메뉴 건너뛰기




Volumn 15, Issue 10, 2013, Pages 1660-1673

The prokaryotic ClpQ protease plays a key role in growth and development of mitochondria in Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

CLPQ PROTEIN; PROTEASOME; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84884703496     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12142     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 59249092921 scopus 로고    scopus 로고
    • Rab11A-controlled assembly of the inner membrane complex is required for completion of apicomplexan cytokinesis
    • Agop-Nersesian, C., Naissant, B., Ben Rached, F., Rauch, M., Kretzschmar, A., Thiberge, S., etal. (2009) Rab11A-controlled assembly of the inner membrane complex is required for completion of apicomplexan cytokinesis. PLoS Pathog 5: e1000270.
    • (2009) PLoS Pathog , vol.5
    • Agop-Nersesian, C.1    Naissant, B.2    Ben Rached, F.3    Rauch, M.4    Kretzschmar, A.5    Thiberge, S.6
  • 2
    • 36749086400 scopus 로고    scopus 로고
    • An FKBP destabilization domain modulates protein levels in Plasmodium falciparum
    • Armstrong, C.M., and Goldberg, D.E. (2007) An FKBP destabilization domain modulates protein levels in Plasmodium falciparum. Nat Methods 4: 1007-1009.
    • (2007) Nat Methods , vol.4 , pp. 1007-1009
    • Armstrong, C.M.1    Goldberg, D.E.2
  • 3
    • 75149132523 scopus 로고    scopus 로고
    • RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
    • Barik, S., Sureka, K., Mukherjee, P., Basu, J., and Kundu, M. (2010) RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis. Mol Microbiol 75: 592-606.
    • (2010) Mol Microbiol , vol.75 , pp. 592-606
    • Barik, S.1    Sureka, K.2    Mukherjee, P.3    Basu, J.4    Kundu, M.5
  • 4
    • 0034232515 scopus 로고    scopus 로고
    • Proteases involved in erythrocyte invasion by the malaria parasite: function and potential as chemotherapeutic targets
    • Blackman, M.J. (2000) Proteases involved in erythrocyte invasion by the malaria parasite: function and potential as chemotherapeutic targets. Curr Drug Targets 1: 59-83.
    • (2000) Curr Drug Targets , vol.1 , pp. 59-83
    • Blackman, M.J.1
  • 5
    • 0037052931 scopus 로고    scopus 로고
    • Transcripts of developmentally regulated Plasmodium falciparum genes quantified by realtime RT-PCR
    • Blair, P.L., Witney, A., Haynes, J.D., Moch, J.K., Carucci, D.J., and Adams, J.H. (2002) Transcripts of developmentally regulated Plasmodium falciparum genes quantified by realtime RT-PCR. Nucleic Acids Res 30: 2224-2231.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2224-2231
    • Blair, P.L.1    Witney, A.2    Haynes, J.D.3    Moch, J.K.4    Carucci, D.J.5    Adams, J.H.6
  • 7
    • 15744384860 scopus 로고    scopus 로고
    • Down regulation of the human Lon protease impairs mitochondrial structure and function and causes cell death
    • Bota, D.A., Ngo, J.K., and Davies, K.J. (2005) Down regulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic Biol Med 38: 665-677.
    • (2005) Free Radic Biol Med , vol.38 , pp. 665-677
    • Bota, D.A.1    Ngo, J.K.2    Davies, K.J.3
  • 8
    • 23944474593 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover, A. (2005) Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ 12: 1178-1190.
    • (2005) Cell Death Differ , vol.12 , pp. 1178-1190
    • Ciechanover, A.1
  • 10
    • 43949134849 scopus 로고    scopus 로고
    • Apicoplast translation, transcription and genome replication: targets for antimalarial antibiotics
    • Dahl, E.L., and Rosenthal, P.J. (2008) Apicoplast translation, transcription and genome replication: targets for antimalarial antibiotics. Trends Parasitol 24: 279-284.
    • (2008) Trends Parasitol , vol.24 , pp. 279-284
    • Dahl, E.L.1    Rosenthal, P.J.2
  • 12
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self compartmentalizing proteases in prokaryotes
    • De Mot, R., Nagy, I., Walz, J., and Baumeister, W. (1999) Proteasomes and other self compartmentalizing proteases in prokaryotes. Trends Microbiol 7: 88-92.
    • (1999) Trends Microbiol , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 13
    • 76449122381 scopus 로고    scopus 로고
    • Functional diversification between two related Plasmodium falciparum merozoite invasion ligands is determined by changes in the cytoplasmic domain
    • Dvorin, J.D., Bei, A.K., Coleman, B.I., and Duraisingh, M.T. (2010) Functional diversification between two related Plasmodium falciparum merozoite invasion ligands is determined by changes in the cytoplasmic domain. Mol Microbiol 75: 990-1006.
    • (2010) Mol Microbiol , vol.75 , pp. 990-1006
    • Dvorin, J.D.1    Bei, A.K.2    Coleman, B.I.3    Duraisingh, M.T.4
  • 14
    • 0026538116 scopus 로고
    • The 6-kb element of Plasmodium falciparum encodes mitochondrial cytochrome genes
    • Feagin, J.E. (1992) The 6-kb element of Plasmodium falciparum encodes mitochondrial cytochrome genes. Mol Biochem Parasitol 52: 145.
    • (1992) Mol Biochem Parasitol , vol.52 , pp. 145
    • Feagin, J.E.1
  • 15
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J.M., Neher, S.B., Kim, Y.I., Sauer, R.T., and Baker, T.A. (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell 11: 671-683.
    • (2003) Mol Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 16
    • 0038236437 scopus 로고    scopus 로고
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
    • Frees, D., Qazi, S.N., Hill, P.J., and Ingmer, H. (2003) Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence. Mol Microbiol 48: 1565-1578.
    • (2003) Mol Microbiol , vol.48 , pp. 1565-1578
    • Frees, D.1    Qazi, S.N.2    Hill, P.J.3    Ingmer, H.4
  • 17
    • 33847266418 scopus 로고    scopus 로고
    • The effects of anti-bacterials on the malaria parasite Plasmodium falciparum
    • Goodman, C.D., Su, V., and McFadden, G.I. (2007) The effects of anti-bacterials on the malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 152: 181-191.
    • (2007) Mol Biochem Parasitol , vol.152 , pp. 181-191
    • Goodman, C.D.1    Su, V.2    McFadden, G.I.3
  • 20
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli
    • Kanemori, M., Nishihara, K., Yanagi, H., and Yura, T. (1997) Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J Bacteriol 179: 7219-7225.
    • (1997) J Bacteriol , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 21
    • 62649150175 scopus 로고    scopus 로고
    • A multifunctional serine protease primes the malaria parasite for red blood cell invasion
    • Koussis, K., Withers-Martinez, C., Yeoh, S., Child, M., Hackett, F., Knuepfer, E., etal. (2009) A multifunctional serine protease primes the malaria parasite for red blood cell invasion. EMBO J 28: 725-735.
    • (2009) EMBO J , vol.28 , pp. 725-735
    • Koussis, K.1    Withers-Martinez, C.2    Yeoh, S.3    Child, M.4    Hackett, F.5    Knuepfer, E.6
  • 22
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stage in culture
    • Lambros, C., and Vanderberg, J.P. (1979) Synchronization of Plasmodium falciparum erythrocytic stage in culture. J Parasitol 65: 418-420.
    • (1979) J Parasitol , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 23
    • 43049091926 scopus 로고    scopus 로고
    • Identification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication
    • Li, Z., Lindsay, M.E., Motyka, S.A., Englund, P.T., and Wang, C.C. (2008) Identification of a bacterial-like HslVU protease in the mitochondria of Trypanosoma brucei and its role in mitochondrial DNA replication. PLoS Pathog 4: e1000048.
    • (2008) PLoS Pathog , vol.4
    • Li, Z.1    Lindsay, M.E.2    Motyka, S.A.3    Englund, P.T.4    Wang, C.C.5
  • 24
    • 84872271398 scopus 로고    scopus 로고
    • Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA(+) Lon protease
    • Lu, B., Lee, J., Nie, X., Li, M., Morozov, Y.I., Venkatesh, S., etal. (2013) Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA(+) Lon protease. Mol Cell 49: 121-132.
    • (2013) Mol Cell , vol.49 , pp. 121-132
    • Lu, B.1    Lee, J.2    Nie, X.3    Li, M.4    Morozov, Y.I.5    Venkatesh, S.6
  • 25
    • 33748300551 scopus 로고    scopus 로고
    • Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination
    • Maier, A.G., Braks, J.A., Waters, A.P., and Cowman, A.F. (2006) Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination. Mol Biochem Parasitol 150: 118-121.
    • (2006) Mol Biochem Parasitol , vol.150 , pp. 118-121
    • Maier, A.G.1    Braks, J.A.2    Waters, A.P.3    Cowman, A.F.4
  • 26
    • 33845968856 scopus 로고    scopus 로고
    • Mitochondrial drug targets in apicomplexan parasites
    • Mather, M.W., Henry, K.W., and Vaidya, A.B. (2007) Mitochondrial drug targets in apicomplexan parasites. Curr Drug Targets 8: 49-60.
    • (2007) Curr Drug Targets , vol.8 , pp. 49-60
    • Mather, M.W.1    Henry, K.W.2    Vaidya, A.B.3
  • 28
    • 71249149462 scopus 로고    scopus 로고
    • Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors
    • Moura, P.A., Dame, J.B., and Fidock, D.A. (2009) Role of Plasmodium falciparum digestive vacuole plasmepsins in the specificity and antimalarial mode of action of cysteine and aspartic protease inhibitors. Antimicrob Agents Chemother 53: 4968-4978.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 4968-4978
    • Moura, P.A.1    Dame, J.B.2    Fidock, D.A.3
  • 29
    • 33847300136 scopus 로고    scopus 로고
    • Characterization and localization of Plasmodium falciparum homolog of prokaryotic ClpQ/HslV protease
    • Ramasamy, G., Gupta, D., Mohmmed, A., and Chauhan, V.S. (2007) Characterization and localization of Plasmodium falciparum homolog of prokaryotic ClpQ/HslV protease. Mol Biochem Parasitol 152: 139-148.
    • (2007) Mol Biochem Parasitol , vol.152 , pp. 139-148
    • Ramasamy, G.1    Gupta, D.2    Mohmmed, A.3    Chauhan, V.S.4
  • 30
    • 77955386462 scopus 로고    scopus 로고
    • A cyanobacterial serine protease of Plasmodium falciparum is targeted to the apicoplast and plays important role in its growth and development
    • Rathore, S., Sinha, D., Asad, M., Böttcher, T., Afreen, F., Chauhan, V.S., etal. (2010) A cyanobacterial serine protease of Plasmodium falciparum is targeted to the apicoplast and plays important role in its growth and development. Mol Microbiol 77: 873-890.
    • (2010) Mol Microbiol , vol.77 , pp. 873-890
    • Rathore, S.1    Sinha, D.2    Asad, M.3    Böttcher, T.4    Afreen, F.5    Chauhan, V.S.6
  • 31
    • 83155182430 scopus 로고    scopus 로고
    • Disruption of a mitochondrial protease machinery in Plasmodium falciparum is an intrinsic signal for parasite cell death
    • Rathore, S., Jain, S., Sinha, D., Gupta, M., Asad, M., Srivastava, A., etal. (2011) Disruption of a mitochondrial protease machinery in Plasmodium falciparum is an intrinsic signal for parasite cell death. Cell Death Dis 2: e231.
    • (2011) Cell Death Dis , vol.2
    • Rathore, S.1    Jain, S.2    Sinha, D.3    Gupta, M.4    Asad, M.5    Srivastava, A.6
  • 32
    • 0035986688 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites: targets for chemotherapy
    • Rosenthal, P.J., Sijwali, P.S., Singh, A., and Shenai, B.R. (2002) Cysteine proteases of malaria parasites: targets for chemotherapy. Curr Pharm Des 8: 1659-1672.
    • (2002) Curr Pharm Des , vol.8 , pp. 1659-1672
    • Rosenthal, P.J.1    Sijwali, P.S.2    Singh, A.3    Shenai, B.R.4
  • 33
    • 60849106255 scopus 로고    scopus 로고
    • A calpain unique to alveolates is essential in Plasmodium falciparum and its knockdown reveals an involvement in pre-S-phase development
    • Russo, I., Oksman, A., Vaupel, B., and Goldberg, D.E. (2009) A calpain unique to alveolates is essential in Plasmodium falciparum and its knockdown reveals an involvement in pre-S-phase development. Proc Natl Acad Sci USA 106: 1554-1559.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1554-1559
    • Russo, I.1    Oksman, A.2    Vaupel, B.3    Goldberg, D.E.4
  • 34
    • 36749000794 scopus 로고    scopus 로고
    • Malaria chemotherapeutics part I: history of antimalarial drug development, currently used therapeutics, and drugs in clinical development
    • Schlitzer, M. (2007) Malaria chemotherapeutics part I: history of antimalarial drug development, currently used therapeutics, and drugs in clinical development. ChemMedChem 2: 944-986.
    • (2007) ChemMedChem , vol.2 , pp. 944-986
    • Schlitzer, M.1
  • 35
    • 0034698280 scopus 로고    scopus 로고
    • The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli
    • Seong, I.S., Oh, J.Y., Lee, J.W., Tanaka, K., and Chung, C.H. (2000) The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli. FEBS Lett 477: 224-229.
    • (2000) FEBS Lett , vol.477 , pp. 224-229
    • Seong, I.S.1    Oh, J.Y.2    Lee, J.W.3    Tanaka, K.4    Chung, C.H.5
  • 36
    • 0034666133 scopus 로고    scopus 로고
    • Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum
    • Shenai, B.R., Sijwali, P.S., Singh, A., and Rosenthal, P.J. (2000) Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum. J Biol Chem 275: 29000-29010.
    • (2000) J Biol Chem , vol.275 , pp. 29000-29010
    • Shenai, B.R.1    Sijwali, P.S.2    Singh, A.3    Rosenthal, P.J.4
  • 37
    • 15044338866 scopus 로고    scopus 로고
    • The global distribution of clinical episodes of Plasmodium falciparum malaria
    • Snow, R.W., Guerra, C.A., Noor, A.M., Myint, H.Y., and Hay, S.I. (2005) The global distribution of clinical episodes of Plasmodium falciparum malaria. Nature 434: 214-217.
    • (2005) Nature , vol.434 , pp. 214-217
    • Snow, R.W.1    Guerra, C.A.2    Noor, A.M.3    Myint, H.Y.4    Hay, S.I.5
  • 38
    • 0025224122 scopus 로고
    • Complex transcription from the extrachromosomal DNA encoding mitochondrial functions of Plasmodium yoelii
    • Suplick, K., Morrisey, J., and Vaidya, A.B. (1990) Complex transcription from the extrachromosomal DNA encoding mitochondrial functions of Plasmodium yoelii. Mol Cell Biol 10: 6381-6388.
    • (1990) Mol Cell Biol , vol.10 , pp. 6381-6388
    • Suplick, K.1    Morrisey, J.2    Vaidya, A.B.3
  • 39
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W., and Jensen, J.B. (1976) Human malaria parasites in continuous culture. Science 193: 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 40
    • 77957752190 scopus 로고    scopus 로고
    • Mitochondrial localization of the threonine peptidase PfHslV, a ClpQ ortholog in Plasmodium falciparum
    • Tschan, S., Kreidenweiss, A., Stierhof, Y.D., Sessler, N., Fendel, R., and Mordmüller, B. (2010) Mitochondrial localization of the threonine peptidase PfHslV, a ClpQ ortholog in Plasmodium falciparum. Int J Parasitol 40: 1517-1523.
    • (2010) Int J Parasitol , vol.40 , pp. 1517-1523
    • Tschan, S.1    Kreidenweiss, A.2    Stierhof, Y.D.3    Sessler, N.4    Fendel, R.5    Mordmüller, B.6
  • 41
    • 0035164972 scopus 로고    scopus 로고
    • Roles of the two ClpC ATP binding sites in the regulation of competence and the stress response
    • Turgay, K., Persuh, M., Hahn, J., and Dubnau, D. (2001) Roles of the two ClpC ATP binding sites in the regulation of competence and the stress response. Mol Microbiol 42: 717-727.
    • (2001) Mol Microbiol , vol.42 , pp. 717-727
    • Turgay, K.1    Persuh, M.2    Hahn, J.3    Dubnau, D.4
  • 42
    • 70349536103 scopus 로고    scopus 로고
    • Mitochondrial evolution and functions in malaria parasites
    • Vaidya, A.B., and Mather, M.W. (2009) Mitochondrial evolution and functions in malaria parasites. Annu Rev Microbiol 63: 249-267.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 249-267
    • Vaidya, A.B.1    Mather, M.W.2
  • 43
    • 9444266430 scopus 로고    scopus 로고
    • The apicoplast: a review of the derived plastid of apicomplexan parasites
    • Waller, R.F., and McFadden, G.I. (2005) The apicoplast: a review of the derived plastid of apicomplexan parasites. Curr Issues Mol Biol 7: 57-79.
    • (2005) Curr Issues Mol Biol , vol.7 , pp. 57-79
    • Waller, R.F.1    McFadden, G.I.2
  • 44
    • 45849099498 scopus 로고    scopus 로고
    • Identification and characterization of a novel Plasmodium falciparum merozoite apical protein involved in erythrocyte binding and invasion
    • Wickramarachchi, T., Devi, Y.S., Mohmmed, A., and Chauhan, V.S. (2008) Identification and characterization of a novel Plasmodium falciparum merozoite apical protein involved in erythrocyte binding and invasion. PLoS ONE 3: e1732.
    • (2008) PLoS ONE , vol.3
    • Wickramarachchi, T.1    Devi, Y.S.2    Mohmmed, A.3    Chauhan, V.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.