메뉴 건너뛰기




Volumn 16, Issue 1, 2004, Pages 201-214

Maize Mutants Lacking Chloroplast FtsY Exhibit Pleiotropic Defects in the Biogenesis of Thylakoid Membranes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; FOOD PRODUCTS; GENES; PHOTOSYNTHESIS; TISSUE;

EID: 0842270048     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.014787     Document Type: Article
Times cited : (71)

References (58)
  • 1
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • Allen, J.F., and Forsberg, J. (2001). Molecular recognition in thylakoid structure and function. Trends Plant Sci. 6, 317-326.
    • (2001) Trends Plant Sci. , vol.6 , pp. 317-326
    • Allen, J.F.1    Forsberg, J.2
  • 2
    • 0033198467 scopus 로고    scopus 로고
    • Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes
    • Amin, P., Sy, D.A., Pilgrim, M.L., Parry, D.H., Nussaume, L., and Hoffman, N.E. (1999). Arabidopsis mutants lacking the 43-and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes. Plant Physiol. 121, 61-70.
    • (1999) Plant Physiol. , vol.121 , pp. 61-70
    • Amin, P.1    Sy, D.A.2    Pilgrim, M.L.3    Parry, D.H.4    Nussaume, L.5    Hoffman, N.E.6
  • 3
    • 0035020030 scopus 로고    scopus 로고
    • Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: Implications for the mechanism of protective energy dissipation
    • Andersson, J., Walters, R.G., Horton, P., and Jansson, S. (2001). Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: Implications for the mechanism of protective energy dissipation. Plant Cell 13, 1193-1204.
    • (2001) Plant Cell , vol.13 , pp. 1193-1204
    • Andersson, J.1    Walters, R.G.2    Horton, P.3    Jansson, S.4
  • 4
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts
    • Arnon, D.I. (1949). Copper enzymes in isolated chloroplasts. Plant Physiol. 24, 1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 5
    • 0038707432 scopus 로고    scopus 로고
    • POR: Import and membrane association of a key element in chloroplast development
    • Aronsson, H., Sundqvist, C., and Dahlin, C. (2003). POR: Import and membrane association of a key element in chloroplast development. Physiol. Plant. 118, 1-9.
    • (2003) Physiol. Plant. , vol.118 , pp. 1-9
    • Aronsson, H.1    Sundqvist, C.2    Dahlin, C.3
  • 7
    • 0022851237 scopus 로고
    • Import of proteins into chloroplasts
    • Cline, K. (1986). Import of proteins into chloroplasts. J. Biol. Chem. 261, 14804-14810.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14804-14810
    • Cline, K.1
  • 9
    • 0034652118 scopus 로고    scopus 로고
    • A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts
    • DeLille, J., Peterson, E.G., Johnson, T., Moore, M., Kight, A., and Henry, R. (2000). A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts. Proc. Natl. Acad. Sci. USA 97, 1926-1931.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1926-1931
    • DeLille, J.1    Peterson, E.G.2    Johnson, T.3    Moore, M.4    Kight, A.5    Henry, R.6
  • 10
    • 0033008601 scopus 로고    scopus 로고
    • Protein targeting to the bacterial cytoplasmic membrane
    • Fekkes, P., and Driessen, A.J. (1999). Protein targeting to the bacterial cytoplasmic membrane. Microbiol. Mol. Biol. Rev. 63, 161-173.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 161-173
    • Fekkes, P.1    Driessen, A.J.2
  • 11
    • 0035958865 scopus 로고    scopus 로고
    • Functional characterization of recombinant chloroplast signal recognition particle
    • Groves, M.R., Mant, A., Kuhn, A., Koch, J., Dubel, S., Robinson, C., and Sinning, I. (2001). Functional characterization of recombinant chloroplast signal recognition particle. J. Biol. Chem. 276, 27778-27786.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27778-27786
    • Groves, M.R.1    Mant, A.2    Kuhn, A.3    Koch, J.4    Dubel, S.5    Robinson, C.6    Sinning, I.7
  • 12
    • 0031020515 scopus 로고    scopus 로고
    • FtsY, the prokaryotlc signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins
    • Herskovits, A., and Bibi, E. (1997). FtsY, the prokaryotlc signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins. J. Biol. Chem. 272, 2053-2055.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2053-2055
    • Herskovits, A.1    Bibi, E.2
  • 13
    • 85041133119 scopus 로고    scopus 로고
    • Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle
    • Herskovits, A., and Bibi, E. (2000). Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle. Proc. Natl. Acad. Sci. USA 97, 4621-4626.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4621-4626
    • Herskovits, A.1    Bibi, E.2
  • 14
    • 0035028336 scopus 로고    scopus 로고
    • Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light
    • Hirohashi, T., Hase, T., and Nakai, M. (2001). Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light. Plant Physiol. 125, 2154-2163.
    • (2001) Plant Physiol. , vol.125 , pp. 2154-2163
    • Hirohashi, T.1    Hase, T.2    Nakai, M.3
  • 15
    • 0034712785 scopus 로고    scopus 로고
    • Molecular cloning and characterization of maize Toc34, a regulatory component of the protein import machinery of chloroplast
    • Hirohashi, T., and Nakai, M. (2000). Molecular cloning and characterization of maize Toc34, a regulatory component of the protein import machinery of chloroplast. Biochim. Biophys. Acta 1491, 309-314.
    • (2000) Biochim. Biophys. Acta , vol.1491 , pp. 309-314
    • Hirohashi, T.1    Nakai, M.2
  • 16
    • 0028430193 scopus 로고
    • Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b-binding polypeptide into thylakoid membranes
    • Hoffman, N.E., and Franklin, A.E. (1994). Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b-binding polypeptide into thylakoid membranes. Plant Physiol. 105, 295-304.
    • (1994) Plant Physiol. , vol.105 , pp. 295-304
    • Hoffman, N.E.1    Franklin, A.E.2
  • 17
    • 0036006185 scopus 로고    scopus 로고
    • Double mutation cpSRP43-/cpSRP54- Is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins
    • Hutin, C., Havaux, M., Carde, J.P., Kloppstech, K., Meiherhoff, K., Hoffman, N., and Nussaume, L. (2002). Double mutation cpSRP43-/cpSRP54-is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins. Plant J. 29, 531-543.
    • (2002) Plant J. , vol.29 , pp. 531-543
    • Hutin, C.1    Havaux, M.2    Carde, J.P.3    Kloppstech, K.4    Meiherhoff, K.5    Hoffman, N.6    Nussaume, L.7
  • 18
    • 0035816712 scopus 로고    scopus 로고
    • Functional analysis of the protein-interacting domains of chloroplast SRP43
    • Jonas-Straube, E., Hutin, C., Hoffman, N.E., and Schunemann, D. (2001). Functional analysis of the protein-interacting domains of chloroplast SRP43. J. Biol. Chem. 276, 24654-24660.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24654-24660
    • Jonas-Straube, E.1    Hutin, C.2    Hoffman, N.E.3    Schunemann, D.4
  • 19
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra, K., and Cline, K. (1999). Protein import and routing systems of chloroplasts. Plant Cell 11, 557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 20
    • 0025787343 scopus 로고
    • Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1
    • Kim, J., Klein, P.G., and Mullet, J.E. (1991). Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1. J. Biol. Chem. 266, 14931-14938.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14931-14938
    • Kim, J.1    Klein, P.G.2    Mullet, J.E.3
  • 21
    • 6544282660 scopus 로고    scopus 로고
    • A chromodomain protein encoded by the Arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting
    • Klimyuk, V.I., Persello-Cartieaux, F., Havaux, M., Contard-David, P., Schuenemann, D., Meiherhoff, K., Gouet, P., Jones, J.D., Hoffman, N.E., and Nussaume, L. (1999). A chromodomain protein encoded by the Arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting. Plant Cell 11, 87-99.
    • (1999) Plant Cell , vol.11 , pp. 87-99
    • Klimyuk, V.I.1    Persello-Cartieaux, F.2    Havaux, M.3    Contard-David, P.4    Schuenemann, D.5    Meiherhoff, K.6    Gouet, P.7    Jones, J.D.8    Hoffman, N.E.9    Nussaume, L.10
  • 22
    • 0032973271 scopus 로고    scopus 로고
    • Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakolds
    • Kogata, N., Nishio, K., Hirohashi, T., Kikuchi, S., and Nakai, M. (1999). Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakolds. FEBS Lett. 447, 329-333.
    • (1999) FEBS Lett. , vol.447 , pp. 329-333
    • Kogata, N.1    Nishio, K.2    Hirohashi, T.3    Kikuchi, S.4    Nakai, M.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0029041304 scopus 로고
    • A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes
    • Li, X., Henry, R., Yuan, J., Cline, K., and Hoffman, N.E. (1995). A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes. Proc. Natl. Acad. Sci. USA 92, 3789-3793.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3789-3793
    • Li, X.1    Henry, R.2    Yuan, J.3    Cline, K.4    Hoffman, N.E.5
  • 25
    • 77957068711 scopus 로고
    • Chlorophylls and carotenoids: Pigments of photosynthetic biomembranes
    • Lichtenthaler, H.K. (1987). Chlorophylls and carotenoids: Pigments of photosynthetic biomembranes. Methods Enzymol. 148, 351-382.
    • (1987) Methods Enzymol. , vol.148 , pp. 351-382
    • Lichtenthaler, H.K.1
  • 26
    • 0027493918 scopus 로고
    • The maize transposable element system Ac/Ds as a mutagen in Arabidopsis: Identification of an albino mutation induced by Ds insertion
    • Long, D., Martin, M., Sundberg, E., Swinburne, J., Puangsomlee, P., and Coupland, G. (1993). The maize transposable element system Ac/Ds as a mutagen in Arabidopsis: Identification of an albino mutation induced by Ds insertion. Proc. Natl. Acad. Sci. USA 90, 10370-10374.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10370-10374
    • Long, D.1    Martin, M.2    Sundberg, E.3    Swinburne, J.4    Puangsomlee, P.5    Coupland, G.6
  • 28
    • 0040958829 scopus 로고    scopus 로고
    • A simple, rapid and quantitative method for preparing Arabidopsis protein extracts for immunoblot analysis
    • Martinez-Garcia, J.F., Monte, E., and Quail, P.H. (1999). A simple, rapid and quantitative method for preparing Arabidopsis protein extracts for immunoblot analysis. Plant J. 20, 251-257.
    • (1999) Plant J. , vol.20 , pp. 251-257
    • Martinez-Garcia, J.F.1    Monte, E.2    Quail, P.H.3
  • 29
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
    • Montoya, G., Svensson, C., Luirink, J., and Sinning, I. (1997). Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 385, 365-368.
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 30
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxa1 p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
    • Moore, M., Harrison, M.S., Peterson, E.G., and Henry, R. (2000). Chloroplast Oxa1 p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J. Biol. Chem. 275, 1529-1532.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, M.S.2    Peterson, E.G.3    Henry, R.4
  • 31
    • 0027944148 scopus 로고
    • Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport
    • Nakai, M., Goto, A., Nohara, T., Sugita, D., and Endo, T. (1994). Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport. J. Biol. Chem. 269, 31338-31341.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31338-31341
    • Nakai, M.1    Goto, A.2    Nohara, T.3    Sugita, D.4    Endo, T.5
  • 32
    • 0033081464 scopus 로고    scopus 로고
    • Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54
    • Nilsson, R., Brunner, J., Hoffman, N.E., and van Wijk, K.J. (1999). Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54. EMBO J. 18, 733-742.
    • (1999) EMBO J. , vol.18 , pp. 733-742
    • Nilsson, R.1    Brunner, J.2    Hoffman, N.E.3    Van Wijk, K.J.4
  • 33
    • 0033590077 scopus 로고    scopus 로고
    • Chloroplast chaperonins: Evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer
    • Nishio, K., Hirohashi, T., and Nakai, M. (1999). Chloroplast chaperonins: Evidence for heterogeneous assembly of alpha and beta Cpn60 polypeptides into a chaperonin oligomer. Biochem. Biophys. Res. Commun. 266, 584-587.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 584-587
    • Nishio, K.1    Hirohashi, T.2    Nakai, M.3
  • 34
    • 0028998696 scopus 로고
    • Isolation and characterization of the cDNA for pea chloroplast SecA: Evolutionary conservation of bacterial-type SecA-dependent protein transport within chloroplasts
    • Nohara, T., Nakai, M., Goto, A., and Endo, T. (1995). Isolation and characterization of the cDNA for pea chloroplast SecA: Evolutionary conservation of bacterial-type SecA-dependent protein transport within chloroplasts. FEBS Lett. 364, 305-308.
    • (1995) FEBS Lett. , vol.364 , pp. 305-308
    • Nohara, T.1    Nakai, M.2    Goto, A.3    Endo, T.4
  • 35
    • 0034595744 scopus 로고    scopus 로고
    • Identification and light-induced expression of a novel gene of NADPH-protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana
    • Oosawa, N., Masuda, T., Awai, K., Fusada, N., Shimada, H., Ohta, H., and Takamiya, K. (2000). Identification and light-induced expression of a novel gene of NADPH-protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana. FEBS Lett. 474, 133-136.
    • (2000) FEBS Lett. , vol.474 , pp. 133-136
    • Oosawa, N.1    Masuda, T.2    Awai, K.3    Fusada, N.4    Shimada, H.5    Ohta, H.6    Takamiya, K.7
  • 36
    • 0002180478 scopus 로고
    • Transmission electron microscopy: Chemical fixation, freezing methods, and immunolocalization
    • M. Freeling and V. Walbot, eds (New York: Springer-Verlag)
    • Parthasarathy, M.V. (1994). Transmission electron microscopy: Chemical fixation, freezing methods, and immunolocalization. In The Maize Handbook, M. Freeling and V. Walbot, eds (New York: Springer-Verlag), pp. 118-134.
    • (1994) The Maize Handbook , pp. 118-134
    • Parthasarathy, M.V.1
  • 37
    • 0026071203 scopus 로고
    • A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein
    • Payan, L.A., and Cline, K. (1991). A stromal protein factor maintains the solubility and insertion competence of an imported thylakoid membrane protein. J. Cell Biol. 112, 603-613.
    • (1991) J. Cell Biol. , vol.112 , pp. 603-613
    • Payan, L.A.1    Cline, K.2
  • 38
    • 0031905338 scopus 로고    scopus 로고
    • Expression of a dominant negative form of cpSRP54 inhibits chloroplast biogenesis in Arabidopsis
    • Pilgrim, M.L., van Wijk, K.J., Parry, D.H., Sy, D.A., and Hoffman, N.E. (1998). Expression of a dominant negative form of cpSRP54 inhibits chloroplast biogenesis in Arabidopsis. Plant J. 13, 177-186.
    • (1998) Plant J. , vol.13 , pp. 177-186
    • Pilgrim, M.L.1    Van Wijk, K.J.2    Parry, D.H.3    Sy, D.A.4    Hoffman, N.E.5
  • 39
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T.A., Jungnickel, B., and Kutay, U. (1996). Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu. Rev. Biochem. 65, 271-303.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 40
    • 0029930771 scopus 로고    scopus 로고
    • Differential D1 dephosphorylation in functional and photodamaged photosystem II centers: Dephosphorylation is a prerequisite for degradation of damaged D1
    • Rintamaki, E., Kettunen, R., and Aro, E.M. (1996). Differential D1 dephosphorylation in functional and photodamaged photosystem II centers: Dephosphorylation is a prerequisite for degradation of damaged D1. J. Biol. Chem. 271, 14870-14875.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14870-14875
    • Rintamaki, E.1    Kettunen, R.2    Aro, E.M.3
  • 41
    • 0032169929 scopus 로고    scopus 로고
    • Multiple pathways for the targeting of thylakoid proteins in chloroplasts
    • Robinson, C., Hynds, P.J., Robinson, D., and Mant, A. (1998). Multiple pathways for the targeting of thylakoid proteins in chloroplasts. Plant Mol. Biol. 38, 209-221.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 209-221
    • Robinson, C.1    Hynds, P.J.2    Robinson, D.3    Mant, A.4
  • 42
    • 0032550223 scopus 로고    scopus 로고
    • A SecY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression
    • Roy, L.M., and Barkan, A. (1998). A SecY homologue is required for the elaboration of the chloroplast thylakoid membrane and for normal chloroplast gene expression. J. Cell Biol. 141, 385-395.
    • (1998) J. Cell Biol. , vol.141 , pp. 385-395
    • Roy, L.M.1    Barkan, A.2
  • 43
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W.A., and von Jagow, G. (1994). Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 45
    • 0037140924 scopus 로고    scopus 로고
    • Conformational change of the N-domain on formation of the complex between the GTPase of Thermus aquaticus Ffh and FtsY
    • Shepotinovskaya, I.V., and Freymann, D.M. (2002). Conformational change of the N-domain on formation of the complex between the GTPase of Thermus aquaticus Ffh and FtsY. Biochim. Biophys. Acta 1597, 107-114.
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 107-114
    • Shepotinovskaya, I.V.1    Freymann, D.M.2
  • 46
    • 0031131609 scopus 로고    scopus 로고
    • ALBINO3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria
    • Sundberg, E., Slagter, J.G., Fridborg, I., Cleary, S.P., Robinson, C., and Coupland, G. (1997). ALBINO3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria. Plant Cell 9, 717-730.
    • (1997) Plant Cell , vol.9 , pp. 717-730
    • Sundberg, E.1    Slagter, J.G.2    Fridborg, I.3    Cleary, S.P.4    Robinson, C.5    Coupland, G.6
  • 47
    • 0023025837 scopus 로고
    • The signal recognition particle receptor is a complex that contains two distinct polypeptide chains
    • Tajima, S., Lauffer, L., Rath, V.L., and Walter, P. (1986). The signal recognition particle receptor is a complex that contains two distinct polypeptide chains. J. Cell Biol. 103, 1167-1178.
    • (1986) J. Cell Biol. , vol.103 , pp. 1167-1178
    • Tajima, S.1    Lauffer, L.2    Rath, V.L.3    Walter, P.4
  • 48
    • 0000580602 scopus 로고    scopus 로고
    • The L18 domain of light-harvesting chlorophyll proteins binds to chloroplast signal recognition particle 43
    • Tu, C.J., Peterson, E.C., Henry, R., and Hoffman, N.E. (2000). The L18 domain of light-harvesting chlorophyll proteins binds to chloroplast signal recognition particle 43. J. Biol. Chem. 275, 13187-13190.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13187-13190
    • Tu, C.J.1    Peterson, E.C.2    Henry, R.3    Hoffman, N.E.4
  • 49
    • 0033578755 scopus 로고    scopus 로고
    • Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes
    • Tu, C.J., Schuenemann, D., and Hoffman, N.E. (1999). Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes. J. Biol. Chem. 274, 27219-27224.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27219-27224
    • Tu, C.J.1    Schuenemann, D.2    Hoffman, N.E.3
  • 50
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker, R., and Barkan, A. (1995). Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 14, 3905-3914.
    • (1995) EMBO J. , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 51
    • 0032746027 scopus 로고    scopus 로고
    • The maize tha4 gene functions in Sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB
    • Walker, M.B., Roy, L.M., Coleman, E., Voelker, R., and Barkan, A. (1999). The maize tha4 gene functions in Sec-independent protein transport in chloroplasts and is related to hcf106, tatA, and tatB. J. Cell Biol. 147, 267-276.
    • (1999) J. Cell Biol. , vol.147 , pp. 267-276
    • Walker, M.B.1    Roy, L.M.2    Coleman, E.3    Voelker, R.4    Barkan, A.5
  • 52
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., and Johnson, A.E. (1994). Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 53
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes1
    • Wollman, F.A., Minai, L., and Nechushtai, R. (1999). The biogenesis and assembly of photosynthetic proteins in thylakoid membranes1. Biochim. Biophys. Acta 1411, 21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 55
    • 0035544110 scopus 로고    scopus 로고
    • Separate localization of light signal perception for sun or shade type chloroplast and palisade tissue differentiation in Chenopodium album
    • Yano, S., and Terashima, I. (2001). Separate localization of light signal perception for sun or shade type chloroplast and palisade tissue differentiation in Chenopodium album. Plant Cell Physiol. 42, 1303-1310.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1303-1310
    • Yano, S.1    Terashima, I.2
  • 56
    • 0035544125 scopus 로고    scopus 로고
    • Photosystem II damage and repair cycle in the green alga Dunaliella salina: Involvement of a chloroplast-localized HSP70
    • Yokthongwattana, K., Chrost, B., Behrman, S., Casper-Lindtey, C., and Melis, A. (2001). Photosystem II damage and repair cycle in the green alga Dunaliella salina: Involvement of a chloroplast-localized HSP70. Plant Cell Physiol. 42, 1389-1397.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1389-1397
    • Yokthongwattana, K.1    Chrost, B.2    Behrman, S.3    Casper-Lindtey, C.4    Melis, A.5
  • 57
    • 0037070198 scopus 로고    scopus 로고
    • Synthesis, membrane insertion and assembly of the chloroplast-encoded D1 protein into photosystem II
    • Zhang, L., and Aro, E.M. (2002). Synthesis, membrane insertion and assembly of the chloroplast-encoded D1 protein into photosystem II. FEBS Lett. 512, 13-18.
    • (2002) FEBS Lett. , vol.512 , pp. 13-18
    • Zhang, L.1    Aro, E.M.2
  • 58
    • 0035851097 scopus 로고    scopus 로고
    • A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis
    • Zhang, L., Paakkarinen, V., Suorsa, M., and Aro, E.M. (2001). A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis. J. Biol. Chem. 276, 37809-37814.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37809-37814
    • Zhang, L.1    Paakkarinen, V.2    Suorsa, M.3    Aro, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.