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Volumn 65, Issue 6, 2007, Pages 1559-1567

Alternative trans-splicing of the Trypanosoma cruzi LYT1 gene transcript results in compartmental and functional switch for the encoded protein

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[No Author keywords available]

Indexed keywords

PROTOZOAL PROTEIN;

EID: 34548317153     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05892.x     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 0035858881 scopus 로고    scopus 로고
    • Intramitochondrial localization of universal minicircle sequence-binding protein, a trypanosomatid protein that binds kinetoplast minicircle replication origins
    • Abu-Elneel, K., Robinson, D.R., Drew, M.E., Englund, P.T. Shlomai, J. (2001) Intramitochondrial localization of universal minicircle sequence-binding protein, a trypanosomatid protein that binds kinetoplast minicircle replication origins. J Cell Biol 14 : 725 734.
    • (2001) J Cell Biol , vol.14 , pp. 725-734
    • Abu-Elneel, K.1    Robinson, D.R.2    Drew, M.E.3    Englund, P.T.4    Shlomai, J.5
  • 2
    • 8644238313 scopus 로고    scopus 로고
    • Lysosomal fusion is essential for the retention of Trypanosoma cruzi inside host cells
    • Andrade, L.O. Andrews, N.W. (2004) Lysosomal fusion is essential for the retention of Trypanosoma cruzi inside host cells. J Exp Med 200 : 1135 1143.
    • (2004) J Exp Med , vol.200 , pp. 1135-1143
    • Andrade, L.O.1    Andrews, N.W.2
  • 3
    • 27244448634 scopus 로고    scopus 로고
    • The Trypanosoma cruzi-host-cell interplay: Location, invasion, retention
    • Andrade, L.O. Andrews, N.W. (2005) The Trypanosoma cruzi-host-cell interplay: location, invasion, retention. Nat Rev Microbiol 3 : 819 823.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 819-823
    • Andrade, L.O.1    Andrews, N.W.2
  • 4
    • 0024583847 scopus 로고
    • Secretion by Trypanosoma cruzi of a hemolysin active at low pH
    • Andrews, N.W. Whitlow, M.B. (1989) Secretion by Trypanosoma cruzi of a hemolysin active at low pH. Mol Biochem Parasitol 15 : 249 256.
    • (1989) Mol Biochem Parasitol , vol.15 , pp. 249-256
    • Andrews, N.W.1    Whitlow, M.B.2
  • 5
    • 0025277577 scopus 로고
    • A T. cruzi-secreted protein immunologically related to the complement component C9: Evidence for membrane pore-forming activity at low pH
    • Andrews, N.W., Abrams, C.K., Slatin, S.L. Griffiths, G. (1990) A T. cruzi-secreted protein immunologically related to the complement component C9: evidence for membrane pore-forming activity at low pH. Cell 61 : 1277 1287.
    • (1990) Cell , vol.61 , pp. 1277-1287
    • Andrews, N.W.1    Abrams, C.K.2    Slatin, S.L.3    Griffiths, G.4
  • 7
    • 0015869325 scopus 로고
    • Biology of Trypanosoma cruzi
    • Brener, Z. (1973) Biology of Trypanosoma cruzi. Annu Rev Microbiol 27 : 347 382.
    • (1973) Annu Rev Microbiol , vol.27 , pp. 347-382
    • Brener, Z.1
  • 8
    • 0028866134 scopus 로고
    • The mechanisms of Trypanosoma cruzi invasion of mammalian cells
    • Burleigh, B.A. Andrews, N.W. (1995) The mechanisms of Trypanosoma cruzi invasion of mammalian cells. Annu Rev Microbiol 49 : 175 200.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 175-200
    • Burleigh, B.A.1    Andrews, N.W.2
  • 9
    • 0036855862 scopus 로고    scopus 로고
    • Cell signalling and Trypanosoma cruzi invasion
    • Burleigh, B.A. Woolsey, A.M. (2002) Cell signalling and Trypanosoma cruzi invasion. Cell Microbiol 4 : 701 711.
    • (2002) Cell Microbiol , vol.4 , pp. 701-711
    • Burleigh, B.A.1    Woolsey, A.M.2
  • 10
    • 0038521140 scopus 로고    scopus 로고
    • Biochemical characterization of proline racemases from the human protozoan parasite Trypanosoma cruzi and definition of putative protein signatures
    • Chamond, N., Gregoire, C., Coatnoan, N., Rougeot, C., Freitas-Junrio, L.H., da Silveira, J.F., et al. (2003) Biochemical characterization of proline racemases from the human protozoan parasite Trypanosoma cruzi and definition of putative protein signatures. J Biol Chem 278 : 15484 15494.
    • (2003) J Biol Chem , vol.278 , pp. 15484-15494
    • Chamond, N.1    Gregoire, C.2    Coatnoan, N.3    Rougeot, C.4    Freitas-Junrio, L.H.5    Da Silveira, J.F.6
  • 11
    • 1442280871 scopus 로고    scopus 로고
    • From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: Dreams and reality
    • De Souza, W. (2002) From the cell biology to the development of new chemotherapeutic approaches against trypanosomatids: dreams and reality. Kinetoplastid Biol Dis 31 : 1 21.
    • (2002) Kinetoplastid Biol Dis , vol.31 , pp. 1-21
    • De Souza, W.1
  • 12
    • 0034602312 scopus 로고    scopus 로고
    • A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity
    • Decatur, A.L. Portnoy, D.A. (2000) A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity. Science 290 : 992 995.
    • (2000) Science , vol.290 , pp. 992-995
    • Decatur, A.L.1    Portnoy, D.A.2
  • 13
    • 0035253755 scopus 로고    scopus 로고
    • The Crithidia fasciculata RNH1 gene encodes both nuclear and mitochondrial isoforms of RNase H
    • Engel, M.L., Hines, J.C. Rays, D.S. (2001) The Crithidia fasciculata RNH1 gene encodes both nuclear and mitochondrial isoforms of RNase H. Nucleic Acids Res 29 : 725 731.
    • (2001) Nucleic Acids Res , vol.29 , pp. 725-731
    • Engel, M.L.1    Hines, J.C.2    Rays, D.S.3
  • 14
    • 0037128936 scopus 로고    scopus 로고
    • The Listeria monocytogenes hemolysis has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells
    • Glomski, I.J., Gedde, M.M., Tsang, A.W., Swanson, J.A. Portnoy, D.A. (2002) The Listeria monocytogenes hemolysis has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells. J Cell Biol 18 : 1029 1038.
    • (2002) J Cell Biol , vol.18 , pp. 1029-1038
    • Glomski, I.J.1    Gedde, M.M.2    Tsang, A.W.3    Swanson, J.A.4    Portnoy, D.A.5
  • 15
  • 16
    • 0026673614 scopus 로고
    • A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania
    • Kelly, J.M., Ward, H.M., Miles, M.A. Kendall, G. (1992) A shuttle vector which facilitates the expression of transfected genes in Trypanosoma cruzi and Leishmania. Nucleic Acids Res 20 : 3963 3969.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3963-3969
    • Kelly, J.M.1    Ward, H.M.2    Miles, M.A.3    Kendall, G.4
  • 17
    • 0025098535 scopus 로고
    • The exit of Trypanosoma cruzi from the phagosome is inhibited by raising the pH of acidic compartments
    • Ley, V., Robbins, E.S., Nussenzweig, V. Andrews, N.W. (1990) The exit of Trypanosoma cruzi from the phagosome is inhibited by raising the pH of acidic compartments. J Exp Med 2 : 401 413.
    • (1990) J Exp Med , vol.2 , pp. 401-413
    • Ley, V.1    Robbins, E.S.2    Nussenzweig, V.3    Andrews, N.W.4
  • 19
    • 0036075814 scopus 로고    scopus 로고
    • Alternative splicing of LYT1 transcripts in Trypanosoma cruzi
    • Manning-Cela, R., González, A. Swindle, J. (2002) Alternative splicing of LYT1 transcripts in Trypanosoma cruzi. Infect Immun 70 : 4726 4728.
    • (2002) Infect Immun , vol.70 , pp. 4726-4728
    • Manning-Cela, R.1    González, A.2    Swindle, J.3
  • 20
    • 0032189258 scopus 로고    scopus 로고
    • Signal sequences: More than just greasy peptides
    • Martoglio, B. Dobberstein, B. (1998) Signal sequences: more than just greasy peptides. Trends Cell Biol 8 : 410 415.
    • (1998) Trends Cell Biol , vol.8 , pp. 410-415
    • Martoglio, B.1    Dobberstein, B.2
  • 22
    • 0028041048 scopus 로고
    • Functional complementation of glycoprotein 72 in a Trypanosoma cruzi glycoprotein 72 null mutant
    • Nozaki, T. Cross, G.A.M. (1994) Functional complementation of glycoprotein 72 in a Trypanosoma cruzi glycoprotein 72 null mutant. Mol Biochem Parasitol 67 : 91 102.
    • (1994) Mol Biochem Parasitol , vol.67 , pp. 91-102
    • Nozaki, T.1    Cross, G.A.M.2
  • 23
    • 33846025784 scopus 로고    scopus 로고
    • Binding of the universal minicircle sequence binding protein at the kinetoplast DNA replication origin
    • Onn, I., Kapeller, I., Abu-Elneel, K. Shlomai, J. (2006) Binding of the universal minicircle sequence binding protein at the kinetoplast DNA replication origin. J Biol Chem 281 : 37468 37476.
    • (2006) J Biol Chem , vol.281 , pp. 37468-37476
    • Onn, I.1    Kapeller, I.2    Abu-Elneel, K.3    Shlomai, J.4
  • 25
    • 33750595935 scopus 로고    scopus 로고
    • Expression of trypomastigote trans-sialidase in metacyclic forms of Trypanosoma cruzi increases parasite escape from its parasitophorous vacuole
    • Rubin-de-Celis, S.S.C., Uemura, H., Yoshida, N. Schenkman, S. (2006) Expression of trypomastigote trans-sialidase in metacyclic forms of Trypanosoma cruzi increases parasite escape from its parasitophorous vacuole. Cell Microbiol 8 : 1888 1898.
    • (2006) Cell Microbiol , vol.8 , pp. 1888-1898
    • Rubin-De-Celis, S.S.C.1    Uemura, H.2    Yoshida, N.3    Schenkman, S.4
  • 27
    • 0344962439 scopus 로고    scopus 로고
    • One ticket for multiple destinations: Dual targeting of proteins to distinct subcellular locations
    • Silva-Filho, M.C. (2003) One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Curr Opinion Plant Biol 6 : 589 595.
    • (2003) Curr Opinion Plant Biol , vol.6 , pp. 589-595
    • Silva-Filho, M.C.1
  • 28
    • 0022507399 scopus 로고
    • The 35-nucleotide spliced leader sequence is common to all trypanosome messenger RNA's
    • Walder, J.A., Eder, P.S., Engman, D.M., Brentano, S.T., Walder, R.Y., Knutzon, D.S., et al. (1986) The 35-nucleotide spliced leader sequence is common to all trypanosome messenger RNA's. Science 233 : 569 571.
    • (1986) Science , vol.233 , pp. 569-571
    • Walder, J.A.1    Eder, P.S.2    Engman, D.M.3    Brentano, S.T.4    Walder, R.Y.5    Knutzon, D.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.