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Volumn 100, Issue 1, 1999, Pages 19-26

Theileria parva 104 kDa microneme-rhoptry protein is membrane-anchored by a non-cleaved amino-terminal signal sequence for entry into the endoplasmic reticulum

Author keywords

Microneme rhoptry biogenesis; Signal anchor sequence; Theileria parva

Indexed keywords

SIGNAL PEPTIDE;

EID: 0033044361     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00020-1     Document Type: Article
Times cited : (8)

References (34)
  • 2
    • 0030221960 scopus 로고    scopus 로고
    • Rhoptry organelles of the apicomplexa: Their role in host cell invasion and intracellular survival
    • Sam-Yellowe T.Y. Rhoptry organelles of the apicomplexa: their role in host cell invasion and intracellular survival. Parasitol. Today. 12(8):1996;308-316.
    • (1996) Parasitol. Today , vol.12 , Issue.8 , pp. 308-316
    • Sam-Yellowe, T.Y.1
  • 3
    • 0003039752 scopus 로고
    • Theileriosis: Antigens and host parasite interactions
    • T.W. Pearson. New York: Marcel Dekker
    • Morrison W.E., Lalor P.A., Goddeeris B.M., Teale A.J. Theileriosis: antigens and host parasite interactions. Pearson T.W. Parasite Antigens. 1986;167-213 Marcel Dekker, New York.
    • (1986) Parasite Antigens , pp. 167-213
    • Morrison, W.E.1    Lalor, P.A.2    Goddeeris, B.M.3    Teale, A.J.4
  • 5
    • 0031017539 scopus 로고    scopus 로고
    • Characterization of a secretory type Theileria parva glutaredoxin homologue identified by novel screening procedure
    • Ebel T., Middleton J.F.S., Frisch A., Lipp J. Characterization of a secretory type Theileria parva glutaredoxin homologue identified by novel screening procedure. J. Biol. Chem. 272:1997;3042-3048.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3042-3048
    • Ebel, T.1    Middleton, J.F.S.2    Frisch, A.3    Lipp, J.4
  • 6
    • 0023681547 scopus 로고
    • Signal and membrane anchor functions overlap in the type II membrane protein I gamma CAT
    • Lipp J., Dobberstein B. Signal and membrane anchor functions overlap in the type II membrane protein I gamma CAT. J. Cell Biol. 106:1988;1813-1820.
    • (1988) J. Cell Biol. , vol.106 , pp. 1813-1820
    • Lipp, J.1    Dobberstein, B.2
  • 7
    • 0021013021 scopus 로고
    • Substrate recognition by oligosaccharyl transferase. Inhibition of co-translational glycosylation by acceptor peptides
    • Lau J.T., Welply J.K., Shenbagamurthi P., Naider F., Lennarz W.J. Substrate recognition by oligosaccharyl transferase. Inhibition of co-translational glycosylation by acceptor peptides. J. Biol. Chem. 258:1983;15255-15260.
    • (1983) J. Biol. Chem. , vol.258 , pp. 15255-15260
    • Lau, J.T.1    Welply, J.K.2    Shenbagamurthi, P.3    Naider, F.4    Lennarz, W.J.5
  • 8
    • 0025350604 scopus 로고
    • In vitro biosynthesis and membrane translocation of the serine rich protein of Plasmodium falciparum
    • Ragge K., Arnold H.H., Tuemmler M., Knapp B., Hundt E., Lingelbach K. In vitro biosynthesis and membrane translocation of the serine rich protein of Plasmodium falciparum. Mol. Biochem. Parasitol. 42:1990;93-100.
    • (1990) Mol. Biochem. Parasitol. , vol.42 , pp. 93-100
    • Ragge, K.1    Arnold, H.H.2    Tuemmler, M.3    Knapp, B.4    Hundt, E.5    Lingelbach, K.6
  • 9
    • 0023057578 scopus 로고
    • The membrane-spanning segment of invariant chain (I gamma) contains a potentially cleavable signal sequence
    • Lipp J., Dobberstein B. The membrane-spanning segment of invariant chain (I gamma) contains a potentially cleavable signal sequence. Cell. 46:1986;1103-1112.
    • (1986) Cell , vol.46 , pp. 1103-1112
    • Lipp, J.1    Dobberstein, B.2
  • 10
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki Y., Hubbard A.L., Fowler S., Lazarow P.B. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:1982;97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 11
    • 0026460954 scopus 로고
    • r Cryptosporidium parvum sporozoite glycoprotein recognized by protective hyperimmune bovine colostral immunoglobulin
    • r Cryptosporidium parvum sporozoite glycoprotein recognized by protective hyperimmune bovine colostral immunoglobulin. Infect. Immun. 60:1992;5132-5138.
    • (1992) Infect. Immun. , vol.60 , pp. 5132-5138
    • Petersen, C.1    Gut, J.2    Doyle, P.S.3    Crabb, J.H.4    Nelson, R.G.5    Leech, J.H.6
  • 13
    • 15844362771 scopus 로고    scopus 로고
    • N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum
    • Kimura E.A., Couto A.S., Peres V.J., Casal O.L., Katzin A.M. N-linked glycoproteins are related to schizogony of the intraerythrocytic stage in Plasmodium falciparum. J. Biol. Chem. 271:1996;14452-14461.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14452-14461
    • Kimura, E.A.1    Couto, A.S.2    Peres, V.J.3    Casal, O.L.4    Katzin, A.M.5
  • 14
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133:1983;17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 16
    • 0022467151 scopus 로고
    • Signal recognition particle-dependent membrane insertion of mouse invariant chain: A membrane-spanning protein with a cytoplasmically exposed amino terminus
    • Lipp J., Dobberstein B. Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminus. J. Cell. Biol. 102:1986;2169-2175.
    • (1986) J. Cell. Biol. , vol.102 , pp. 2169-2175
    • Lipp, J.1    Dobberstein, B.2
  • 17
    • 0021767942 scopus 로고
    • A novel in vitro transcription translation system: Accurate and efficient synthesis of single proteins from cloned DNA sequences
    • Stueber D., Ibrahimi I., Cutler D., Dobberstein B., Bujard H. A novel in vitro transcription translation system: accurate and efficient synthesis of single proteins from cloned DNA sequences. EMBO J. 3:1984;3143-3148.
    • (1984) EMBO J. , vol.3 , pp. 3143-3148
    • Stueber, D.1    Ibrahimi, I.2    Cutler, D.3    Dobberstein, B.4    Bujard, H.5
  • 18
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • von Heijne G. Transcending the impenetrable: how proteins come to terms with membranes. Biochim. Biophys. Acta. 947:1988;307-333.
    • (1988) Biochim. Biophys. Acta , vol.947 , pp. 307-333
    • Von Heijne, G.1
  • 19
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport T.A., Jungnickel B., Kutay U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65:1996;271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 20
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P., Johnson A.E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10:1994;87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 21
    • 0020059828 scopus 로고
    • Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane
    • Blok J., Air G.M., Laver W.G., Ward C.W., Lilley G.G., Woods E.F., Roxburgh C.M., Inglis A.S. Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane. Virology. 119:1982;109-121.
    • (1982) Virology , vol.119 , pp. 109-121
    • Blok, J.1    Air, G.M.2    Laver, W.G.3    Ward, C.W.4    Lilley, G.G.5    Woods, E.F.6    Roxburgh, C.M.7    Inglis, A.S.8
  • 22
    • 0029415127 scopus 로고
    • The secretory pathway of Plasmodium falciparum regulates transport of p82/RAP1 to the rhoptries
    • Howard R.F., Schmidt C.M. The secretory pathway of Plasmodium falciparum regulates transport of p82/RAP1 to the rhoptries. Mol. Biochem. Parasitol. 74:1995;43-54.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 43-54
    • Howard, R.F.1    Schmidt, C.M.2
  • 23
    • 0030222003 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel acidic microneme protein (Etmic-2) from the apicomplexan protozoan parasite, Eimeria tenella
    • Tomley F.M., Bumstead J.M., Billington K.J., Dunn P.P. Molecular cloning and characterization of a novel acidic microneme protein (Etmic-2) from the apicomplexan protozoan parasite, Eimeria tenella. Mol. Biochem. Parasitol. 79:1996;195-206.
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 195-206
    • Tomley, F.M.1    Bumstead, J.M.2    Billington, K.J.3    Dunn, P.P.4
  • 24
    • 0029973716 scopus 로고    scopus 로고
    • In vitro biosynthesis and in vivo processing of the major microneme antigen of Sarcocystis muris cyst merozoites
    • Klein H., Mehlhorn H., Ruger W. In vitro biosynthesis and in vivo processing of the major microneme antigen of Sarcocystis muris cyst merozoites. Parasitol. Res. 82:1996;468-474.
    • (1996) Parasitol. Res. , vol.82 , pp. 468-474
    • Klein, H.1    Mehlhorn, H.2    Ruger, W.3
  • 25
    • 0023218259 scopus 로고
    • Structure of the gene encoding the circumsporozoite protein of Plasmodium yoelii. A rodent model for examining antimalarial sporozoite vaccines
    • Lal A.A., de la Cruz V.F., Welsh J.A., Charoenvit Y., Maloy W.L., McCutchan T.F. Structure of the gene encoding the circumsporozoite protein of Plasmodium yoelii. A rodent model for examining antimalarial sporozoite vaccines. J. Biol. Chem. 262:1987;2937-2940.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2937-2940
    • Lal, A.A.1    De La Cruz, V.F.2    Welsh, J.A.3    Charoenvit, Y.4    Maloy, W.L.5    McCutchan, T.F.6
  • 26
    • 0026762575 scopus 로고
    • Characterization of the gene encoding sporozoite surface protein 2, a protective Plasmodium yoelii sporozoite antigen
    • Rogers W.O., Rogers M.D., Hedstrom R.C., Hoffman S.L. Characterization of the gene encoding sporozoite surface protein 2, a protective Plasmodium yoelii sporozoite antigen. Mol. Biochem. Parasitol. 53:1992;45-51.
    • (1992) Mol. Biochem. Parasitol. , vol.53 , pp. 45-51
    • Rogers, W.O.1    Rogers, M.D.2    Hedstrom, R.C.3    Hoffman, S.L.4
  • 27
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:1986;4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 29
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann E., Rapoport T.A., Lodish H.F. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA. 86:1989;5786-5790.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 30
    • 0030919649 scopus 로고    scopus 로고
    • Multiple determinants direct the orientation of signal-anchor proteins: The topogenic role of the hydrophobic signal domain
    • Wahlberg J.M., Spiess M. Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. J. Cell. Biol. 137:1997;555-562.
    • (1997) J. Cell. Biol. , vol.137 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 31
    • 0026595204 scopus 로고
    • How individual cells develop from a syncytium: Merogony in Theileria parva (Apicomplexa)
    • Shaw M.K., Tilney L.G. How individual cells develop from a syncytium: merogony in Theileria parva (Apicomplexa). J. Cell Sci. 101:1992;109-123.
    • (1992) J. Cell Sci. , vol.101 , pp. 109-123
    • Shaw, M.K.1    Tilney, L.G.2
  • 32
    • 0019956642 scopus 로고
    • The entry of sporozoites of Theileria parva into bovine lymphocytes in vitro. Electron microscopic observations
    • Fawcett D.W., Doxsey S. The entry of sporozoites of Theileria parva into bovine lymphocytes in vitro. Electron microscopic observations. Eur. J. Cell Biol. 27:1982;10-21.
    • (1982) Eur. J. Cell Biol. , vol.27 , pp. 10-21
    • Fawcett, D.W.1    Doxsey, S.2
  • 33
    • 0031253216 scopus 로고    scopus 로고
    • Targeting the secretory pathway of Toxoplasma gondii
    • Karsten V., Qi H., Beckers C.J., Joiner K.A. Targeting the secretory pathway of Toxoplasma gondii. Methods. 13:1997;103-111.
    • (1997) Methods , vol.13 , pp. 103-111
    • Karsten, V.1    Qi, H.2    Beckers, C.J.3    Joiner, K.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.