메뉴 건너뛰기




Volumn 580, Issue 27, 2006, Pages 6509-6512

Corrigendum to "Differential uptake of photosynthetic and non-photosynthetic proteins by pea root plastids" [FEBS Lett. 580 (2006) 6509-6512] (DOI:10.1016/j.febslet.2006.10.057);Differential uptake of photosynthetic and non-photosynthetic proteins by pea root plastids

Author keywords

Non photosynthetic; Photosynthetic; Pisum sativum; Protein import; Root plastids; Transit peptide

Indexed keywords

FERREDOXIN; FERREDOXIN I; FERREDOXIN III; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; PEPTIDE; PROTEIN; RIBULOSEBISPHOSPHATE CARBOXYLASE; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 33750972862     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.11.067     Document Type: Erratum
Times cited : (22)

References (31)
  • 1
    • 0030040689 scopus 로고    scopus 로고
    • Regulation of organelle biogenesis
    • Nunnari J., and Walter P. Regulation of organelle biogenesis. Cell 84 (1996) 389-394
    • (1996) Cell , vol.84 , pp. 389-394
    • Nunnari, J.1    Walter, P.2
  • 2
    • 23944431704 scopus 로고    scopus 로고
    • Recognition and envelope translocation of chloroplast preproteins
    • Bédard J., and Jarvis P. Recognition and envelope translocation of chloroplast preproteins. J. Exp. Bot. 56 419 (2005) 2287-2320
    • (2005) J. Exp. Bot. , vol.56 , Issue.419 , pp. 2287-2320
    • Bédard, J.1    Jarvis, P.2
  • 4
    • 0027984260 scopus 로고
    • Identification of two GTP-binding proteins in the chloroplast protein import machinery
    • Kessler F., Blobel G., Patel H.A., and Schnell D.J. Identification of two GTP-binding proteins in the chloroplast protein import machinery. Science 266 (1994) 1035-1039
    • (1994) Science , vol.266 , pp. 1035-1039
    • Kessler, F.1    Blobel, G.2    Patel, H.A.3    Schnell, D.J.4
  • 5
    • 0028584270 scopus 로고
    • A receptor component of the chloroplast protein translocation machinery
    • Hirsch S., Muckel E., Heemeyer F., von Heijine G., and Soll J. A receptor component of the chloroplast protein translocation machinery. Science 266 (1994) 1989-1992
    • (1994) Science , vol.266 , pp. 1989-1992
    • Hirsch, S.1    Muckel, E.2    Heemeyer, F.3    von Heijine, G.4    Soll, J.5
  • 6
    • 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. A constituent of the chloroplast import complex represents a new type of GTP-binding protein. Plant J. 7 (1995) 401-411
    • (1995) Plant J. , vol.7 , pp. 401-411
    • Seedorf, M.1    Waegemann, K.2    Soll, J.3
  • 7
    • 0027953126 scopus 로고
    • Envelope membrane proteins that interact with chloroplastic precursor proteins
    • Perry S.E., and Keegstra K. Envelope membrane proteins that interact with chloroplastic precursor proteins. Plant Cell 6 (1994) 93-105
    • (1994) Plant Cell , vol.6 , pp. 93-105
    • Perry, S.E.1    Keegstra, K.2
  • 8
    • 0029053516 scopus 로고
    • A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway
    • Tranel P., Froehlich J., Goyal A., and Keegstra K. A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. EMBO J. 14 (1995) 2436-2446
    • (1995) EMBO J. , vol.14 , pp. 2436-2446
    • Tranel, P.1    Froehlich, J.2    Goyal, A.3    Keegstra, K.4
  • 9
    • 0034689055 scopus 로고    scopus 로고
    • a new component of the protein translocon of chloroplasts
    • Sohrt K., and Soll J. a new component of the protein translocon of chloroplasts. J. Cell Biol. 148 (2000) 1213-1221
    • (2000) J. Cell Biol. , vol.148 , pp. 1213-1221
    • Sohrt, K.1    Soll, J.2
  • 10
    • 0000262786 scopus 로고
    • Chloroplast protein import-quantitative-analysis of precursor binding
    • Friedman A.L., and Keegstra K. Chloroplast protein import-quantitative-analysis of precursor binding. Plasma Phys. 89 (1989) 993-999
    • (1989) Plasma Phys. , vol.89 , pp. 993-999
    • Friedman, A.L.1    Keegstra, K.2
  • 11
    • 0029856727 scopus 로고    scopus 로고
    • Transit peptides play a major role in the preferential import of proteins into leucoplasts and chloroplasts
    • Wan J., Blakeley S.D., Dennis D.T., and Ko K. Transit peptides play a major role in the preferential import of proteins into leucoplasts and chloroplasts. J. Biol. Chem. 49 (1996) 31227-31233
    • (1996) J. Biol. Chem. , vol.49 , pp. 31227-31233
    • Wan, J.1    Blakeley, S.D.2    Dennis, D.T.3    Ko, K.4
  • 12
    • 0035037171 scopus 로고    scopus 로고
    • Arabidopsis genes encoding components of the chloroplastic protein import apparatus
    • Jackson-Constan D., and Keegstra K. Arabidopsis genes encoding components of the chloroplastic protein import apparatus. Plasma Phys. 125 (2001) 1567-1576
    • (2001) Plasma Phys. , vol.125 , pp. 1567-1576
    • Jackson-Constan, D.1    Keegstra, K.2
  • 14
    • 0034642558 scopus 로고    scopus 로고
    • The major protein import receptor of plastids is essential for chloroplast biogenesis
    • Bauer J., Chen K., Hiltbunner A., Wehrli E., Eugster M., Schnell D.J., and Kessler F. The major protein import receptor of plastids is essential for chloroplast biogenesis. Nature 403 (2000) 203-207
    • (2000) Nature , vol.403 , pp. 203-207
    • Bauer, J.1    Chen, K.2    Hiltbunner, A.3    Wehrli, E.4    Eugster, M.5    Schnell, D.J.6    Kessler, F.7
  • 15
    • 0033802314 scopus 로고    scopus 로고
    • Functional analysis of the two Arabidopsis homologues of Toc34, a component of the chloroplast protein import apparatus
    • Gutensohn M., Schulz B., Nicolay P., and Flugge U.I. Functional analysis of the two Arabidopsis homologues of Toc34, a component of the chloroplast protein import apparatus. Plant J. 23 (2000) 771-783
    • (2000) Plant J. , vol.23 , pp. 771-783
    • Gutensohn, M.1    Schulz, B.2    Nicolay, P.3    Flugge, U.I.4
  • 16
    • 0041920588 scopus 로고    scopus 로고
    • The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins
    • Kubis S., Baldwin A., Patel R., Razzaq A., Dupree P., Lilley K., Kurth J., Leister D., and Jarvis P. The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins. Plant Cell 15 (2003) 1859-1871
    • (2003) Plant Cell , vol.15 , pp. 1859-1871
    • Kubis, S.1    Baldwin, A.2    Patel, R.3    Razzaq, A.4    Dupree, P.5    Lilley, K.6    Kurth, J.7    Leister, D.8    Jarvis, P.9
  • 17
    • 0001552084 scopus 로고
    • Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L
    • Bowsher C.G., Hucklesby D.P., and Emes J.M. Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L. Planta 177 (1989) 359-366
    • (1989) Planta , vol.177 , pp. 359-366
    • Bowsher, C.G.1    Hucklesby, D.P.2    Emes, J.M.3
  • 18
    • 0002541390 scopus 로고
    • In vitro import of proteins into chloroplasts
    • Cold Spring Harbor Laboratory Press, NY
    • Lamppa G.K. In vitro import of proteins into chloroplasts. Methods in Plant Molecular Biology (1995), Cold Spring Harbor Laboratory Press, NY
    • (1995) Methods in Plant Molecular Biology
    • Lamppa, G.K.1
  • 19
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 20
    • 0000619617 scopus 로고
    • Plastid import and iron-sulfur cluster assembly of photosynthetic and non-photosynthetic ferredoxin isoproteins in maize
    • Suzuki S., Izumihara K., and Hase T. Plastid import and iron-sulfur cluster assembly of photosynthetic and non-photosynthetic ferredoxin isoproteins in maize. Plasma Phys. 97 (1991) 375-380
    • (1991) Plasma Phys. , vol.97 , pp. 375-380
    • Suzuki, S.1    Izumihara, K.2    Hase, T.3
  • 21
    • 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. Maize non-photosynthetic ferredoxin precursor is mis-sorted to the intermembrane space of chloroplasts in the presence of light. Plasma Phys. 125 (2001) 2154-2163
    • (2001) Plasma Phys. , vol.125 , pp. 2154-2163
    • Hirohashi, T.1    Hase, T.2    Nakai, M.3
  • 22
    • 0022903381 scopus 로고
    • Synthesis of the small subunit of ribulose-bisphosphate carboxylase from genes cloned into plasmids containing the SP6 promoter
    • Anderson S., and Smith S.M. Synthesis of the small subunit of ribulose-bisphosphate carboxylase from genes cloned into plasmids containing the SP6 promoter. Biochem. J. 240 (1986) 709-715
    • (1986) Biochem. J. , vol.240 , pp. 709-715
    • Anderson, S.1    Smith, S.M.2
  • 23
    • 0242692112 scopus 로고    scopus 로고
    • + oxidoreductase cDNA (Accession No. X99419)
    • + oxidoreductase cDNA (Accession No. X99419). Plasma Phys. 112 (1996) 861
    • (1996) Plasma Phys. , vol.112 , pp. 861
    • Bowsher, C.G.1    Knight, J.S.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0003022798 scopus 로고
    • Molecular cloning and differential expression of the maize ferredoxin gene family
    • Hase T., Kimata Y., Yonekura K., Matsumura T., and Sakakibara H. Molecular cloning and differential expression of the maize ferredoxin gene family. Plasma Phys. 96 (1991) 77-83
    • (1991) Plasma Phys. , vol.96 , pp. 77-83
    • Hase, T.1    Kimata, Y.2    Yonekura, K.3    Matsumura, T.4    Sakakibara, H.5
  • 27
    • 3042724874 scopus 로고    scopus 로고
    • Members of the toc159 import receptor family represent distinct pathways for protein targeting to plastids
    • Ivanova Y., Smith M.D., Chen K., and Schnell D.J. Members of the toc159 import receptor family represent distinct pathways for protein targeting to plastids. Mol. Biol. Cell 15 (2004) 3379-3392
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3379-3392
    • Ivanova, Y.1    Smith, M.D.2    Chen, K.3    Schnell, D.J.4
  • 29
    • 0038629037 scopus 로고    scopus 로고
    • Two Toc34 homologues with different properties
    • Jelic M., Soll J., and Schleiff E. Two Toc34 homologues with different properties. Biochem. 42 (2003) 5906-5916
    • (2003) Biochem. , vol.42 , pp. 5906-5916
    • Jelic, M.1    Soll, J.2    Schleiff, E.3
  • 30
    • 0034969808 scopus 로고    scopus 로고
    • Compartmentation of metabolism within mitochondria and plastids
    • Bowsher C.G., and Tobin A.K. Compartmentation of metabolism within mitochondria and plastids. J. Exp. Bot. 52 (2001) 513-527
    • (2001) J. Exp. Bot. , vol.52 , pp. 513-527
    • Bowsher, C.G.1    Tobin, A.K.2
  • 31
    • 0034818037 scopus 로고    scopus 로고
    • Chloroplast protein translocon components atToc159 and atToc33 are not essential for chloroplast biogenesis in guard cells and root cells
    • Yu T., and Li H. Chloroplast protein translocon components atToc159 and atToc33 are not essential for chloroplast biogenesis in guard cells and root cells. Plasma Phys. 127 (2001) 90-96
    • (2001) Plasma Phys. , vol.127 , pp. 90-96
    • Yu, T.1    Li, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.