메뉴 건너뛰기




Volumn 64, Issue 5, 2007, Pages 1154-1163

A functionally divergent hydrogenosomal peptidase with protomitochondrial ancestry

Author keywords

[No Author keywords available]

Indexed keywords

HETERODIMER; MATRIX METALLOPROTEINASE; MITOCHONDRIAL ENZYME; PEPTIDASE; PROTOZOAL PROTEIN;

EID: 34249820287     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05719.x     Document Type: Article
Times cited : (26)

References (51)
  • 2
    • 33747178174 scopus 로고    scopus 로고
    • A common genetic system for functional studies of pitrilysin and related M16A proteases
    • Alper, B.J., Nienow, T.E. Schmidt, W.K. (2006) A common genetic system for functional studies of pitrilysin and related M16A proteases. Biochem J 398: 145 152.
    • (2006) Biochem J , vol.398 , pp. 145-152
    • Alper, B.J.1    Nienow, T.E.2    Schmidt, W.K.3
  • 3
    • 21144441817 scopus 로고    scopus 로고
    • Lateral gene transfer in eukaryotes
    • Andersson, J.O. (2005) Lateral gene transfer in eukaryotes. Cell Mol Life Sci 62: 1182 1197.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1182-1197
    • Andersson, J.O.1
  • 6
    • 0031010331 scopus 로고    scopus 로고
    • Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: Similarities with mitochondrial protein import
    • Bradley, P.J., Lahti, C.J., Plumper, E. Johnson, P.J. (1997) Targeting and translocation of proteins into the hydrogenosome of the protist Trichomonas: similarities with mitochondrial protein import. EMBO J 16: 3484 3493.
    • (1997) EMBO J , vol.16 , pp. 3484-3493
    • Bradley, P.J.1    Lahti, C.J.2    Plumper, E.3    Johnson, P.J.4
  • 7
    • 33846840372 scopus 로고    scopus 로고
    • Protein targeting in parasites with cryptic mitochondria
    • doi:10.1016/j.ijpara.2006.1012.1004.
    • Burri, L. Keeling, P.J. (2007) Protein targeting in parasites with cryptic mitochondria. International J Parasitol 37: 265 272. doi:10.1016/j.ijpara.2006.1012.1004.
    • (2007) International J Parasitol , vol.37 , pp. 265-272
    • Burri, L.1    Keeling, P.J.2
  • 8
    • 33750436226 scopus 로고    scopus 로고
    • Microsporidian mitosomes retain elements of the general mitochondrial targeting system
    • Burri, L., Williams, B.A., Bursac, D., Lithgow, T. Keeling, P.J. (2006) Microsporidian mitosomes retain elements of the general mitochondrial targeting system. Proc Natl Acad Sci USA 103: 15916 15920.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 15916-15920
    • Burri, L.1    Williams, B.A.2    Bursac, D.3    Lithgow, T.4    Keeling, P.J.5
  • 9
    • 33846528971 scopus 로고    scopus 로고
    • Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis
    • Carlton, J.M., Hirt, R.P., Silva, J.C., Delcher, A.L., Schatz, M., Zhao, Q., et al. (2007) Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis. Science 315: 207 212.
    • (2007) Science , vol.315 , pp. 207-212
    • Carlton, J.M.1    Hirt, R.P.2    Silva, J.C.3    Delcher, A.L.4    Schatz, M.5    Zhao, Q.6
  • 10
    • 23344449206 scopus 로고    scopus 로고
    • Giardia mitosomes and trichomonad hydrogenosomes share a common mode of protein targeting
    • Dolezal, P., Smid, O., Rada, P., Zubacova, Z., Bursac, D., Sutak, R., et al. (2005) Giardia mitosomes and trichomonad hydrogenosomes share a common mode of protein targeting. Proc Natl Acad Sci USA 102: 10924 10929.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10924-10929
    • Dolezal, P.1    Smid, O.2    Rada, P.3    Zubacova, Z.4    Bursac, D.5    Sutak, R.6
  • 11
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, P., Likic, V., Tachezy, J. Lithgow, T. (2006) Evolution of the molecular machines for protein import into mitochondria. Science 313: 314 318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 12
    • 0034023895 scopus 로고    scopus 로고
    • Presence of a member of the mitochondrial carrier family in hydrogenosomes: Conservation of membrane-targeting pathways between hydrogenosomes and mitochondria
    • Dyall, S.D., Koehler, C.M., Delgadillo-Correa, M.G., Bradley, P.J., Plumper, E., Leuenberger, D., et al. (2000) Presence of a member of the mitochondrial carrier family in hydrogenosomes: conservation of membrane-targeting pathways between hydrogenosomes and mitochondria. Mol Cell Biol 20: 2488 2497.
    • (2000) Mol Cell Biol , vol.20 , pp. 2488-2497
    • Dyall, S.D.1    Koehler, C.M.2    Delgadillo-Correa, M.G.3    Bradley, P.J.4    Plumper, E.5    Leuenberger, D.6
  • 13
    • 1842429937 scopus 로고    scopus 로고
    • Ancient invasions: From endosymbionts to organelles
    • Dyall, S.D., Brown, M.T. Johnson, P.J. (2004a) Ancient invasions: from endosymbionts to organelles. Science 304: 253 257.
    • (2004) Science , vol.304 , pp. 253-257
    • Dyall, S.D.1    Brown, M.T.2    Johnson, P.J.3
  • 15
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R.C. (2004) MUSCLE: a multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 16
    • 33747810433 scopus 로고    scopus 로고
    • Multiple secondary origins of the anaerobic lifestyle in eukaryotes
    • Embley, T.M. (2006) Multiple secondary origins of the anaerobic lifestyle in eukaryotes. Philos Trans R Soc Lond B Biol Sci 361: 1055 1067.
    • (2006) Philos Trans R Soc Lond B Biol Sci , vol.361 , pp. 1055-1067
    • Embley, T.M.1
  • 17
    • 33645456207 scopus 로고    scopus 로고
    • Eukaryotic evolution, changes and challenges
    • Embley, T.M. Martin, W. (2006) Eukaryotic evolution, changes and challenges. Nature 440: 623 630.
    • (2006) Nature , vol.440 , pp. 623-630
    • Embley, T.M.1    Martin, W.2
  • 20
    • 0032738979 scopus 로고    scopus 로고
    • Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants
    • Glaser, E. Dessi, P. (1999) Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants. J Bioenerg Biomembr 31: 259 274.
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 259-274
    • Glaser, E.1    Dessi, P.2
  • 21
    • 0032511986 scopus 로고    scopus 로고
    • Rickettsia, typhus and the mitochondrial connection
    • Gray, M.W. (1998) Rickettsia, typhus and the mitochondrial connection. Nature 396: 109 110.
    • (1998) Nature , vol.396 , pp. 109-110
    • Gray, M.W.1
  • 22
    • 14544269861 scopus 로고    scopus 로고
    • Evolutionary biology: The hydrogenosome's murky past
    • Gray, M.W. (2005) Evolutionary biology: the hydrogenosome's murky past. Nature 434: 29 31.
    • (2005) Nature , vol.434 , pp. 29-31
    • Gray, M.W.1
  • 23
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray, M.W., Burger, G. Lang, B.F. (1999) Mitochondrial evolution. Science 283: 1476 1481.
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 24
    • 33747887707 scopus 로고    scopus 로고
    • Mitochondria, hydrogenosomes and mitosomes: Products of evolutionary tinkering!
    • Hackstein, J.H., Tjaden, J. Huynen, M. (2006) Mitochondria, hydrogenosomes and mitosomes: products of evolutionary tinkering!. Curr Genet 50: 225 245.
    • (2006) Curr Genet , vol.50 , pp. 225-245
    • Hackstein, J.H.1    Tjaden, J.2    Huynen, M.3
  • 25
    • 0642342084 scopus 로고    scopus 로고
    • Evolutionary biology: Essence of mitochondria
    • Henze, K. Martin, W. (2003) Evolutionary biology: essence of mitochondria. Nature 426: 127 128.
    • (2003) Nature , vol.426 , pp. 127-128
    • Henze, K.1    Martin, W.2
  • 26
    • 10344254308 scopus 로고    scopus 로고
    • Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I
    • Hrdy, I., Hirt, R.P., Dolezal, P., Bardonova, L., Foster, P.G., Tachezy, J. Embley, T.M. (2004) Trichomonas hydrogenosomes contain the NADH dehydrogenase module of mitochondrial complex I. Nature 432: 618 622.
    • (2004) Nature , vol.432 , pp. 618-622
    • Hrdy, I.1    Hirt, R.P.2    Dolezal, P.3    Bardonova, L.4    Foster, P.G.5    Tachezy, J.6    Embley, T.M.7
  • 28
    • 0037449819 scopus 로고    scopus 로고
    • Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity
    • Kitada, S., Yamasaki, E., Kojima, K. Ito, A. (2003) Determination of the cleavage site of the presequence by mitochondrial processing peptidase on the substrate binding scaffold and the multiple subsites inside a molecular cavity. J Biol Chem 278: 1879 1885.
    • (2003) J Biol Chem , vol.278 , pp. 1879-1885
    • Kitada, S.1    Yamasaki, E.2    Kojima, K.3    Ito, A.4
  • 29
    • 33846625139 scopus 로고    scopus 로고
    • A protein from a parasitic microorganism, rickettsia prowazekii, can cleave the signal sequences of proteins targeting mitochondria
    • Kitada, S., Uchiyama, T., Funatsu, T., Kitada, Y., Ogishima, T. Ito, A. (2007) A protein from a parasitic microorganism, rickettsia prowazekii, can cleave the signal sequences of proteins targeting mitochondria. J Bacteriol 189: 844 850.
    • (2007) J Bacteriol , vol.189 , pp. 844-850
    • Kitada, S.1    Uchiyama, T.2    Funatsu, T.3    Kitada, Y.4    Ogishima, T.5    Ito, A.6
  • 30
    • 0028132843 scopus 로고
    • Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships
    • Lange, S., Rozario, C. Muller, M. (1994) Primary structure of the hydrogenosomal adenylate kinase of Trichomonas vaginalis and its phylogenetic relationships. Mol Biochem Parasitol 66: 297 308.
    • (1994) Mol Biochem Parasitol , vol.66 , pp. 297-308
    • Lange, S.1    Rozario, C.2    Muller, M.3
  • 31
    • 20044392656 scopus 로고    scopus 로고
    • Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20
    • Likic, V.A., Perry, A., Hulett, J., Derby, M., Traven, A., Waller, R.F., et al. (2005) Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20. J Mol Biol 347: 81 93.
    • (2005) J Mol Biol , vol.347 , pp. 81-93
    • Likic, V.A.1    Perry, A.2    Hulett, J.3    Derby, M.4    Traven, A.5    Waller, R.F.6
  • 32
    • 0030871088 scopus 로고    scopus 로고
    • Functional cooperation of the mitochondrial processing peptidase subunits
    • Luciano, P., Geoffroy, S., Brandt, A., Hernandez, J.F. Geli, V. (1997) Functional cooperation of the mitochondrial processing peptidase subunits. J Mol Biol 272: 213 225.
    • (1997) J Mol Biol , vol.272 , pp. 213-225
    • Luciano, P.1    Geoffroy, S.2    Brandt, A.3    Hernandez, J.F.4    Geli, V.5
  • 33
    • 0032504096 scopus 로고    scopus 로고
    • The mitochondrial processing peptidase behaves as a zinc-metallopeptidase
    • Luciano, P., Tokatlidis, K., Chambre, I., Germanique, J.C. Geli, V. (1998) The mitochondrial processing peptidase behaves as a zinc- metallopeptidase. J Mol Biol 280: 193 199.
    • (1998) J Mol Biol , vol.280 , pp. 193-199
    • Luciano, P.1    Tokatlidis, K.2    Chambre, I.3    Germanique, J.C.4    Geli, V.5
  • 34
    • 24944591095 scopus 로고    scopus 로고
    • The missing link between hydrogenosomes and mitochondria
    • Martin, W. (2005) The missing link between hydrogenosomes and mitochondria. Trends Microbiol 13: 457 459.
    • (2005) Trends Microbiol , vol.13 , pp. 457-459
    • Martin, W.1
  • 35
    • 4544228401 scopus 로고    scopus 로고
    • Evolutionary biology: Early evolution comes full circle
    • Martin, W. Embley, T.M. (2004) Evolutionary biology: early evolution comes full circle. Nature 431: 134 137.
    • (2004) Nature , vol.431 , pp. 134-137
    • Martin, W.1    Embley, T.M.2
  • 36
    • 33845677739 scopus 로고    scopus 로고
    • Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis
    • Mukherjee, M., Brown, M.T., McArthur, A.G. Johnson, P.J. (2006) Proteins of the glycine decarboxylase complex in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell 5: 2062 2071.
    • (2006) Eukaryot Cell , vol.5 , pp. 2062-2071
    • Mukherjee, M.1    Brown, M.T.2    McArthur, A.G.3    Johnson, P.J.4
  • 37
    • 0027787578 scopus 로고
    • The hydrogenosome
    • Muller, M. (1993) The hydrogenosome. J Gen Microbiol 139: 2879 2889.
    • (1993) J Gen Microbiol , vol.139 , pp. 2879-2889
    • Muller, M.1
  • 38
    • 0034602332 scopus 로고    scopus 로고
    • Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteins
    • Nagao, Y., Kitada, S., Kojima, K., Toh, H., Kuhara, S., Ogishima, T. Ito, A. (2000) Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteins. J Biol Chem 275: 34552 34556.
    • (2000) J Biol Chem , vol.275 , pp. 34552-34556
    • Nagao, Y.1    Kitada, S.2    Kojima, K.3    Toh, H.4    Kuhara, S.5    Ogishima, T.6    Ito, A.7
  • 39
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou, W.J., Ito, A., Okazaki, H. Omura, T. (1989) Purification and characterization of a processing protease from rat liver mitochondria. EMBO J 8: 2605 2612.
    • (1989) EMBO J , vol.8 , pp. 2605-2612
    • Ou, W.J.1    Ito, A.2    Okazaki, H.3    Omura, T.4
  • 41
    • 0024119655 scopus 로고
    • The processing peptidase of yeast mitochondria: The two co-operating components MPP and PEP are structurally related
    • Pollock, R.A., Hartl, F.U., Cheng, M.Y., Ostermann, J., Horwich, A. Neupert, W. (1988) The processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related. EMBO J 7: 3493 3500.
    • (1988) EMBO J , vol.7 , pp. 3493-3500
    • Pollock, R.A.1    Hartl, F.U.2    Cheng, M.Y.3    Ostermann, J.4    Horwich, A.5    Neupert, W.6
  • 43
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist, F. Huelsenbeck, J.P. (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572 1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 44
    • 0345690206 scopus 로고    scopus 로고
    • Structural basis of core promoter recognition in a primitive eukaryote
    • Schumacher, M.A., Lau, A.O. Johnson, P.J. (2003) Structural basis of core promoter recognition in a primitive eukaryote. Cell 115: 413 424.
    • (2003) Cell , vol.115 , pp. 413-424
    • Schumacher, M.A.1    Lau, A.O.2    Johnson, P.J.3
  • 45
    • 3142746681 scopus 로고    scopus 로고
    • Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis
    • Sutak, R., Dolezal, P., Fiumera, H.L., Hrdy, I., Dancis, A., Delgadillo-Correa, M., et al. (2004) Mitochondrial-type assembly of FeS centers in the hydrogenosomes of the amitochondriate eukaryote Trichomonas vaginalis. Proc Natl Acad Sci USA 101: 10368 10373.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10368-10373
    • Sutak, R.1    Dolezal, P.2    Fiumera, H.L.3    Hrdy, I.4    Dancis, A.5    Delgadillo-Correa, M.6
  • 46
    • 0034940401 scopus 로고    scopus 로고
    • Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
    • Taylor, A.B., Smith, B.S., Kitada, S., Kojima, K., Miyaura, H., Otwinowski, Z., et al. (2001) Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Structure (Camb) 9: 615 625.
    • (2001) Structure (Camb) , vol.9 , pp. 615-625
    • Taylor, A.B.1    Smith, B.S.2    Kitada, S.3    Kojima, K.4    Miyaura, H.5    Otwinowski, Z.6
  • 48
    • 0032988857 scopus 로고    scopus 로고
    • The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica
    • Tovar, J., Fischer, A. Clark, C.G. (1999) The mitosome, a novel organelle related to mitochondria in the amitochondrial parasite Entamoeba histolytica. Mol Microbiol 32: 1013 1021.
    • (1999) Mol Microbiol , vol.32 , pp. 1013-1021
    • Tovar, J.1    Fischer, A.2    Clark, C.G.3
  • 49
    • 0344633597 scopus 로고    scopus 로고
    • Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation
    • Tovar, J., Leon-Avila, G., Sanchez, L.B., Sutak, R., Tachezy, J., van der Giezen, M., et al. (2003) Mitochondrial remnant organelles of Giardia function in iron-sulphur protein maturation. Nature 426: 172 176.
    • (2003) Nature , vol.426 , pp. 172-176
    • Tovar, J.1    Leon-Avila, G.2    Sanchez, L.B.3    Sutak, R.4    Tachezy, J.5    Van Der Giezen, M.6
  • 50
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • Wiedemann, N., Frazier, A.E. Pfanner, N. (2004) The protein import machinery of mitochondria. J Biol Chem 279: 14473 14476.
    • (2004) J Biol Chem , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 51
    • 0037158721 scopus 로고    scopus 로고
    • A mitochondrial remnant in the microsporidian Trachipleistophora hominis
    • Williams, B.A., Hirt, R.P., Lucocq, J.M. Embley, T.M. (2002) A mitochondrial remnant in the microsporidian Trachipleistophora hominis. Nature 418: 865 869.
    • (2002) Nature , vol.418 , pp. 865-869
    • Williams, B.A.1    Hirt, R.P.2    Lucocq, J.M.3    Embley, T.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.