메뉴 건너뛰기




Volumn 12, Issue 1, 2000, Pages 53-63

14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; FUNGI; PISUM SATIVUM; TRITICUM AESTIVUM;

EID: 0033950443     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.2307/3871029     Document Type: Article
Times cited : (271)

References (49)
  • 1
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 and its possible role in coordinating multiple signaling pathways
    • Aitken, A. (1996). 14-3-3 and its possible role in coordinating multiple signaling pathways. Trends Cell Biol. 6, 341-347.
    • (1996) Trends Cell Biol. , vol.6 , pp. 341-347
    • Aitken, A.1
  • 3
    • 0020671498 scopus 로고
    • Preparation of a cell-free protein-synthesizing system from wheat germ
    • Anderson, C.W., Straus, J.W., and Dudock, B.S. (1983). Preparation of a cell-free protein-synthesizing system from wheat germ. Methods Enzymol. 101, 635-644.
    • (1983) Methods Enzymol. , vol.101 , pp. 635-644
    • Anderson, C.W.1    Straus, J.W.2    Dudock, B.S.3
  • 4
    • 0032512413 scopus 로고    scopus 로고
    • Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews, R.K., Harris, S.J., McNally, T., and Berndt, M.C. (1998). Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. Biochemistry 37, 638-647.
    • (1998) Biochemistry , vol.37 , pp. 638-647
    • Andrews, R.K.1    Harris, S.J.2    McNally, T.3    Berndt, M.C.4
  • 5
    • 0025303147 scopus 로고
    • Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.E., and Welch, W.J. (1990). Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 6
    • 0039652375 scopus 로고    scopus 로고
    • A protein import receptor in pea chloroplasts, Toc86, is only a proteolytic fragment of a larger polypeptide
    • Bölter, B., May, T., and Soll, J. (1998). A protein import receptor in pea chloroplasts, Toc86, is only a proteolytic fragment of a larger polypeptide. FEBS Lett. 441, 59-62.
    • (1998) FEBS Lett. , vol.441 , pp. 59-62
    • Bölter, B.1    May, T.2    Soll, J.3
  • 7
    • 0005703602 scopus 로고
    • A nuclear gene encoding the β subunit of the mitochondrial ATP synthase in Nicotiana plumbaginifolia
    • Boutry, M., and Chua, N.-H. (1985). A nuclear gene encoding the β subunit of the mitochondrial ATP synthase in Nicotiana plumbaginifolia. EMBO J. 4, 2159-2165.
    • (1985) EMBO J. , vol.4 , pp. 2159-2165
    • Boutry, M.1    Chua, N.-H.2
  • 8
    • 0031053909 scopus 로고    scopus 로고
    • Mft52, an acid-bristle protein in the cytosol that delivers precursor proteins to yeast mitochondria
    • Cartwright, P., Beilharz, T., Hansen, P., Garrett, J., and Lithgow, T. (1997). Mft52, an acid-bristle protein in the cytosol that delivers precursor proteins to yeast mitochondria. J. Biol. Chem. 272, 5320-5325.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5320-5325
    • Cartwright, P.1    Beilharz, T.2    Hansen, P.3    Garrett, J.4    Lithgow, T.5
  • 9
    • 0033020533 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Chen, X., and Schnell, D.J. (1999). Protein import into chloroplasts. Trends Cell Biol. 9, 222-227.
    • (1999) Trends Cell Biol. , vol.9 , pp. 222-227
    • Chen, X.1    Schnell, D.J.2
  • 10
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline, K., Henry, R., Li, C., and Yuan, J. (1993). Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J. 12, 4105-4114.
    • (1993) EMBO J. , vol.12 , pp. 4105-4114
    • Cline, K.1    Henry, R.2    Li, C.3    Yuan, J.4
  • 11
    • 0001160047 scopus 로고    scopus 로고
    • Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein
    • de Castro Silva-Filho, M., Wieërs, M.-C., Flügge, U.-I., Chaumont, F., and Boutry, M. (1997). Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J. Biol. Chem. 272, 15264-15269.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15264-15269
    • De Castro Silva-Filho, M.1    Wieërs, M.-C.2    Flügge, U.-I.3    Chaumont, F.4    Boutry, M.5
  • 12
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R.J., Koch, B.D., Werner-Washburne, M., Craig, E.A., and Schekman, R. (1988). A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332, 800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 15
    • 0033167387 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Eukaryotic regulatory proteins with many functions
    • Finnie, C., Borch, J., and Collinge, D.B. (1999). 14-3-3 proteins: Eukaryotic regulatory proteins with many functions. Plant Mol. Biol. 40, 545-554.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 545-554
    • Finnie, C.1    Borch, J.2    Collinge, D.B.3
  • 16
    • 0032478067 scopus 로고    scopus 로고
    • The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo
    • George, R., Beddoe, T., Landl, K., and Lithgow, T. (1998). The yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo. Proc. Natl. Acad. Sci. USA 95, 2296-2301.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2296-2301
    • George, R.1    Beddoe, T.2    Landl, K.3    Lithgow, T.4
  • 17
    • 0027418577 scopus 로고
    • A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins
    • Hachiya, N., Alam, R., Sakasegawa, Y., Sakaguchi, M., Mihara, K., and Omura, T. (1993). A mitochondrial import factor purified from rat liver cytosol is an ATP-dependent conformational modulator for precursor proteins. EMBO J. 12, 1579-1586.
    • (1993) EMBO J. , vol.12 , pp. 1579-1586
    • Hachiya, N.1    Alam, R.2    Sakasegawa, Y.3    Sakaguchi, M.4    Mihara, K.5    Omura, T.6
  • 18
    • 0029096887 scopus 로고
    • Reconstitution of the initial steps of mitochondrial protein import
    • Hachiya, N., Mihara, K., Suda, K., Horst, M., Schatz, G., and Lithgow, T. (1995). Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709.
    • (1995) Nature , vol.376 , pp. 705-709
    • Hachiya, N.1    Mihara, K.2    Suda, K.3    Horst, M.4    Schatz, G.5    Lithgow, T.6
  • 19
    • 0031106617 scopus 로고    scopus 로고
    • Import of proteins into mitochondria and chloroplasts
    • Haucke, V., and Schatz, G. (1997). Import of proteins into mitochondria and chloroplasts. Trends Cell Biol. 7, 103-106.
    • (1997) Trends Cell Biol. , vol.7 , pp. 103-106
    • Haucke, V.1    Schatz, G.2
  • 20
    • 0027467268 scopus 로고
    • Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2
    • Hennekes, H., Peter, M., Weber, K., and Nigg, E.A. (1993). Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2. J. Cell Biol. 120, 1293-1304.
    • (1993) J. Cell Biol. , vol.120 , pp. 1293-1304
    • Hennekes, H.1    Peter, M.2    Weber, K.3    Nigg, E.A.4
  • 21
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah, S.C., Hill, K., Wagner, R., Schlicher, T., and Soll, J. (1997). Reconstitution of a chloroplast protein import channel. EMBO J. 16, 7351-7360.
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 22
    • 0026558918 scopus 로고
    • A plant homologue to mammalian brain 14-3-3 protein and protein kinase C inhibitor
    • Hirsch, S., Aitken, A., Bertsch, U., and Soll, J. (1992). A plant homologue to mammalian brain 14-3-3 protein and protein kinase C inhibitor. FEBS Lett. 296, 222-224.
    • (1992) FEBS Lett. , vol.296 , pp. 222-224
    • Hirsch, S.1    Aitken, A.2    Bertsch, U.3    Soll, J.4
  • 23
    • 0025919717 scopus 로고
    • p34cdc2-Mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins
    • Jans, D.A., Ackermann, M.J., Bischoff, J.R., Beach, D.H., and Peters, R. (1991). p34cdc2-mediated phosphorylation at T124 inhibits nuclear import of SV-40 T antigen proteins. J. Cell Biol. 115, 1203-1212.
    • (1991) J. Cell Biol. , vol.115 , pp. 1203-1212
    • Jans, D.A.1    Ackermann, M.J.2    Bischoff, J.R.3    Beach, D.H.4    Peters, R.5
  • 24
    • 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
  • 26
    • 0000095603 scopus 로고
    • Photoaffinity labeling of mature and precursor forms of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase after expression in Escherichia coli
    • Klein, R.R., and Salvucci, M.E. (1992). Photoaffinity labeling of mature and precursor forms of the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase after expression in Escherichia coli. Plant Physiol. 98, 546-553.
    • (1992) Plant Physiol. , vol.98 , pp. 546-553
    • Klein, R.R.1    Salvucci, M.E.2
  • 27
    • 0030752305 scopus 로고    scopus 로고
    • Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones
    • Komiya, T., Rospert, S., Schatz, G., and Mihara, K. (1997). Binding of mitochondrial precursor proteins to the cytoplasmic domains of the import receptors Tom70 and Tom20 is determined by cytoplasmic chaperones. EMBO J. 16, 4267-4275.
    • (1997) EMBO J. , vol.16 , pp. 4267-4275
    • Komiya, T.1    Rospert, S.2    Schatz, G.3    Mihara, K.4
  • 28
    • 0031408330 scopus 로고    scopus 로고
    • Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts
    • Kouranov, A., and Schnell, D.J. (1997). Analysis of the interactions of preproteins with the import machinery over the course of protein import into chloroplasts. J. Cell Biol. 139, 1677-1685.
    • (1997) J. Cell Biol. , vol.139 , pp. 1677-1685
    • Kouranov, A.1    Schnell, D.J.2
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the heads of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the heads of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0029894578 scopus 로고    scopus 로고
    • Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope
    • Ma, Y., Kouranov, A., LaSala, S.E., and Schnell, D.J. (1996). Two components of the chloroplast protein import apparatus, IAP86 and IAP75, interact with the transit sequence during the recognition and translocation of precursor proteins at the outer envelope, J. Cell Biol. 134, 315-327.
    • (1996) J. Cell Biol. , vol.134 , pp. 315-327
    • Ma, Y.1    Kouranov, A.2    LaSala, S.E.3    Schnell, D.J.4
  • 32
    • 0001057395 scopus 로고
    • Assay and purification of protein (serine/threonine) phosphatases
    • D.G. Hardie, ed (New York: Oxford University Press)
    • MacKintosh, C. (1993). Assay and purification of protein (serine/threonine) phosphatases. In Protein Phosphorylation, D.G. Hardie, ed (New York: Oxford University Press), pp. 197-230.
    • (1993) Protein Phosphorylation , pp. 197-230
    • MacKintosh, C.1
  • 33
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5
    • Moll, T., Tebb, G., Surana, U., Robitsch, H., and Nasmyth, K. (1991). The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66, 743-758.
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 34
    • 0026689327 scopus 로고
    • Presequence binding factor-dependent and -independent import of proteins into mitochondria
    • Murakami, K., Tanase, S., Morino, Y., and Mori, M. (1992). Presequence binding factor-dependent and -independent import of proteins into mitochondria. J. Biol. Chem. 267, 13119-13122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13119-13122
    • Murakami, K.1    Tanase, S.2    Morino, Y.3    Mori, M.4
  • 35
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A.J., Tanner, J.W., Allen, P.M., and Shaw, A.S. (1996). Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84, 889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 37
    • 0027953126 scopus 로고
    • Envelope membrane proteins that interact with chloroplastic precursor proteins
    • Perry, S.E., and Keegstra, K. (1994). Envelope membrane proteins that interact with chloroplastic precursor proteins. Plant Cell 6, 93-105.
    • (1994) Plant Cell , vol.6 , pp. 93-105
    • Perry, S.E.1    Keegstra, K.2
  • 39
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen
    • Rihs, H.-P., Jans, D.A., Fan, H., and Peters, R. (1991). The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 10, 633-639.
    • (1991) EMBO J. , vol.10 , pp. 633-639
    • Rihs, H.-P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 40
    • 0029257229 scopus 로고
    • A constituent of the chloroplast import complex represents a new type of GTP-binding protein
    • Seedorf, M., Waegemann, K., and Soll, J. (1995). A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J. 7, 401-411
    • (1995) Plant J. , vol.7 , pp. 401-411
    • Seedorf, M.1    Waegemann, K.2    Soll, J.3
  • 41
    • 0000489161 scopus 로고
    • Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts
    • Waegemann, K., and Soll, J. (1991). Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts. Plant J. 1, 149-158.
    • (1991) Plant J. , vol.1 , pp. 149-158
    • Waegemann, K.1    Soll, J.2
  • 42
    • 0029448155 scopus 로고
    • Characterization and isolation of the chloroplast protein import machinery
    • Waegemann, K., and Soll, J. (1995). Characterization and isolation of the chloroplast protein import machinery. Methods Cell Biol. 50, 255-267.
    • (1995) Methods Cell Biol. , vol.50 , pp. 255-267
    • Waegemann, K.1    Soll, J.2
  • 43
    • 0029868470 scopus 로고    scopus 로고
    • Phosphorylation of the transit sequence of chloroplast precursor proteins
    • Waegemann, K., and Soll, J. (1996). Phosphorylation of the transit sequence of chloroplast precursor proteins. J. Biol. Chem. 271, 6545-6554.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6545-6554
    • Waegemann, K.1    Soll, J.2
  • 44
    • 0025093379 scopus 로고
    • Translocation of proteins into chloroplasts requires cytosolic factors to obtain import competence
    • Waegemann, K., Paulsen, H., and Soll, J. (1990). Translocation of proteins into chloroplasts requires cytosolic factors to obtain import competence. FEBS Lett. 261, 89-92.
    • (1990) FEBS Lett. , vol.261 , pp. 89-92
    • Waegemann, K.1    Paulsen, H.2    Soll, J.3
  • 45
    • 0031200784 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 multigene family
    • Wu, K., Rooney, M.F., and Ferl, R.J. (1997). The Arabidopsis 14-3-3 multigene family. Plant Physiol. 114, 1421-1431.
    • (1997) Plant Physiol. , vol.114 , pp. 1421-1431
    • Wu, K.1    Rooney, M.F.2    Ferl, R.J.3
  • 46
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signaling pathways
    • Xiao, B., Smerdon, S.J., Jones, D.H., Dodson, G.G., Soneji, Y., Aitken, A., and Gamblin, S.J. (1995). Structure of a 14-3-3 protein and implications for coordination of multiple signaling pathways. Nature 376, 188-191.
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5    Aitken, A.6    Gamblin, S.J.7
  • 48
    • 0033561439 scopus 로고    scopus 로고
    • Maintenance of G2 arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import
    • Yang, J., Winkler, K., Yoshida, M., and Kornbluth, S. (1999). Maintenance of G2 arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import. EMBO J. 18, 2174-2183.
    • (1999) EMBO J. , vol.18 , pp. 2174-2183
    • Yang, J.1    Winkler, K.2    Yoshida, M.3    Kornbluth, S.4
  • 49
    • 0024077833 scopus 로고
    • Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes
    • Zimmermann, R., Sagstetter, M., Lewis, M.J., and Pelham, H.R. (1988). Seventy-kilodalton heat shock proteins and an additional component from reticulocyte lysate stimulate import of M13 procoat protein into microsomes. EMBO J. 7, 2875-2880.
    • (1988) EMBO J. , vol.7 , pp. 2875-2880
    • Zimmermann, R.1    Sagstetter, M.2    Lewis, M.J.3    Pelham, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.