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mBio
Volumn 6, Issue 1, 2015, Pages
Mitochondrial heat shock protein machinery Hsp70/Hsp40 Is indispensable for proper mitochondrial DNA maintenance and replication
Author keywords

[No Author keywords available]
Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; IRON SULFUR PROTEIN; KINETOPLAST DNA; MINICIRCLE DNA; MITOCHONDRIAL DNA; PROTOZOAL PROTEIN;
EID: 84924166321     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.02425-14     Document Type: Article
Times cited : (37)
References (91)
  • 2
    • 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 HM, Tyynismaa H, Wanrooij S, Suomalainen A, Spelbrink JN. 2009. Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling. Hum Mol Genet 18: 328-340. http://dx. doi. org/10. 1093/hmg/ddn359.
    • (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
  • 3
    • 77957957247 scopus 로고    scopus 로고
    • The mitochondrial proteome and human disease
    • Calvo SE, Mootha VK. 2010. The mitochondrial proteome and human disease. Annu Rev Genomics Hum Genet 11: 25-44. http://dx. doi. org/10. 1146/annurev-genom-082509-141720.
    • (2010) Annu Rev Genomics Hum Genet , vol.11 , pp. 25-44
    • Calvo, S.E.1    Mootha, V.K.2
  • 4
    • 39649120348 scopus 로고    scopus 로고
    • Inherited mitochondrial diseases of DNA replication
    • Copeland WC. 2008. Inherited mitochondrial diseases of DNA replication. Annu Rev Med 59: 131-146. http://dx. doi. org/10. 1146/annurev. med. 59. 053006. 104646.
    • (2008) Annu Rev Med , vol.59 , pp. 131-146
    • Copeland, W.C.1
  • 5
    • 84876180436 scopus 로고    scopus 로고
    • Mitochondrial DNA depletion syndromes: Review and updates of genetic basis, manifestations, and therapeutic options
    • El-Hattab AW, Scaglia F. 2013. Mitochondrial DNA depletion syndromes: review and updates of genetic basis, manifestations, and therapeutic options. Neurotherapeutics 10: 186-198. http://dx. doi. org/10. 1007/s13311-013-0177-6.
    • (2013) Neurotherapeutics , vol.10 , pp. 186-198
    • El-Hattab, A.W.1    Scaglia, F.2
  • 6
    • 0028125027 scopus 로고
    • Cloning of the hsp70 (dnaK) genes from Rhizobium meliloti and Pseudomonas cepacia: Phylogenetic analyses of mitochondrial origin based on a highly conserved protein sequence
    • Falah M, Gupta RS. 1994. Cloning of the hsp70 (dnaK) genes from Rhizobium meliloti and Pseudomonas cepacia: phylogenetic analyses of mitochondrial origin based on a highly conserved protein sequence. J Bacteriol 176: 7748-7753.
    • (1994) J Bacteriol , vol.176 , pp. 7748-7753
    • Falah, M.1    Gupta, R.S.2
  • 7
    • 34250351297 scopus 로고    scopus 로고
    • A postgenomic view of the heat shock proteins in kinetoplastids
    • Folgueira C, Requena JM. 2007. A postgenomic view of the heat shock proteins in kinetoplastids. FEMS Microbiol Rev 31: 359-377. http://dx. doi. org/10. 1111/j. 1574-6976. 2007. 00069. x.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 359-377
    • Folgueira, C.1    Requena, J.M.2
  • 8
    • 0037009130 scopus 로고    scopus 로고
    • Molecular chaperones as essential mediators of mitochondrial biogenesis
    • Voos W, Röttgers K. 2002. Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592: 51-62. http://dx. doi. org/10. 1016/S0167-4889(02)00264-1.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 51-62
    • Voos, W.1    Röttgers, K.2
  • 9
    • 0035794158 scopus 로고    scopus 로고
    • Mitochondrial Hsp70 Ssc1: Role in protein folding
    • Liu Q, Krzewska J, Liberek K, Craig EA. 2001. Mitochondrial Hsp70 Ssc1: role in protein folding. J Biol Chem 276: 6112-6118. http://dx. doi. org/10. 1074/jbc. M009519200.
    • (2001) J Biol Chem , vol.276 , pp. 6112-6118
    • Liu, Q.1    Krzewska, J.2    Liberek, K.3    Craig, E.A.4
  • 10
    • 0042531776 scopus 로고    scopus 로고
    • Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart
    • Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J. 2003. Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J Biol Chem 278: 29719-29727. http://dx. doi. org/10. 1074/jbc. M303527200.
    • (2003) J Biol Chem , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1    Schilke, B.2    Knieszner, H.3    Walter, W.4    Craig, E.A.5    Marszalek, J.6
  • 11
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill R, Mühlenhoff U. 2008. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu Rev B i o c h e m 7 7: 6 6 9-7 0 0. h t t p://d x. d o i. o r g/1 0. 1 1 4 6/annurev. biochem. 76. 052705. 162653.
    • (2008) Annu Rev B i o c h e m 7 , vol.7 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 12
    • 0037418880 scopus 로고    scopus 로고
    • Regulated cycling of mitochondrial Hsp70 at the protein import channel
    • Liu Q, D'Silva P, Walter W, Marszalek J, Craig EA. 2003. Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300: 139-141. http://dx. doi. org/10. 1126/science. 1083379.
    • (2003) Science , vol.300 , pp. 139-141
    • Liu, Q.1    D'Silva, P.2    Walter, W.3    Marszalek, J.4    Craig, E.A.5
  • 13
    • 37849035275 scopus 로고    scopus 로고
    • The direct route: A simplified pathway for protein import into the mitochondrion of trypanosomes
    • Schneider A, Bursać D, Lithgow T. 2008. The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes. Trends Cell Biol 18: 12-18. http://dx. doi. org/10. 1016/j. tcb. 2007. 09. 009.
    • (2008) Trends Cell Biol , vol.18 , pp. 12-18
    • Schneider, A.1    Bursać, D.2    Lithgow, T.3
  • 14
    • 79961024966 scopus 로고    scopus 로고
    • In vivo study in Trypanosoma brucei links mitochondrial transfer RNA import to mitochondrial protein import
    • Tschopp F, Charrière F, Schneider A. 2011. In vivo study in Trypanosoma brucei links mitochondrial transfer RNA import to mitochondrial protein import. EMBO Rep 12: 825-832. http://dx. doi. org/10. 1038/embor. 2011. 111.
    • (2011) EMBO Rep , vol.12 , pp. 825-832
    • Tschopp, F.1    Charrière, F.2    Schneider, A.3
  • 15
    • 70349467827 scopus 로고    scopus 로고
    • Mitochondrial tRNA import-the challenge to understand has just begun
    • Alfonzo JD, Söll D. 2009. Mitochondrial tRNA import-the challenge to understand has just begun. Biol Chem 390: 717-722. http://dx. doi. org/10. 1515/BC. 2009. 101.
    • (2009) Biol Chem , vol.390 , pp. 717-722
    • Alfonzo, J.D.1    Söll, D.2
  • 16
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
    • Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci U S A 91: 10345-10349. http://dx. doi. org/10. 1073/pnas. 91. 22. 10345.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 17
    • 0031556950 scopus 로고    scopus 로고
    • Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
    • Miao B, Davis JE, Craig EA. 1997. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J Mol Biol 265: 541-552. http://dx. doi. org/10. 1006/jmbi. 1996. 0762.
    • (1997) J Mol Biol , vol.265 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 18
    • 0035850757 scopus 로고    scopus 로고
    • The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1
    • Schmidt S, Strub A, Röttgers K, Zufall N, Voos W. 2001. The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1. J Mol Biol 313: 13-26. http://dx. doi. org/10. 1006/jmbi. 2001. 5013.
    • (2001) J Mol Biol , vol.313 , pp. 13-26
    • Schmidt, S.1    Strub, A.2    Röttgers, K.3    Zufall, N.4    Voos, W.5
  • 19
    • 36349010951 scopus 로고    scopus 로고
    • The interplay between components of the mitochondrial protein translocation motor studied using purified components
    • Slutsky-Leiderman O, Marom M, Iosefson O, Levy R, Maoz S, Azem A. 2007. The interplay between components of the mitochondrial protein translocation motor studied using purified components. J Biol Chem 282: 33935-33942. http://dx. doi. org/10. 1074/jbc. M704435200.
    • (2007) J Biol Chem , vol.282 , pp. 33935-33942
    • Slutsky-Leiderman, O.1    Marom, M.2    Iosefson, O.3    Levy, R.4    Maoz, S.5    Azem, A.6
  • 20
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan CY, Lee S, Cyr DM. 2003. Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8: 309-316. http://dx. doi. org/10. 1379/1466-1268(2003)008_0309: MFROHF_2. 0. CO; 2.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 21
    • 84871792997 scopus 로고    scopus 로고
    • Mitochondrial protein import: Common principles and physiological networks
    • Dudek J, Rehling P, van der Laan M. 2013. Mitochondrial protein import: common principles and physiological networks. Biochim Biophys Acta 1833: 274-285. http://dx. doi. org/10. 1016/j. bbamcr. 2012. 05. 028.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 274-285
    • Dudek, J.1    Rehling, P.2    van der Laan, M.3
  • 22
    • 77958456516 scopus 로고    scopus 로고
    • The Hsp70 chaperones of the Tritryps are characterized by unusual features and novel members
    • Louw CA, Ludewig MH, Mayer J, Blatch GL. 2010. The Hsp70 chaperones of the Tritryps are characterized by unusual features and novel members. Parasitol Int 59: 497-505. http://dx. doi. org/10. 1016/j. parint. 2010. 08. 008.
    • (2010) Parasitol Int , vol.59 , pp. 497-505
    • Louw, C.A.1    Ludewig, M.H.2    Mayer, J.3    Blatch, G.L.4
  • 23
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • Uzarska MA, Dutkiewicz R, Freibert SA, Lill R, Mühlenhoff U. 2013. The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation. Mol Biol Cell 24: 1830-1841. http://dx. doi. org/10. 1091/mbc. E12-09-0644.
    • (2013) Mol Biol Cell , vol.24 , pp. 1830-1841
    • Uzarska, M.A.1    Dutkiewicz, R.2    Freibert, S.A.3    Lill, R.4    Mühlenhoff, U.5
  • 24
    • 0042736165 scopus 로고    scopus 로고
    • Ecm10p localizes in yeast mitochondrial nucleoids and its overexpression induces extensive mitochondrial DNA aggregations
    • Sakasegawa Y, Hachiya NS, Tsukita S, Kaneko K. 2003. Ecm10p localizes in yeast mitochondrial nucleoids and its overexpression induces extensive mitochondrial DNA aggregations. Biochem Biophys Res Commun 309: 217-221. http://dx. doi. org/10. 1016/S0006-291X(03)01548-1.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 217-221
    • Sakasegawa, Y.1    Hachiya, N.S.2    Tsukita, S.3    Kaneko, K.4
  • 25
    • 0034731487 scopus 로고    scopus 로고
    • Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae
    • Baumann F, Milisav I, Neupert W, Herrmann JM. 2000. Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae. FEBS Lett 487: 307-312. http://dx. doi. org/10. 1016/S0014-5793(00)02364-4.
    • (2000) FEBS Lett , vol.487 , pp. 307-312
    • Baumann, F.1    Milisav, I.2    Neupert, W.3    Herrmann, J.M.4
  • 26
    • 0023956637 scopus 로고
    • The dnaK gene of Escherichia coli functions in initiation of chromosome replication
    • Sakakibara Y. 1988. The dnaK gene of Escherichia coli functions in initiation of chromosome replication. J Bacteriol 170: 972-979.
    • (1988) J Bacteriol , vol.170 , pp. 972-979
    • Sakakibara, Y.1
  • 27
    • 0027251270 scopus 로고
    • Heat shock proteins DnaJ, DnaK, and GrpE stimulate P1 plasmid replication by promoting initiator binding to the origin
    • Sozhamannan S, Chattoraj DK. 1993. Heat shock proteins DnaJ, DnaK, and GrpE stimulate P1 plasmid replication by promoting initiator binding to the origin. J Bacteriol 175: 3546-3555.
    • (1993) J Bacteriol , vol.175 , pp. 3546-3555
    • Sozhamannan, S.1    Chattoraj, D.K.2
  • 28
    • 0027050320 scopus 로고
    • Activity of the Hsp70 chaperone complex-DnaK, DnaJ, and GrpE-in initiating phage lambda DNA replication by sequestering and releasing lambda P protein
    • Hoffmann HJ, Lyman SK, Lu C, Petit MA, Echols H. 1992. Activity of the Hsp70 chaperone complex-DnaK, DnaJ, and GrpE-in initiating phage lambda DNA replication by sequestering and releasing lambda P protein. Proc Natl Acad Sci U S A 89: 12108-12111. http://dx. doi. org/10. 1073/pnas. 89. 24. 12108.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 12108-12111
    • Hoffmann, H.J.1    Lyman, S.K.2    Lu, C.3    Petit, M.A.4    Echols, H.5
  • 29
    • 15544362672 scopus 로고    scopus 로고
    • All three J-domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins
    • Gur E, Katz C, Ron EZ. 2005. All three J-domain proteins of the Escherichia coli DnaK chaperone machinery are DNA binding proteins. FEBS Lett 579: 1935-1939. http://dx. doi. org/10. 1016/j. febslet. 2005. 01. 084.
    • (2005) FEBS Lett , vol.579 , pp. 1935-1939
    • Gur, E.1    Katz, C.2    Ron, E.Z.3
  • 30
    • 33645974004 scopus 로고    scopus 로고
    • Mitochondrial chromosome structure: An insight from analysis of complete yeast genomes
    • Nosek J, Tomáška L, Bolotin-Fukuhara M, Miyakawa I. 2006. Mitochondrial chromosome structure: an insight from analysis of complete yeast genomes. FEMS Yeast Res 6: 356-370. http://dx. doi. org/10. 1111/j. 1567-1364. 2005. 00016. x.
    • (2006) FEMS Yeast Res , vol.6 , pp. 356-370
    • Nosek, J.1    Tomáška, L.2    Bolotin-Fukuhara, M.3    Miyakawa, I.4
  • 31
    • 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 DF. 2006. Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane. J Biol Chem 281: 25791-25802. http://dx. doi. org/10. 1074/jbc. M604501200.
    • (2006) J Biol Chem , vol.281 , pp. 25791-25802
    • Wang, Y.1    Bogenhagen, D.F.2
  • 32
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • Bogenhagen DF, Rousseau D, Burke S. 2008. The layered structure of human mitochondrial DNA nucleoids. J Biol Chem 283: 3665-3675. http://dx. doi. org/10. 1074/jbc. M708444200.
    • (2008) J Biol Chem , vol.283 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 34
    • 0024347362 scopus 로고
    • Molecular cloning of mtp70, a mitochondrial member of the hsp70 family
    • Engman DM, Kirchhoff LV, Donelson JE. 1989. Molecular cloning of mtp70, a mitochondrial member of the hsp70 family. Mol Cell Biol 9: 5163-5168.
    • (1989) Mol Cell Biol , vol.9 , pp. 5163-5168
    • Engman, D.M.1    Kirchhoff, L.V.2    Donelson, J.E.3
  • 37
    • 0037008763 scopus 로고    scopus 로고
    • A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase
    • Germaniuk A, Liberek K, Marszalek J. 2002. A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277: 27801-27808. http://dx. doi. org/10. 1074/jbc. M201756200.
    • (2002) J Biol Chem , vol.277 , pp. 27801-27808
    • Germaniuk, A.1    Liberek, K.2    Marszalek, J.3
  • 38
    • 33744964531 scopus 로고    scopus 로고
    • Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate
    • Lu B, Garrido N, Spelbrink JN, Suzuki CK. 2006. Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate. J Biol Chem 281: 13150-13158. http://dx. doi. org/10. 1074/jbc. M509179200.
    • (2006) J Biol Chem , vol.281 , pp. 13150-13158
    • Lu, B.1    Garrido, N.2    Spelbrink, J.N.3    Suzuki, C.K.4
  • 41
    • 0017867183 scopus 로고
    • The replication of kinetoplast DNA networks in Crithidia fasciculata
    • Englund PT. 1978. The replication of kinetoplast DNA networks in Crithidia fasciculata. Cell 14: 157-168. http://dx. doi. org/10. 1016/0092-8674(78)90310-0.
    • (1978) Cell , vol.14 , pp. 157-168
    • Englund, P.T.1
  • 42
    • 0025061165 scopus 로고
    • Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei
    • Woodward R, Gull K. 1990. Timing of nuclear and kinetoplast DNA replication and early morphological events in the cell cycle of Trypanosoma brucei. J Cell Sci 95: 49-57.
    • (1990) J Cell Sci , vol.95 , pp. 49-57
    • Woodward, R.1    Gull, K.2
  • 43
    • 84872241347 scopus 로고    scopus 로고
    • Network news: The replication of kinetoplast DNA
    • Jensen RE, Englund PT. 2012. Network news: the replication of kinetoplast DNA. Annu Rev Microbiol 66: 473-491. http://dx. doi. org/10. 1146/annurev-micro-092611-150057.
    • (2012) Annu Rev Microbiol , vol.66 , pp. 473-491
    • Jensen, R.E.1    Englund, P.T.2
  • 44
    • 84872865493 scopus 로고    scopus 로고
    • Dual core processing: MRB1 is an emerging kinetoplast RNA editing complex
    • Hashimi H, Zimmer SL, Ammerman ML, Read LK, Lukeš J. 2013. Dual core processing: MRB1 is an emerging kinetoplast RNA editing complex. Trends Parasitol 29: 91-99. http://dx. doi. org/10. 1016/j. pt. 2012. 11. 005.
    • (2013) Trends Parasitol , vol.29 , pp. 91-99
    • Hashimi, H.1    Zimmer, S.L.2    Ammerman, M.L.3    Read, L.K.4    Lukeš, J.5
  • 46
    • 0037910381 scopus 로고    scopus 로고
    • A high-order transmembrane structural linkage is responsible for mitochondrial genome positioning and segregation by flagellar basal bodies in trypanosomes
    • Ogbadoyi EO, Robinson DR, Gull K. 2003. A high-order transmembrane structural linkage is responsible for mitochondrial genome positioning and segregation by flagellar basal bodies in trypanosomes. Mol Biol Cell 14: 1769-1779. http://dx. doi. org/10. 1091/mbc. E02-08-0525.
    • (2003) Mol Biol Cell , vol.14 , pp. 1769-1779
    • Ogbadoyi, E.O.1    Robinson, D.R.2    Gull, K.3
  • 52
    • 15044362303 scopus 로고    scopus 로고
    • Energy generation in insect stages of Trypanosoma brucei: Metabolism in flux
    • Besteiro S, Barrett MP, Rivière L, Bringaud F. 2005. Energy generation in insect stages of Trypanosoma brucei: metabolism in flux. Trends Parasitol 21: 185-191. http://dx. doi. org/10. 1016/j. pt. 2005. 02. 008.
    • (2005) Trends Parasitol , vol.21 , pp. 185-191
    • Besteiro, S.1    Barrett, M.P.2    Rivière, L.3    Bringaud, F.4
  • 53
    • 33745844850 scopus 로고    scopus 로고
    • Role of p38 in replication of Trypanosoma brucei kinetoplast DNA
    • Liu B, Molina H, Kalume D, Pandey A, Griffith JD, Englund PT. 2006. Role of p38 in replication of Trypanosoma brucei kinetoplast DNA. Mol Cell Biol 26: 5382-5393. http://dx. doi. org/10. 1128/MCB. 00369-06.
    • (2006) Mol Cell Biol , vol.26 , pp. 5382-5393
    • Liu, B.1    Molina, H.2    Kalume, D.3    Pandey, A.4    Griffith, J.D.5    Englund, P.T.6
  • 54
    • 0036342502 scopus 로고    scopus 로고
    • Multiple mitochondrial DNA polymerases in Trypanosoma brucei
    • Klingbeil MM, Motyka SA, Englund PT. 2002. Multiple mitochondrial DNA polymerases in Trypanosoma brucei. Mol Cell 10: 175-186. http://dx. doi. org/10. 1016/S1097-2765(02)00571-3.
    • (2002) Mol Cell , vol.10 , pp. 175-186
    • Klingbeil, M.M.1    Motyka, S.A.2    Englund, P.T.3
  • 55
    • 57349176187 scopus 로고    scopus 로고
    • Stem-loop silencing reveals that a third mitochondrial DNA polymerase, POLID, is required for kinetoplast DNA replication in trypanosomes
    • Chandler J, Vandoros AV, Mozeleski B, Klingbeil MM. 2008. Stem-loop silencing reveals that a third mitochondrial DNA polymerase, POLID, is required for kinetoplast DNA replication in trypanosomes. Eukaryot Cell 7: 2141-2146. http://dx. doi. org/10. 1128/EC. 00199-08.
    • (2008) Eukaryot Cell , vol.7 , pp. 2141-2146
    • Chandler, J.1    Vandoros, A.V.2    Mozeleski, B.3    Klingbeil, M.M.4
  • 56
    • 38449123072 scopus 로고    scopus 로고
    • A mitochondrial topoisomerase IA essential for late theta structure resolution in African trypanosomes
    • Scocca JR, Shapiro TA. 2008. A mitochondrial topoisomerase IA essential for late theta structure resolution in African trypanosomes. Mol Microbiol 67: 820-829. http://dx. doi. org/10. 1111/j. 1365-2958. 2007. 06087. x.
    • (2008) Mol Microbiol , vol.67 , pp. 820-829
    • Scocca, J.R.1    Shapiro, T.A.2
  • 57
    • 77749330824 scopus 로고    scopus 로고
    • A mitochondrial DNA primase is essential for cell growth and kinetoplast DNA replication in Trypanosoma brucei
    • Hines JC, Ray DS. 2010. A mitochondrial DNA primase is essential for cell growth and kinetoplast DNA replication in Trypanosoma brucei. Mol Cell Biol 30: 1319-1328. http://dx. doi. org/10. 1128/MCB. 01231-09.
    • (2010) Mol Cell Biol , vol.30 , pp. 1319-1328
    • Hines, J.C.1    Ray, D.S.2
  • 59
    • 84863332115 scopus 로고    scopus 로고
    • Dynamic localization of Trypanosoma brucei mitochondrial DNA polymerase ID
    • Concepción-Acevedo J, Luo J, Klingbeil MM. 2012. Dynamic localization of Trypanosoma brucei mitochondrial DNA polymerase ID. Eukaryot Cell 11: 844-855. http://dx. doi. org/10. 1128/EC. 05291-11.
    • (2012) Eukaryot Cell , vol.11 , pp. 844-855
    • Concepción-Acevedo, J.1    Luo, J.2    Klingbeil, M.M.3
  • 60
    • 84901632078 scopus 로고    scopus 로고
    • Ultrastructure and molecular phylogeny of four new species of monoxenous trypanosomatids from flies (Diptera: Brachycera) with redefinition of the genus Wallaceina
    • Yurchenko V, Votýpka J, Tesařová M, Klepetková H, Kraeva N, Jirků M, Lukeš J. 2014. Ultrastructure and molecular phylogeny of four new species of monoxenous trypanosomatids from flies (Diptera: Brachycera) with redefinition of the genus Wallaceina. Folia Parasitol 61: 97-112. http://dx. doi. org/10. 14411/fp. 2014. 023.
    • (2014) Folia Parasitol , vol.61 , pp. 97-112
    • Yurchenko, V.1    Votýpka, J.2    Tesařová, M.3    Klepetková, H.4    Kraeva, N.5    Jirků, M.6    Lukeš, J.7
  • 62
    • 84860369351 scopus 로고    scopus 로고
    • Protein translocase of mitochondrial inner membrane in Trypanosoma brucei
    • Singha UK, Hamilton V, Duncan MR, Weems E, Tripathi MK, Chaudhuri M. 2012. Protein translocase of mitochondrial inner membrane in Trypanosoma brucei. J Biol Chem 287: 14480-14493. http://dx. doi. org/10. 1074/jbc. M111. 322925.
    • (2012) J Biol Chem , vol.287 , pp. 14480-14493
    • Singha, U.K.1    Hamilton, V.2    Duncan, M.R.3    Weems, E.4    Tripathi, M.K.5    Chaudhuri, M.6
  • 63
    • 0028361303 scopus 로고
    • Kinetoplastidae display naturally occurring ancillary DNA-containing structures
    • Miyahira Y, Dvorak JA. 1994. Kinetoplastidae display naturally occurring ancillary DNA-containing structures. Mol Biochem Parasitol 65: 339-349. http://dx. doi. org/10. 1016/0166-6851(94)90084-1.
    • (1994) Mol Biochem Parasitol , vol.65 , pp. 339-349
    • Miyahira, Y.1    Dvorak, J.A.2
  • 64
    • 13244257143 scopus 로고    scopus 로고
    • RNA interference analyses suggest a transcript-specific regulatory role for mitochondrial RNA-binding proteins MRP1 and MRP2 in RNA editing and other RNA processing in Trypanosoma brucei
    • Vondrušková E, van den Burg J, Zíková A, Ernst NL, Stuart K, Benne R, Lukeš J. 2005. RNA interference analyses suggest a transcript-specific regulatory role for mitochondrial RNA-binding proteins MRP1 and MRP2 in RNA editing and other RNA processing in Trypanosoma brucei. J Biol Chem 280: 2429-2438. http://dx. doi. org/10. 1074/jbc. M405933200.
    • (2005) J Biol Chem , vol.280 , pp. 2429-2438
    • Vondrušková, E.1    van den Burg, J.2    Zíková, A.3    Ernst, N.L.4    Stuart, K.5    Benne, R.6    Lukeš, J.7
  • 65
    • 33749415299 scopus 로고    scopus 로고
    • Knock-downs of iron-sulfur cluster assembly proteins IscS and IscU down-regulate the active mitochondrion of procyclic Trypanosoma brucei
    • Smíd O, Horáková E, Vilímová V, Hrdy I, Cammack R, Horváth A, Lukeš J, Tachezy J. 2006. Knock-downs of iron-sulfur cluster assembly proteins IscS and IscU down-regulate the active mitochondrion of procyclic Trypanosoma brucei. J Biol Chem 281: 28679-28686. http://dx. doi. org/10. 1074/jbc. M513781200.
    • (2006) J Biol Chem , vol.281 , pp. 28679-28686
    • Smíd, O.1    Horáková, E.2    Vilímová, V.3    Hrdy, I.4    Cammack, R.5    Horváth, A.6    Lukeš, J.7    Tachezy, J.8
  • 66
    • 45149131789 scopus 로고    scopus 로고
    • Ancestral roles of eukaryotic frataxin: Mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes
    • Long S, Jirků M, Mach J, Ginger ML, Sutak R, Richardson D, Tachezy J, Lukeš J. 2008. Ancestral roles of eukaryotic frataxin: mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes. Mol Microbiol 69: 94-109. http://dx. doi. org/10. 1111/j. 1365-2958. 2008. 06260. x.
    • (2008) Mol Microbiol , vol.69 , pp. 94-109
    • Long, S.1    Jirků, M.2    Mach, J.3    Ginger, M.L.4    Sutak, R.5    Richardson, D.6    Tachezy, J.7    Lukeš, J.8
  • 67
    • 77954619982 scopus 로고    scopus 로고
    • The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei
    • Paris Z, Changmai P, Rubio MA, Zíková A, Stuart KD, Alfonzo JD, Lukeš J. 2010. The Fe/S cluster assembly protein Isd11 is essential for tRNA thiolation in Trypanosoma brucei. J Biol Chem 285: 22394-22402. http://dx. doi. org/10. 1074/jbc. M109. 083774.
    • (2010) J Biol Chem , vol.285 , pp. 22394-22402
    • Paris, Z.1    Changmai, P.2    Rubio, M.A.3    Zíková, A.4    Stuart, K.D.5    Alfonzo, J.D.6    Lukeš, J.7
  • 68
    • 50049135930 scopus 로고    scopus 로고
    • Analysis of the Trypanosoma brucei cell cycle by quantitative DAPI imaging
    • Siegel TN, Hekstra DR, Cross GA. 2008. Analysis of the Trypanosoma brucei cell cycle by quantitative DAPI imaging. Mol Biochem Parasitol 160: 171-174. http://dx. doi. org/10. 1016/j. molbiopara. 2008. 04. 004.
    • (2008) Mol Biochem Parasitol , vol.160 , pp. 171-174
    • Siegel, T.N.1    Hekstra, D.R.2    Cross, G.A.3
  • 69
    • 0018786803 scopus 로고
    • Free minicircles of kinetoplast DNA in Crithidia fasciculata
    • Englund PT. 1979. Free minicircles of kinetoplast DNA in Crithidia fasciculata. J Biol Chem 254: 4895-4900.
    • (1979) J Biol Chem , vol.254 , pp. 4895-4900
    • Englund, P.T.1
  • 70
    • 0024340331 scopus 로고
    • Synthesis and processing of kinetoplast DNAminicircles in Trypanosoma equiperdum
    • Ryan KA, Englund PT. 1989. Synthesis and processing of kinetoplast DNAminicircles in Trypanosoma equiperdum. Mol Cell Biol 9: 3212-3217.
    • (1989) Mol Cell Biol , vol.9 , pp. 3212-3217
    • Ryan, K.A.1    Englund, P.T.2
  • 71
    • 41449087417 scopus 로고    scopus 로고
    • Effect of hydroxyurea on procyclic Trypanosoma brucei: An unconventional mechanism for achieving synchronous growth
    • Chowdhury AR, Zhao Z, Englund PT. 2008. Effect of hydroxyurea on procyclic Trypanosoma brucei: an unconventional mechanism for achieving synchronous growth. Eukaryot Cell 7: 425-428. http://dx. doi. org/10. 1128/EC. 00369-07.
    • (2008) Eukaryot Cell , vol.7 , pp. 425-428
    • Chowdhury, A.R.1    Zhao, Z.2    Englund, P.T.3
  • 72
    • 0028965720 scopus 로고
    • Mitochondrial heat shock protein 70 is distributed throughout the mitochondrion in a dyskinetoplastic mutant of Trypanosoma brucei
    • Klein KG, Olson CL, Engman DM. 1995. Mitochondrial heat shock protein 70 is distributed throughout the mitochondrion in a dyskinetoplastic mutant of Trypanosoma brucei. Mol Biochem Parasitol 70: 207-209. http://dx. doi. org/10. 1016/0166-6851(95)00013-Q.
    • (1995) Mol Biochem Parasitol , vol.70 , pp. 207-209
    • Klein, K.G.1    Olson, C.L.2    Engman, D.M.3
  • 73
    • 0027267007 scopus 로고
    • Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major
    • Searle S, McCrossan MV, Smith DF. 1993. Expression of a mitochondrial stress protein in the protozoan parasite Leishmania major. J Cell Sci 104: 1091-1100.
    • (1993) J Cell Sci , vol.104 , pp. 1091-1100
    • Searle, S.1    McCrossan, M.V.2    Smith, D.F.3
  • 75
    • 84874025753 scopus 로고    scopus 로고
    • Proteomic analysis reveals diverse classes of arginine methylproteins in mitochondria of trypanosomes
    • Fisk JC, Li J, Wang H, Aletta JM, Qu J, Read LK. 2013. Proteomic analysis reveals diverse classes of arginine methylproteins in mitochondria of trypanosomes. Mol Cell Proteomics 12: 302-311. http://dx. doi. org/10. 1074/mcp. M112. 022533.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 302-311
    • Fisk, J.C.1    Li, J.2    Wang, H.3    Aletta, J.M.4    Qu, J.5    Read, L.K.6
  • 76
    • 84856035513 scopus 로고    scopus 로고
    • TbPIF8, a Trypanosoma brucei protein related to the yeast Pif1 helicase, is essential for cell viability and mitochondrial genome maintenance
    • Wang J, Englund PT, Jensen RE. 2012. TbPIF8, a Trypanosoma brucei protein related to the yeast Pif1 helicase, is essential for cell viability and mitochondrial genome maintenance. Mol Microbiol 83: 471-485. http://dx. doi. org/10. 1111/j. 1365-2958. 2011. 07938. x.
    • (2012) Mol Microbiol , vol.83 , pp. 471-485
    • Wang, J.1    Englund, P.T.2    Jensen, R.E.3
  • 77
    • 41149092935 scopus 로고    scopus 로고
    • Adaptations of Trypanosoma brucei to gradual loss of kinetoplast DNA: Trypanosoma equiperdum and Trypanosoma evansi are petite mutants of T. brucei
    • Lai D-, Hashimi H, Lun Z-, Ayala FJ, Lukeš J. 2008. Adaptations of Trypanosoma brucei to gradual loss of kinetoplast DNA: Trypanosoma equiperdum and Trypanosoma evansi are petite mutants of T. brucei. Proc Natl Acad Sci U S A 105: 1999-2004. http://dx. doi. org/10. 1073/pnas. 0711799105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 1999-2004
    • Lai, D.1    Hashimi, H.2    Lun, Z.3    Ayala, F.J.4    Lukeš, J.5
  • 78
    • 68949202846 scopus 로고    scopus 로고
    • Trypanosomes have six mitochondrial DNA helicases with one controlling kinetoplast maxicircle replication
    • Liu B, Wang J, Yaffe N, Lindsay ME, Zhao Z, Zick A, Shlomai J, Englund PT. 2009. Trypanosomes have six mitochondrial DNA helicases with one controlling kinetoplast maxicircle replication. Mol Cell 35: 490-501. http://dx. doi. org/10. 1016/j. molcel. 2009. 07. 004.
    • (2009) Mol Cell , vol.35 , pp. 490-501
    • Liu, B.1    Wang, J.2    Yaffe, N.3    Lindsay, M.E.4    Zhao, Z.5    Zick, A.6    Shlomai, J.7    Englund, P.T.8
  • 79
    • 0037805691 scopus 로고    scopus 로고
    • RBP38, a novel RNA-binding protein from trypanosomatid mitochondria, modulates RNA stability
    • Sbicego S, Alfonzo JD, Estévez AM, Rubio MA, Kang X, Turck CW, Peris M, Simpson L. 2003. RBP38, a novel RNA-binding protein from trypanosomatid mitochondria, modulates RNA stability. Eukaryot Cell 2: 560-568. http://dx. doi. org/10. 1128/EC. 2. 3. 560-568. 2003.
    • (2003) Eukaryot Cell , vol.2 , pp. 560-568
    • Sbicego, S.1    Alfonzo, J.D.2    Estévez, A.M.3    Rubio, M.A.4    Kang, X.5    Turck, C.W.6    Peris, M.7    Simpson, L.8
  • 80
    • 79952292701 scopus 로고    scopus 로고
    • A second mitochondrial DNA primase is essential for cell growth and kinetoplast minicircle DNA replication in Trypanosoma brucei
    • Hines JC, Ray DS. 2011. A second mitochondrial DNA primase is essential for cell growth and kinetoplast minicircle DNA replication in Trypanosoma brucei. Eukaryot Cell 10: 445-454. http://dx. doi. org/10. 1128/EC. 00308-10.
    • (2011) Eukaryot Cell , vol.10 , pp. 445-454
    • Hines, J.C.1    Ray, D.S.2
  • 81
    • 18044389729 scopus 로고    scopus 로고
    • Mitochondrial DNA ligases of Trypanosoma brucei
    • Downey N, Hines JC, Sinha KM, Ray DS. 2005. Mitochondrial DNA ligases of Trypanosoma brucei. Eukaryot Cell 4: 765-774. http://dx. doi. org/10. 1128/EC. 4. 4. 765-774. 2005.
    • (2005) Eukaryot Cell , vol.4 , pp. 765-774
    • Downey, N.1    Hines, J.C.2    Sinha, K.M.3    Ray, D.S.4
  • 82
    • 70349659011 scopus 로고    scopus 로고
    • TbPIF5 is a Trypanosoma brucei mitochondrial DNA helicase involved in processing of minicircle Okazaki fragments
    • Liu B, Wang J, Yildirir G, Englund PT. 2009. TbPIF5 is a Trypanosoma brucei mitochondrial DNA helicase involved in processing of minicircle Okazaki fragments. PLoS Pathog 5: e1000589. http://dx. doi. org/10. 1371/journal. ppat. 1000589.
    • (2009) PLoS Pathog , vol.5
    • Liu, B.1    Wang, J.2    Yildirir, G.3    Englund, P.T.4
  • 83
    • 77951221949 scopus 로고    scopus 로고
    • TbPIF1, a Trypanosoma brucei mitochondrial DNA helicase, is essential for kinetoplast minicircle replication
    • Liu B, Yildirir G, Wang J, Tolun G, Griffith JD, Englund PT. 2010. TbPIF1, a Trypanosoma brucei mitochondrial DNA helicase, is essential for kinetoplast minicircle replication. J Biol Chem 285: 7056-7066. http://dx. doi. org/10. 1074/jbc. M109. 084038.
    • (2010) J Biol Chem , vol.285 , pp. 7056-7066
    • Liu, B.1    Yildirir, G.2    Wang, J.3    Tolun, G.4    Griffith, J.D.5    Englund, P.T.6
  • 84
    • 1542677269 scopus 로고    scopus 로고
    • Trypanosoma brucei has two distinct mitochondrialDNApolymerase beta enzymes
    • Saxowsky TT, Choudhary G, Klingbeil MM, Englund PT. 2003. Trypanosoma brucei has two distinct mitochondrialDNApolymerase beta enzymes. J Biol Chem 278: 49095-49101. http://dx. doi. org/10. 1074/jbc. M308565200.
    • (2003) J Biol Chem , vol.278 , pp. 49095-49101
    • Saxowsky, T.T.1    Choudhary, G.2    Klingbeil, M.M.3    Englund, P.T.4
  • 85
    • 58149136352 scopus 로고    scopus 로고
    • DNA polymerase kappa from Trypanosoma cruzi localizes to the mitochondria, bypasses 8-oxoguanine lesions and performs DNA synthesis in a recombination intermediate
    • Rajão MA, Passos-Silva DG, DaRocha WD, Franco GR, Macedo AM, Pena SD, Teixeira SM, Machado CR. 2009. DNA polymerase kappa from Trypanosoma cruzi localizes to the mitochondria, bypasses 8-oxoguanine lesions and performs DNA synthesis in a recombination intermediate. Mol Microbiol 71: 185-197. http://dx. doi. org/10. 1111/j. 1365-2958. 2008. 06521. x.
    • (2009) Mol Microbiol , vol.71 , pp. 185-197
    • Rajão, M.A.1    Passos-Silva, D.G.2    DaRocha, W.D.3    Franco, G.R.4    Macedo, A.M.5    Pena, S.D.6    Teixeira, S.M.7    Machado, C.R.8
  • 86
    • 84871793725 scopus 로고    scopus 로고
    • Chaperone-protease networks in mitochondrial protein homeostasis
    • Voos W. 2013. Chaperone-protease networks in mitochondrial protein homeostasis. Biochim Biophys Acta 1833: 388-399. http://dx. doi. org/10. 1016/j. bbamcr. 2012. 06. 005.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 388-399
    • Voos, W.1
  • 87
    • 84861551208 scopus 로고    scopus 로고
    • DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster
    • Wu Y, Brosh RM. 2012. DNA helicase and helicase-nuclease enzymes with a conserved iron-sulfur cluster. Nucleic Acids Res 40: 4247-4260. http://dx. doi. org/10. 1093/nar/gks039.
    • (2012) Nucleic Acids Res , vol.40 , pp. 4247-4260
    • Wu, Y.1    Brosh, R.M.2
  • 89
    • 27744552907 scopus 로고    scopus 로고
    • Highly efficient tandem affinity purification of trypanosome protein complexes based on a novel epitope combination
    • Schimanski B, Nguyen TN, Günzl A. 2005. Highly efficient tandem affinity purification of trypanosome protein complexes based on a novel epitope combination. Eukaryot Cell 4: 1942-1950. http://dx. doi. org/10. 1128/EC. 4. 11. 1942-1950. 2005.
    • (2005) Eukaryot Cell , vol.4 , pp. 1942-1950
    • Schimanski, B.1    Nguyen, T.N.2    Günzl, A.3
  • 90
    • 84906933588 scopus 로고    scopus 로고
    • Cytosolic iron-sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream Trypanosoma brucei
    • Basu S, Netz DJ, Haindrich AC, Herlerth N, Lagny TJ, Pierik AJ, Lill R, Lukeš J. 2014. Cytosolic iron-sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream Trypanosoma brucei. Mol Microbiol 93: 897-910. http://dx. doi. org/10. 1111/mmi. 12706.
    • (2014) Mol Microbiol , vol.93 , pp. 897-910
    • Basu, S.1    Netz, D.J.2    Haindrich, A.C.3    Herlerth, N.4    Lagny, T.J.5    Pierik, A.J.6    Lill, R.7    Lukeš, J.8
  • 91
    • 0022262659 scopus 로고
    • A gap at a unique location in newly replicated kinetoplast DNA minicircles from Trypanosoma equiperdum
    • Ntambi JM, Englund PT. 1985. A gap at a unique location in newly replicated kinetoplast DNA minicircles from Trypanosoma equiperdum. J Biol Chem 260: 5574-5579.
    • (1985) J Biol Chem , vol.260 , pp. 5574-5579
    • Ntambi, J.M.1    Englund, P.T.2

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