golik, P.1    Szczepanek, T.2    Bartnik, E.3    Stepien, P.P.4    Lazowska, J.5
  • 43
    • 0029089849 scopus 로고
    • The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for mitochondrial biogenesis
    • Dmochowska A., Golik P., Stepien P.P. The novel nuclear gene DSS-1 of Saccharomyces cerevisiae is necessary for mitochondrial biogenesis. Curr. Genet. 1995, 28:108-112.
    • (1995) Curr. Genet. , vol.28 , pp. 108-112
    • Dmochowska, A.1    Golik, P.2    Stepien, P.P.3
  • 44
    • 77950569293 scopus 로고    scopus 로고
    • RNP
    • Turk E.M., Caprara M.G. Splicing of yeast aI5 group I intron requires SUV3 to recycle MRS1 via mitochondrial degradosome-promoted decay of excised intron ribonucleoprotein. J. Biol. Chem. 2010, 285:8585-8594.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8585-8594
    • Turk, E.M.1    Caprara, M.G.2
  • 45
    • 58249089329 scopus 로고    scopus 로고
    • In vivo and in vitro approaches for studying the yeast mitochondrial RNA degradosome complex
    • Malecki M., Jedrzejczak R., Puchta O., Stepien P.P., Golik P. In vivo and in vitro approaches for studying the yeast mitochondrial RNA degradosome complex. Methods Enzymol. 2008, 447:463-488.
    • (2008) Methods Enzymol. , vol.447 , pp. 463-488
    • Malecki, M.1    Jedrzejczak, R.2    Puchta, O.3    Stepien, P.P.4    Golik, P.5
  • 46
    • 34547683820 scopus 로고    scopus 로고
    • In vitro reconstitution and characterization of the yeast mitochondrial degradosome complex unravels tight functional interdependence
    • Malecki M., Jedrzejczak R., Stepien P.P., Golik P. In vitro reconstitution and characterization of the yeast mitochondrial degradosome complex unravels tight functional interdependence. J. Mol. Biol. 2007, 372:23-36.
    • (2007) J. Mol. Biol. , vol.372 , pp. 23-36
    • Malecki, M.1    Jedrzejczak, R.2    Stepien, P.P.3    Golik, P.4
  • 47
    • 77952980570 scopus 로고    scopus 로고
    • Assays of the helicase, ATPase, and exoribonuclease activities of the yeast mitochondrial degradosome
    • Malecki M., Stepien P.P., Golik P. Assays of the helicase, ATPase, and exoribonuclease activities of the yeast mitochondrial degradosome. Methods Mol. Biol. 2010, 587:339-358.
    • (2010) Methods Mol. Biol. , vol.587 , pp. 339-358
    • Malecki, M.1    Stepien, P.P.2    Golik, P.3
  • 48
    • 80055074798 scopus 로고    scopus 로고
    • Uncoupling the roles of the SUV3 helicase in maintenance of mitochondrial genome stability and RNA degradation
    • Guo X.E., Chen C.F., Wang D.D., Modrek A.S., Phan V.H., Lee W.H., Chen P.L. Uncoupling the roles of the SUV3 helicase in maintenance of mitochondrial genome stability and RNA degradation. J. Biol. Chem. 2011, 286:38783-38794.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38783-38794
    • Guo, X.E.1    Chen, C.F.2    Wang, D.D.3    Modrek, A.S.4    Phan, V.H.5    Lee, W.H.6    Chen, P.L.7
  • 49
    • 0036849206 scopus 로고    scopus 로고
    • Overexpressed yeast mitochondrial putative RNA helicase Mss116 partially restores proper mtRNA metabolism in strains lacking the Suv3 mtRNA helicase
    • Minczuk M., Dmochowska A., Palczewska M., Stepien P.P. Overexpressed yeast mitochondrial putative RNA helicase Mss116 partially restores proper mtRNA metabolism in strains lacking the Suv3 mtRNA helicase. Yeast 2002, 19:1285-1293.
    • (2002) Yeast , vol.19 , pp. 1285-1293
    • Minczuk, M.1    Dmochowska, A.2    Palczewska, M.3    Stepien, P.P.4
  • 50
    • 0033133863 scopus 로고    scopus 로고
    • Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families
    • de la Cruz J., Kressler D., Linder P. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem. Sci. 1999, 24:192-198.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 192-198
    • de la Cruz, J.1    Kressler, D.2    Linder, P.3
  • 51
    • 37748999305 scopus 로고    scopus 로고
    • Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination
    • Alvaro D., Lisby M., Rothstein R. Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination. PLoS Genet. 2007, 3:e228.
    • (2007) PLoS Genet. , vol.3
    • Alvaro, D.1    Lisby, M.2    Rothstein, R.3
  • 53
    • 76249088524 scopus 로고    scopus 로고
    • Genome-wide deletion mutant analysis reveals genes required for respiratory growth, mitochondrial genome maintenance and mitochondrial protein synthesis in Saccharomyces cerevisiae
    • Merz S., Westermann B. Genome-wide deletion mutant analysis reveals genes required for respiratory growth, mitochondrial genome maintenance and mitochondrial protein synthesis in Saccharomyces cerevisiae. Genome Biol. 2009, 10:R95.
    • (2009) Genome Biol. , vol.10
    • Merz, S.1    Westermann, B.2
  • 54
    • 0014415120 scopus 로고
    • Ethidium bromide induced mutation of yeast mitochondria: complete transformation of cells into respiratory deficient non-chromosomal "petites"
    • Slonimski P.P., Perrodin G., Croft J.H. Ethidium bromide induced mutation of yeast mitochondria: complete transformation of cells into respiratory deficient non-chromosomal "petites". Biochem. Biophys. Res. Commun. 1968, 30:232-239.
    • (1968) Biochem. Biophys. Res. Commun. , vol.30 , pp. 232-239
    • Slonimski, P.P.1    Perrodin, G.2    Croft, J.H.3
  • 55
    • 0022110054 scopus 로고
    • Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae
    • Myers A.M., Pape L.K., Tzagoloff A. Mitochondrial protein synthesis is required for maintenance of intact mitochondrial genomes in Saccharomyces cerevisiae. EMBO J. 1985, 4:2087-2092.
    • (1985) EMBO J. , vol.4 , pp. 2087-2092
    • Myers, A.M.1    Pape, L.K.2    Tzagoloff, A.3
  • 56
    • 33745188484 scopus 로고    scopus 로고
    • A "petite obligate" mutant of Saccharomyces cerevisiae: functional mtDNA is lethal in cells lacking the delta subunit of mitochondrial F1-ATPase
    • Duvezin-Caubet S., Rak M., Lefebvre-Legendre L., Tetaud E., Bonnefoy N., di Rago J.P. A "petite obligate" mutant of Saccharomyces cerevisiae: functional mtDNA is lethal in cells lacking the delta subunit of mitochondrial F1-ATPase. J. Biol. Chem. 2006, 281:16305-16313.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16305-16313
    • Duvezin-Caubet, S.1    Rak, M.2    Lefebvre-Legendre, L.3    Tetaud, E.4    Bonnefoy, N.5    di Rago, J.P.6
  • 57
    • 0034530444 scopus 로고    scopus 로고
    • Partial assembly of the yeast mitochondrial ATP synthase
    • Mueller D.M. Partial assembly of the yeast mitochondrial ATP synthase. J. Bioenerg. Biomembr. 2000, 32:391-400.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 391-400
    • Mueller, D.M.1
  • 58
    • 77955865813 scopus 로고    scopus 로고
    • DMR1 (CCM1/YGR150C) of Saccharomyces cerevisiae encodes an RNA-binding protein from the pentatricopeptide repeat family required for the maintenance of the mitochondrial 15S ribosomal RNA
    • Puchta O., Lubas M., Lipinski K.A., Piatkowski J., Malecki M., Golik P. DMR1 (CCM1/YGR150C) of Saccharomyces cerevisiae encodes an RNA-binding protein from the pentatricopeptide repeat family required for the maintenance of the mitochondrial 15S ribosomal RNA. Genetics 2010, 184:959-973.
    • (2010) Genetics , vol.184 , pp. 959-973
    • Puchta, O.1    Lubas, M.2    Lipinski, K.A.3    Piatkowski, J.4    Malecki, M.5    Golik, P.6
  • 59
    • 0032233832 scopus 로고    scopus 로고
    • Yeast nuclear PET127 gene can suppress deletions of the SUV3 or DSS1 genes: an indication of a functional interaction between 3' and 5' ends of mitochondrial mRNAs
    • Wegierski T., Dmochowska A., Jablonowska A., Dziembowski A., Bartnik E., Stepien P.P. Yeast nuclear PET127 gene can suppress deletions of the SUV3 or DSS1 genes: an indication of a functional interaction between 3' and 5' ends of mitochondrial mRNAs. Acta Biochim. Pol. 1998, 45:935-940.
    • (1998) Acta Biochim. Pol. , vol.45 , pp. 935-940
    • Wegierski, T.1    Dmochowska, A.2    Jablonowska, A.3    Dziembowski, A.4    Bartnik, E.5    Stepien, P.P.6
  • 60
    • 0034603852 scopus 로고    scopus 로고
    • New features of mitochondrial DNA replication system in yeast and man
    • Lecrenier N., Foury F. New features of mitochondrial DNA replication system in yeast and man. Gene 2000, 246:37-48.
    • (2000) Gene , vol.246 , pp. 37-48
    • Lecrenier, N.1    Foury, F.2
  • 61
    • 0033529190 scopus 로고    scopus 로고
    • Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase
    • Wang Y., Shadel G.S. Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:8046-8051.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8046-8051
    • Wang, Y.1    Shadel, G.S.2
  • 62
    • 0025192467 scopus 로고
    • RPO41-independent maintenance of [rho-] mitochondrial DNA in Saccharomyces cerevisiae
    • Fangman W.L., Henly J.W., Brewer B.J. RPO41-independent maintenance of [rho-] mitochondrial DNA in Saccharomyces cerevisiae. Mol. Cell. Biol. 1990, 10:10-15.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 10-15
    • Fangman, W.L.1    Henly, J.W.2    Brewer, B.J.3
  • 63
    • 0029147736 scopus 로고
    • A test of the transcription model for biased inheritance of yeast mitochondrial DNA
    • Lorimer H.E., Brewer B.J., Fangman W.L. A test of the transcription model for biased inheritance of yeast mitochondrial DNA. Mol. Cell. Biol. 1995, 15:4803-4809.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4803-4809
    • Lorimer, H.E.1    Brewer, B.J.2    Fangman, W.L.3
  • 67
    • 21244454028 scopus 로고    scopus 로고
    • Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
    • Nagaike T., Suzuki T., Katoh T., Ueda T. Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J. Biol. Chem. 2005, 280:19721-19727.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19721-19727
    • Nagaike, T.1    Suzuki, T.2    Katoh, T.3    Ueda, T.4
  • 70
    • 80053219536 scopus 로고    scopus 로고
    • PDE12 removes mitochondrial RNA poly(A) tails and controls translation in human mitochondria
    • Rorbach J., Nicholls T.J., Minczuk M. PDE12 removes mitochondrial RNA poly(A) tails and controls translation in human mitochondria. Nucleic Acids Res. 2011, 39:7750-7763.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7750-7763
    • Rorbach, J.1    Nicholls, T.J.2    Minczuk, M.3
  • 73
    • 84864318790 scopus 로고    scopus 로고
    • Of P and Z: mitochondrial tRNA processing enzymes
    • Rossmanith W. Of P and Z: mitochondrial tRNA processing enzymes. Biochim. Biophys. Acta 2012, 1819:1017-1026.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 1017-1026
    • Rossmanith, W.1
  • 74
    • 84862227617 scopus 로고    scopus 로고
    • The post-transcriptional life of mammalian mitochondrial RNA
    • Rorbach J., Minczuk M. The post-transcriptional life of mammalian mitochondrial RNA. Biochem. J. 2012, 444:357-373.
    • (2012) Biochem. J. , vol.444 , pp. 357-373
    • Rorbach, J.1    Minczuk, M.2
  • 76
  • 78
    • 23044511811 scopus 로고    scopus 로고
    • The 5' region of the human hSUV3 gene encoding mitochondrial DNA and RNA helicase: promoter characterization and alternative pre-mRNA splicing
    • Minczuk M., Lilpop J., Boros J., Stepien P.P. The 5' region of the human hSUV3 gene encoding mitochondrial DNA and RNA helicase: promoter characterization and alternative pre-mRNA splicing. Biochim. Biophys. Acta 2005, 1729:81-87.
    • (2005) Biochim. Biophys. Acta , vol.1729 , pp. 81-87
    • Minczuk, M.1    Lilpop, J.2    Boros, J.3    Stepien, P.P.4
  • 79
    • 55249119103 scopus 로고    scopus 로고
    • Role of SUV3 helicase in maintaining mitochondrial homeostasis in human cells
    • Khidr L., Wu G., Davila A., Procaccio V., Wallace D., Lee W.H. Role of SUV3 helicase in maintaining mitochondrial homeostasis in human cells. J. Biol. Chem. 2008, 283:27064-27073.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27064-27073
    • Khidr, L.1    Wu, G.2    Davila, A.3    Procaccio, V.4    Wallace, D.5    Lee, W.H.6
  • 82
    • 81155154361 scopus 로고    scopus 로고
    • The human Suv3 helicase interacts with replication protein A and flap endonuclease 1 in the nucleus
    • Veno S.T., Kulikowicz T., Pestana C., Stepien P.P., Stevnsner T., Bohr V.A. The human Suv3 helicase interacts with replication protein A and flap endonuclease 1 in the nucleus. Biochem. J. 2011, 440:293-300.
    • (2011) Biochem. J. , vol.440 , pp. 293-300
    • Veno, S.T.1    Kulikowicz, T.2    Pestana, C.3    Stepien, P.P.4    Stevnsner, T.5    Bohr, V.A.6
  • 83
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • Bogenhagen D.F., Rousseau D., Burke S. The layered structure of human mitochondrial DNA nucleoids. J. Biol. Chem. 2008, 283:3665-3675.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 84
    • 33748746678 scopus 로고    scopus 로고
    • Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane
    • Wang Y., Bogenhagen D.F. Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane. J. Biol. Chem. 2006, 281:25791-25802.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25791-25802
    • Wang, Y.1    Bogenhagen, D.F.2
  • 87
    • 1942438570 scopus 로고    scopus 로고
    • Purified human SUV3p exhibits multiple-substrate unwinding activity upon conformational change
    • Shu Z., Vijayakumar S., Chen C.F., Chen P.L., Lee W.H. Purified human SUV3p exhibits multiple-substrate unwinding activity upon conformational change. Biochemistry 2004, 43:4781-4790.
    • (2004) Biochemistry , vol.43 , pp. 4781-4790
    • Shu, Z.1    Vijayakumar, S.2    Chen, C.F.3    Chen, P.L.4    Lee, W.H.5
  • 88
    • 84869822219 scopus 로고    scopus 로고
    • LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria
    • Chujo T., Ohira T., Sakaguchi Y., Goshima N., Nomura N., Nagao A., Suzuki T. LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria. Nucleic Acids Res. 2012, 40:8033-8047.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8033-8047
    • Chujo, T.1    Ohira, T.2    Sakaguchi, Y.3    Goshima, N.4    Nomura, N.5    Nagao, A.6    Suzuki, T.7
  • 90
    • 0015242887 scopus 로고
    • Expression of the mitochondrial genome in HeLa cells. II. Evidence for complete transcription of mitochondrial DNA
    • Aloni Y., Attardi G. Expression of the mitochondrial genome in HeLa cells. II. Evidence for complete transcription of mitochondrial DNA. J. Mol. Biol. 1971, 55:251-267.
    • (1971) J. Mol. Biol. , vol.55 , pp. 251-267
    • Aloni, Y.1    Attardi, G.2
  • 91
    • 38649115643 scopus 로고    scopus 로고
    • Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA
    • Slomovic S., Schuster G. Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA. RNA 2008, 14:310-323.
    • (2008) RNA , vol.14 , pp. 310-323
    • Slomovic, S.1    Schuster, G.2
  • 92
    • 0019444843 scopus 로고
    • TRNA punctuation model of RNA processing in human mitochondria
    • Ojala D., Montoya J., Attardi G. tRNA punctuation model of RNA processing in human mitochondria. Nature 1981, 290:470-474.
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 93
    • 68949108247 scopus 로고    scopus 로고
    • Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality
    • Wang D.D., Shu Z., Lieser S.A., Chen P.L., Lee W.H. Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality. J. Biol. Chem. 2009, 284:20812-20821.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20812-20821
    • Wang, D.D.1    Shu, Z.2    Lieser, S.A.3    Chen, P.L.4    Lee, W.H.5
  • 95
    • 84874956967 scopus 로고    scopus 로고
    • Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging
    • Rhee H.W., Zou P., Udeshi N.D., Martell J.D., Mootha V.K., Carr S.A., Ting A.Y. Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging. Science 2013, 10.1126/science.1230593.
    • (2013) Science
    • Rhee, H.W.1    Zou, P.2    Udeshi, N.D.3    Martell, J.D.4    Mootha, V.K.5    Carr, S.A.6    Ting, A.Y.7
  • 96
    • 26244453890 scopus 로고    scopus 로고
    • Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP
    • Minczuk M., Mroczek S., Pawlak S.D., Stepien P.P. Human ATP-dependent RNA/DNA helicase hSuv3p interacts with the cofactor of survivin HBXIP. FEBS J. 2005, 272:5008-5019.
    • (2005) FEBS J. , vol.272 , pp. 5008-5019
    • Minczuk, M.1    Mroczek, S.2    Pawlak, S.D.3    Stepien, P.P.4
  • 99
    • 33748744378 scopus 로고    scopus 로고
    • Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability
    • Sharma S., Doherty K.M., Brosh R.M. Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability. Biochem. J. 2006, 398:319-337.
    • (2006) Biochem. J. , vol.398 , pp. 319-337
    • Sharma, S.1    Doherty, K.M.2    Brosh, R.M.3
  • 100
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • Chaganti R.S., Schonberg S., German J. A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes. Proc. Natl. Acad. Sci. U. S. A. 1974, 71:4508-4512.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 4508-4512
    • Chaganti, R.S.1    Schonberg, S.2    German, J.3
  • 101
    • 81155154361 scopus 로고    scopus 로고
    • The human Suv3 helicase interacts with replication protein A and flap endonuclease 1 in the nucleus
    • Venoe S., Kulikowicz T., Pestana C., Stepien P., Stevnsner T., Bohr V. The human Suv3 helicase interacts with replication protein A and flap endonuclease 1 in the nucleus. Biochem. J. 2011, 440:293-300.
    • (2011) Biochem. J. , vol.440 , pp. 293-300
    • Venoe, S.1    Kulikowicz, T.2    Pestana, C.3    Stepien, P.4    Stevnsner, T.5    Bohr, V.6
  • 102
    • 84874679741 scopus 로고    scopus 로고
    • Mitochondrial genome instability resulting from SUV3 haploinsufficiency leads to tumorigenesis and shortened lifespan
    • Chen P.L., Chen C.F., Chen Y., Guo X.E., Huang C.K., Shew J.Y., Reddick R.L., Wallace D.C., Lee W.H. Mitochondrial genome instability resulting from SUV3 haploinsufficiency leads to tumorigenesis and shortened lifespan. Oncogene 2013, 32:1193-1201.
    • (2013) Oncogene , vol.32 , pp. 1193-1201
    • Chen, P.L.1    Chen, C.F.2    Chen, Y.3    Guo, X.E.4    Huang, C.K.5    Shew, J.Y.6    Reddick, R.L.7    Wallace, D.C.8    Lee, W.H.9
  • 107
    • 0035943626 scopus 로고    scopus 로고
    • Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization
    • Valgardsdottir R., Brede G., Eide L.G., Frengen E., Prydz H. Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization. J. Biol. Chem. 2001, 276:32056-32063.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32056-32063
    • Valgardsdottir, R.1    Brede, G.2    Eide, L.G.3    Frengen, E.4    Prydz, H.5
  • 108
    • 0038079978 scopus 로고    scopus 로고
    • Transport signals and transcription-dependent nuclear localization of the putative DEAD-box helicase MDDX28
    • Valgardsdottir R., Prydz H. Transport signals and transcription-dependent nuclear localization of the putative DEAD-box helicase MDDX28. J. Biol. Chem. 2003, 278:21146-21154.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21146-21154
    • Valgardsdottir, R.1    Prydz, H.2
  • 109
    • 4444341362 scopus 로고    scopus 로고
    • Regulated compartmentalization of the putative DEAD-box helicase MDDX28 within the mitochondria in COS-1 cells
    • Valgardsdottir R., Ottersen O.P., Prydz H. Regulated compartmentalization of the putative DEAD-box helicase MDDX28 within the mitochondria in COS-1 cells. Exp. Cell Res. 2004, 299:294-302.
    • (2004) Exp. Cell Res. , vol.299 , pp. 294-302
    • Valgardsdottir, R.1    Ottersen, O.P.2    Prydz, H.3
  • 110
    • 39149116732 scopus 로고    scopus 로고
    • The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities
    • Farge G., Holmlund T., Khvorostova J., Rofougaran R., Hofer A., Falkenberg M. The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities. Nucleic Acids Res. 2008, 36:393-403.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 393-403
    • Farge, G.1    Holmlund, T.2    Khvorostova, J.3    Rofougaran, R.4    Hofer, A.5    Falkenberg, M.6
  • 111
    • 33745637944 scopus 로고    scopus 로고
    • Twinkle, the mitochondrial replicative DNA helicase, is widespread in the eukaryotic radiation and may also be the mitochondrial DNA primase in most eukaryotes
    • Shutt T.E., Gray M.W. Twinkle, the mitochondrial replicative DNA helicase, is widespread in the eukaryotic radiation and may also be the mitochondrial DNA primase in most eukaryotes. J. Mol. Evol. 2006, 62:588-599.
    • (2006) J. Mol. Evol. , vol.62 , pp. 588-599
    • Shutt, T.E.1    Gray, M.W.2
  • 112
    • 1542677230 scopus 로고    scopus 로고
    • TWINKLE has 5'→3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein
    • Korhonen J.A., Gaspari M., Falkenberg M. TWINKLE has 5'→3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein. J. Biol. Chem. 2003, 278:48627-48632.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48627-48632
    • Korhonen, J.A.1    Gaspari, M.2    Falkenberg, M.3
  • 113
    • 84860379072 scopus 로고    scopus 로고
    • Human mitochondrial DNA helicase TWINKLE is both an unwinding and annealing helicase
    • Sen D., Nandakumar D., Tang G.Q., Patel S.S. Human mitochondrial DNA helicase TWINKLE is both an unwinding and annealing helicase. J. Biol. Chem. 2012, 287:14545-14556.
    • (2012) J. Biol. Chem. , vol.287 , pp. 14545-14556
    • Sen, D.1    Nandakumar, D.2    Tang, G.Q.3    Patel, S.S.4
  • 114
  • 115
    • 0042200759 scopus 로고    scopus 로고
    • Replicative helicase loaders: ring breakers and ring makers
    • Davey M.J., O'Donnell M. Replicative helicase loaders: ring breakers and ring makers. Curr. Biol. 2003, 13:R594-R596.
    • (2003) Curr. Biol. , vol.13
    • Davey, M.J.1    O'Donnell, M.2
  • 116
    • 82255185604 scopus 로고    scopus 로고
    • The mitochondrial DNA helicase TWINKLE can assemble on a closed circular template and support initiation of DNA synthesis
    • Jemt E., Farge G., Backstrom S., Holmlund T., Gustafsson C.M., Falkenberg M. The mitochondrial DNA helicase TWINKLE can assemble on a closed circular template and support initiation of DNA synthesis. Nucleic Acids Res. 2011, 39:9238-9249.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 9238-9249
    • Jemt, E.1    Farge, G.2    Backstrom, S.3    Holmlund, T.4    Gustafsson, C.M.5    Falkenberg, M.6
  • 118
    • 34250868951 scopus 로고    scopus 로고
    • Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes
    • Wanrooij S., Goffart S., Pohjoismaki J.L., Yasukawa T., Spelbrink J.N. Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes. Nucleic Acids Res. 2007, 35:3238-3251.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3238-3251
    • Wanrooij, S.1    Goffart, S.2    Pohjoismaki, J.L.3    Yasukawa, T.4    Spelbrink, J.N.5
  • 119
    • 58149163606 scopus 로고    scopus 로고
    • Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling
    • Goffart S., Cooper H.M., Tyynismaa H., Wanrooij S., Suomalainen A., Spelbrink J.N. Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling. Hum. Mol. Genet. 2009, 18:328-340.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 328-340
    • Goffart, S.1    Cooper, H.M.2    Tyynismaa, H.3    Wanrooij, S.4    Suomalainen, A.5    Spelbrink, J.N.6
  • 120
    • 79959272474 scopus 로고    scopus 로고
    • The Pif1 family in prokaryotes: what are our helicases doing in your bacteria?
    • Bochman M.L., Judge C.P., Zakian V.A. The Pif1 family in prokaryotes: what are our helicases doing in your bacteria?. Mol. Biol. Cell 2011, 22:1955-1959.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1955-1959
    • Bochman, M.L.1    Judge, C.P.2    Zakian, V.A.3
  • 121
    • 33749136403 scopus 로고    scopus 로고
    • Roles of Pif1-like helicases in the maintenance of genomic stability
    • Boule J.B., Zakian V.A. Roles of Pif1-like helicases in the maintenance of genomic stability. Nucleic Acids Res. 2006, 34:4147-4153.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4147-4153
    • Boule, J.B.1    Zakian, V.A.2
  • 122
    • 0020823462 scopus 로고
    • Pif mutation blocks recombination between mitochondrial rho+ and rho- genomes having tandemly arrayed repeat units in Saccharomyces cerevisiae
    • Foury F., Kolodynski J. pif mutation blocks recombination between mitochondrial rho+ and rho- genomes having tandemly arrayed repeat units in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1983, 80:5345-5349.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 5345-5349
    • Foury, F.1    Kolodynski, J.2
  • 123
    • 76749129611 scopus 로고    scopus 로고
    • Unwinding the functions of the Pif1 family helicases
    • Bochman M.L., Sabouri N., Zakian V.A. Unwinding the functions of the Pif1 family helicases. DNA Repair (Amst) 2010, 9:237-249.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 237-249
    • Bochman, M.L.1    Sabouri, N.2    Zakian, V.A.3
  • 124
    • 34848908787 scopus 로고    scopus 로고
    • The yeast Pif1p DNA helicase preferentially unwinds RNA DNA substrates
    • Boule J.B., Zakian V.A. The yeast Pif1p DNA helicase preferentially unwinds RNA DNA substrates. Nucleic Acids Res. 2007, 35:5809-5818.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5809-5818
    • Boule, J.B.1    Zakian, V.A.2
  • 125
    • 33845433365 scopus 로고    scopus 로고
    • Human PIF helicase is cell cycle regulated and associates with telomerase
    • Mateyak M.K., Zakian V.A. Human PIF helicase is cell cycle regulated and associates with telomerase. Cell Cycle 2006, 5:2796-2804.
    • (2006) Cell Cycle , vol.5 , pp. 2796-2804
    • Mateyak, M.K.1    Zakian, V.A.2
  • 126
    • 34548635045 scopus 로고    scopus 로고
    • Mitochondrial and nuclear localization of human Pif1 helicase
    • Futami K., Shimamoto A., Furuichi Y. Mitochondrial and nuclear localization of human Pif1 helicase. Biol. Pharm. Bull. 2007, 30:1685-1692.
    • (2007) Biol. Pharm. Bull. , vol.30 , pp. 1685-1692
    • Futami, K.1    Shimamoto, A.2    Furuichi, Y.3
  • 127
    • 56049120070 scopus 로고    scopus 로고
    • Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain
    • Gu Y., Masuda Y., Kamiya K. Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain. Nucleic Acids Res. 2008, 36:6295-6308.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6295-6308
    • Gu, Y.1    Masuda, Y.2    Kamiya, K.3
  • 128
    • 33645009269 scopus 로고    scopus 로고
    • The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity
    • Zhang D.H., Zhou B., Huang Y., Xu L.X., Zhou J.Q. The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity. Nucleic Acids Res. 2006, 34:1393-1404.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1393-1404
    • Zhang, D.H.1    Zhou, B.2    Huang, Y.3    Xu, L.X.4    Zhou, J.Q.5
  • 130
    • 71049180940 scopus 로고    scopus 로고
    • Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks
    • George T., Wen Q., Griffiths R., Ganesh A., Meuth M., Sanders C.M. Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks. Nucleic Acids Res. 2009, 37:6491-6502.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6491-6502
    • George, T.1    Wen, Q.2    Griffiths, R.3    Ganesh, A.4    Meuth, M.5    Sanders, C.M.6
  • 131
    • 77955487510 scopus 로고    scopus 로고
    • Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity
    • Sanders C.M. Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity. Biochem. J. 2010, 430:119-128.
    • (2010) Biochem. J. , vol.430 , pp. 119-128
    • Sanders, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.