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Volumn 7, Issue 1, 2002, Pages 14-21

Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone

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Indexed keywords

EMBRYOPHYTA;

EID: 0036007390     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(01)02180-X     Document Type: Review
Times cited : (195)

References (87)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 3
    • 0032051742 scopus 로고    scopus 로고
    • The organization and evolution of the spinach stress 70 molecular chaperone gene family
    • (1998) Plant Cell , vol.10 , pp. 539-556
    • Guy, C.L.1    Li, Q.B.2
  • 4
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.1
  • 5
    • 0033597380 scopus 로고    scopus 로고
    • Interaction of mitochondrial presequences with DnaK and mitochondriaI Hsp70
    • (1999) J. Mol. Biol. , vol.288 , pp. 177-190
    • Zhang, X.P.1
  • 6
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1
  • 7
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding-specificity of Bip
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1
  • 8
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekii and the origin of mitochondria
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.1
  • 10
    • 0031021278 scopus 로고    scopus 로고
    • The mitochondrial genome of Arabidopsis thaliana contains 57 genes in 366,924 nucleotides
    • (1997) Nat. Genet. , vol.15 , pp. 57-61
    • Unseld, M.1
  • 11
    • 0033615372 scopus 로고    scopus 로고
    • Complete structure of the chloroplast genome of Arabidopsis thaliana
    • (1999) DNA Res. , vol.6 , pp. 283-290
    • Sato, S.1
  • 12
    • 36348955545 scopus 로고    scopus 로고
    • A prediction of the size and evolutionary origin of the proteome of chloroplasts of Arabidopsis
    • (2000) Trends Plant Sci. , vol.5 , pp. 141-142
    • Abdallah, F.1
  • 13
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • (2000) Nature , vol.408 , pp. 796-815
  • 14
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1
  • 16
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1
  • 18
    • 0033807725 scopus 로고    scopus 로고
    • Travelling of proteins through membranes: Translocation into chloroplasts
    • (2000) Planta , vol.211 , pp. 449-456
    • Schleiff, E.1    Soll, J.2
  • 20
    • 0033928908 scopus 로고    scopus 로고
    • How do plant mitochondria avoid importing chloroplast proteins? Components of the import apparatus Tom20 and Tom22 from Arabidopsis differ from their fungal counterparts
    • (2000) Plant Physiol. , vol.123 , pp. 811-816
    • Macasev, D.1
  • 23
    • 0033523765 scopus 로고    scopus 로고
    • Stromal processing peptidase binds transit peptides and initiates their ATP-dependent turnover in chloroplasts
    • (1999) J. Cell Biol. , vol.147 , pp. 33-44
    • Richter, S.1    Lamppa, G.K.2
  • 25
    • 0034598904 scopus 로고    scopus 로고
    • Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20
    • (2000) Cell , vol.100 , pp. 551-560
    • Abe, Y.1
  • 26
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 Proteins form a guidance complex with chloroplast precursor proteins in plants
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soil, J.2
  • 27
    • 0027986880 scopus 로고
    • A spectroscopic study of the mitochondrial transit peptide of rat malate dehydrogenase
    • (1994) Biochem. J. , vol.303 , pp. 657-662
    • MacLachlan, L.K.1
  • 28
    • 0034687710 scopus 로고    scopus 로고
    • Interaction of a mitochondrial presequence with lipid membranes: Role of helix formation for membrane binding and perturbation
    • (2000) Biochemistry , vol.39 , pp. 15297-15305
    • Wieprecht, T.1
  • 29
    • 0026683021 scopus 로고
    • The chloroplast-targeting domain of plastocyanin transit peptide can form a helical structure but does not have a high affinity for lipid bilayers
    • (1992) Eur. J. Biochem. , vol.207 , pp. 671-675
    • Endo, T.1
  • 30
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • (1986) EMBO J. , vol.5 , pp. 1335-1342
    • Von Heijne, G.1
  • 32
    • 0024723123 scopus 로고
    • N-terminal half of a mitochondrial presequence peptide takes a helical conformation when bound to dodecylphosphocholine micelles: A proton nuclear magnetic resonance study
    • (1989) J. Biochem. , vol.106 , pp. 396-400
    • Endo, T.1
  • 33
    • 0027295559 scopus 로고
    • Import, processing, and two-dimensional NMR structure of a linker-deleted signal peptide of rat liver mitochondrial aldehyde dehydrogenase
    • (1993) J. Biol. Chem. , vol.268 , pp. 19906-19914
    • Thornton, K.1
  • 34
    • 0033215007 scopus 로고    scopus 로고
    • A coil-helix instead of a helix-coil motif can be induced in a chloroplast transit peptide from Chlamydomonas reinhardtii
    • (1999) Eur. J. Biochem. , vol.265 , pp. 171-180
    • Krimm, I.1
  • 35
    • 0034794778 scopus 로고    scopus 로고
    • Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase
    • (2001) Plant J. , vol.27 , pp. 427-438
    • Zhang, X.P.1
  • 39
    • 0027949375 scopus 로고
    • MSF, a novel cytoplasmic chaperone which functions in precursor targeting to mitochondria
    • (1994) EMBO J. , vol.13 , pp. 5146-5154
    • Hachiya, N.1
  • 40
    • 0030049440 scopus 로고    scopus 로고
    • Binding of mitochondrial presequences to yeast cytosolic heat shock protein 70 depends on the amphiphilicity of the presequence
    • (1996) J. Biol. Chem. , vol.271 , pp. 4161-4167
    • Endo, T.1
  • 41
    • 0028808103 scopus 로고
    • Structural features of the precursor to mitochondrial aspartate aminotransferase responsible for binding to Hsp70
    • (1995) J. Biol. Chem. , vol.270 , pp. 24732-24739
    • Lain, B.1
  • 42
    • 0025872169 scopus 로고
    • Interaction of peptides corresponding to mitochondrial presequences with membranes
    • (1991) J. Biol. Chem. , vol.266 , pp. 21693-21699
    • Hoyt, D.W.1
  • 44
    • 0030769419 scopus 로고    scopus 로고
    • Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70
    • (1997) J. Biol. Chem. , vol.272 , pp. 20730-20735
    • Brix, J.1
  • 45
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of Tom20
    • (2001) Plant Physiol , vol.125 , pp. 943-954
    • Werhahn, W.1
  • 47
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Δψ drives the movement of presequences
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1
  • 48
    • 0025039149 scopus 로고
    • Requirement for Hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1
  • 49
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kD mitochondrial stress protein
    • (1990) EMBO J. , vol.9 , pp. 4315-4322
    • Scherer, P.E.1
  • 52
    • 0028132179 scopus 로고
    • Mitochondrial Hsp70/MIM44 complex facilitates protein import
    • (1994) Nature , vol.371 , pp. 768-774
    • Schneider, H.C.1
  • 53
    • 0023656946 scopus 로고
    • The role of protein structure in the mitochondrial import pathway. Unfolding of mitochondrially bound precursors is required for membrane translocation
    • (1987) J. Biol. Chem. , vol.262 , pp. 15605-15609
    • Chen, W.J.1    Douglas, M.G.2
  • 54
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • (1997) EMBO J. , vol.16 , pp. 6727-6736
    • Matouschek, A.1
  • 55
    • 0034328890 scopus 로고    scopus 로고
    • Protein unfolding by mitochondria. The Hsp70 import motor
    • (2000) EMBO Rep. , vol.1 , pp. 404-410
    • Matouschek, A.1
  • 56
    • 0032708369 scopus 로고    scopus 로고
    • Mitochondria unfold precursor proteins by unraveling them from their N-termini
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1132-1138
    • Huang, S.1
  • 57
    • 0026450340 scopus 로고
    • Characterisation of PHSP1, a cDNA encoding a mitochondrial HSP70 from Pisum sativum
    • (1992) Plant Mol. Biol. , vol.18 , pp. 23-32
    • Watts, F.Z.1
  • 60
    • 0027523621 scopus 로고
    • The transit sequence mediates the specific interaction of the precursor of ferredoxin with chloroplast envelope membrane lipids
    • (1993) J. Biol. Chem. , vol.268 , pp. 4037-4042
    • Van't Hof, R.1
  • 61
    • 0030472762 scopus 로고    scopus 로고
    • In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent
    • (1996) J. Biol. Chem. , vol.271 , pp. 32907-32915
    • Pinnaduwage, P.1    Bruce, B.D.2
  • 65
    • 0028109712 scopus 로고
    • Isolation of components of the chloroplast protein import machinery
    • (1994) Science , vol.266 , pp. 1007-1012
    • Schnell, D.J.1
  • 68
    • 0024978279 scopus 로고
    • Internal ATP is the only energy requirement for the translocation of precursor proteins across chloroplastic membranes
    • (1989) J. Biol. Chem. , vol.264 , pp. 6730-6736
    • Theg, S.M.1
  • 69
    • 0026803387 scopus 로고
    • New insights into the import mechanism of the ferredoxin precursor into chloroplasts
    • (1992) J. Biol. Chem. , vol.267 , pp. 2548-2556
    • Pilon, M.1
  • 70
    • 0030067134 scopus 로고    scopus 로고
    • A new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: Energetics and mechanistic implications
    • (1996) J. Cell Biol. , vol.132 , pp. 63-75
    • Scott, S.V.1    Theg, S.M.2
  • 71
    • 0030896924 scopus 로고    scopus 로고
    • Identification of protein transport complexes in the chloroplastic envelope membranes via chemical cross-linking
    • (1997) J. Cell Biol. , vol.136 , pp. 983-994
    • Akita, M.1
  • 72
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • (1997) EMBO J. , vol.16 , pp. 935-946
    • Nielsen, E.1
  • 79
    • 0033996510 scopus 로고    scopus 로고
    • Identification of a Hsp70 recognition domain within the Rubisco small subunit transit peptide
    • (2000) Plant Physiol. , vol.122 , pp. 1289-1299
    • Ivey, R.A.1
  • 80
    • 0033781954 scopus 로고    scopus 로고
    • Interaction of the targeting sequence of chloroplast precursors with Hsp70 molecular chaperones
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6239-6248
    • Rial, D.V.1
  • 82
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1
  • 83
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 85
    • 0027401683 scopus 로고
    • Three-dimensional models of four mouse mast cell chymases. Identification of proteoglycan binding regions and protease-specific antigenic epitopes
    • (1993) J. Biol. Chem. , vol.268 , pp. 9023-9034
    • Šali, A.1


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