메뉴 건너뛰기




Volumn 207, Issue 4, 1999, Pages 624-627

Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the ΔpH-dependent pathway

Author keywords

Arabidopsis (protein transport); Chloro plast; Protein transport; Targeting signal; Thylakoid lumen

Indexed keywords

ALPHA ALLOPHYCOCYANIN; CARBOXY TERMINAL SEQUENCE; COMPLEMENTARY DNA; HYDROPHOBICITY; PH; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN SYNTHESIS; PROTEIN TARGETING; PROTEIN TRANSLOCASE; THYLAKOID;

EID: 0033082633     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050527     Document Type: Article
Times cited : (5)

References (23)
  • 1
    • 0030310296 scopus 로고
    • Fast protein fold recognition via sequence to structure alignment and contact capacity potentials
    • Hunter L, Klein TE (eds), World Scientific Publishing Co., Singapore
    • Alexandrov NN, Nussinov R, Zimmer RM (1995) Fast protein fold recognition via sequence to structure alignment and contact capacity potentials. In: Hunter L, Klein TE (eds) Pacific Symposium on Biocomputing '96, World Scientific Publishing Co., Singapore, pp 53-72
    • (1995) Pacific Symposium on Biocomputing '96 , pp. 53-72
    • Alexandrov, N.N.1    Nussinov, R.2    Zimmer, R.M.3
  • 2
    • 0026316318 scopus 로고
    • Transport of proteins into chloroplasts: Delineation of envelope transit and thylakoid transfer signals within the presequences of three imported thylakoid lumen proteins
    • Bassham DC. Bartling D, Mould RM, Dunbar B, Weisbeek P, Hermann RG, Robinson C (1991) Transport of proteins into chloroplasts: delineation of envelope transit and thylakoid transfer signals within the presequences of three imported thylakoid lumen proteins. J Biol Chem 266: 23606-23610
    • (1991) J Biol Chem , vol.266 , pp. 23606-23610
    • Bassham, D.C.1    Bartling, D.2    Mould, R.M.3    Dunbar, B.4    Weisbeek, P.5    Hermann, R.G.6    Robinson, C.7
  • 3
    • 0030976930 scopus 로고    scopus 로고
    • Pathway specificity for a ΔpH-dependcnt precursor thylakoid lumen protein is governed by a "Sec-avoidance" motif in the transfer peptidc and a "Sec-incompatible" mature protein
    • Bogsch E, Brink S, Robinson C (1997) Pathway specificity for a ΔpH-dependcnt precursor thylakoid lumen protein is governed by a "Sec-avoidance" motif in the transfer peptidc and a "Sec-incompatible" mature protein. EMBO J 16: 3851-3858
    • (1997) EMBO J , vol.16 , pp. 3851-3858
    • Bogsch, E.1    Brink, S.2    Robinson, C.3
  • 4
    • 0032435519 scopus 로고    scopus 로고
    • Targeting of thylakoid proteins by the ΔpH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the twin-arginine motif
    • Brink S, Bogsch EG, Edwards WR, Hynds PJ, Robinson C (1998) Targeting of thylakoid proteins by the ΔpH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the twin-arginine motif. FEBS Letts 434: 425-430
    • (1998) FEBS Letts , vol.434 , pp. 425-430
    • Brink, S.1    Bogsch, E.G.2    Edwards, W.R.3    Hynds, P.J.4    Robinson, C.5
  • 5
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase
    • Chaddock AM, Mant A, Karnauchov I, Brink S, Herrmann RG, Klösgen RB, Robinson C (1995) A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the ΔpH-dependent thylakoidal protein translocase. EMBO J 14: 2715-2722
    • (1995) EMBO J , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchov, I.3    Brink, S.4    Herrmann, R.G.5    Klösgen, R.B.6    Robinson, C.7
  • 6
    • 0026787702 scopus 로고
    • Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP
    • Cline K, Ettigner WF, Theg SM (1992) Protein-specific energy requirements for protein transport across or into thylakoid membranes. Two lumenal proteins are transported in the absence of ATP. J Biol Chem 267: 2688-2696
    • (1992) J Biol Chem , vol.267 , pp. 2688-2696
    • Cline, K.1    Ettigner, W.F.2    Theg, S.M.3
  • 7
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline K, Henry R, Li C, Yuan J (1993) Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J 12: 1405-4114
    • (1993) EMBO J , vol.12 , pp. 1405-4114
    • Cline, K.1    Henry, R.2    Li, C.3    Yuan, J.4
  • 8
    • 0032536779 scopus 로고    scopus 로고
    • A novel multifunctional chloroplast protein: Identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen
    • Fulgosi H, Vener A, Altschmied L, Herrmann RG, Andersson B (1998) A novel multifunctional chloroplast protein: identification of a 40 kDa immunophilin-like protein located in the thylakoid lumen. EMBO J 17: 1577-1587
    • (1998) EMBO J , vol.17 , pp. 1577-1587
    • Fulgosi, H.1    Vener, A.2    Altschmied, L.3    Herrmann, R.G.4    Andersson, B.5
  • 9
    • 0028290813 scopus 로고
    • Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport
    • Henry R, Kapazoglou A, McCaffery M, Cline K (1994) Differences between lumen targeting domains of chloroplast transit peptides determine pathway specificity for thylakoid transport. J Biol Chem 269: 10189-10192
    • (1994) J Biol Chem , vol.269 , pp. 10189-10192
    • Henry, R.1    Kapazoglou, A.2    McCaffery, M.3    Cline, K.4
  • 10
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard JW, Kendall DA (1994) Signal peptides: exquisitely designed transport promoters. Mol Microbiol 13: 765-773
    • (1994) Mol Microbiol , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 11
    • 0032549515 scopus 로고    scopus 로고
    • The thylakoid lumen of chloroplasts: Isolation and characterisation
    • Kieselbach T, Hagman A, Andersson B, Schröder WP (1998) The thylakoid lumen of chloroplasts: isolation and characterisation. J Biol Chem 273: 6710-6716
    • (1998) J Biol Chem , vol.273 , pp. 6710-6716
    • Kieselbach, T.1    Hagman, A.2    Andersson, B.3    Schröder, W.P.4
  • 12
    • 0028365045 scopus 로고
    • The SecA inhibitor, azide, reversibly blocks the translocation of a subset of lumenal proteins across the thylakoid membrane
    • Knott TG, Robinson C (1994) The SecA inhibitor, azide, reversibly blocks the translocation of a subset of lumenal proteins across the thylakoid membrane. J Biol Chem 269: 7843-7846
    • (1994) J Biol Chem , vol.269 , pp. 7843-7846
    • Knott, T.G.1    Robinson, C.2
  • 13
    • 0025781325 scopus 로고
    • A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane
    • Mould RM, Robinson C (1991) A proton gradient is required for the transport of two lumenal oxygen-evolving proteins across the thylakoid membrane. J Biol Chem 266: 12189-12193
    • (1991) J Biol Chem , vol.266 , pp. 12189-12193
    • Mould, R.M.1    Robinson, C.2
  • 14
    • 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, 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
  • 15
    • 0028169710 scopus 로고
    • Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate cleavage site: Role of the ΔpH in translocation across the thylakoid membrane
    • Nielsen VS, Mant A, Knoetzel J, Møller BL, Robinson C (1994) Import of barley photosystem I subunit N into the thylakoid lumen is mediated by a bipartite presequence lacking an intermediate cleavage site: role of the ΔpH in translocation across the thylakoid membrane. J Biol Chem 269: 3762-3766
    • (1994) J Biol Chem , vol.269 , pp. 3762-3766
    • Nielsen, V.S.1    Mant, A.2    Knoetzel, J.3    Møller, B.L.4    Robinson, C.5
  • 16
    • 0027980013 scopus 로고
    • The presequence of a chimeric construct dictates which of two mechanisms is utitlised for translocation across the thylakoid membrane: Evidence for the existence of two distinct translocation systems
    • Robinson C, Cai D, Hulford A, Brock IW, Michl D, Hazell L, Schmidt I, Herrmann RG, Klösgen RB (1994) The presequence of a chimeric construct dictates which of two mechanisms is utitlised for translocation across the thylakoid membrane: evidence for the existence of two distinct translocation systems. EMBO J 13: 279-285
    • (1994) EMBO J , vol.13 , pp. 279-285
    • Robinson, C.1    Cai, D.2    Hulford, A.3    Brock, I.W.4    Michl, D.5    Hazell, L.6    Schmidt, I.7    Herrmann, R.G.8    Klösgen, R.B.9
  • 17
    • 0030826871 scopus 로고    scopus 로고
    • Targeting of proteins into and across the thylakoid membrane
    • Robinson C, Mant A (1997) Targeting of proteins into and across the thylakoid membrane. Trends Plant Sci 2: 431-437
    • (1997) Trends Plant Sci , vol.2 , pp. 431-437
    • Robinson, C.1    Mant, A.2
  • 18
    • 0025830411 scopus 로고
    • The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton JB, Robinson C (1991) The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. J Biol Chem 266: 12152-12156
    • (1991) J Biol Chem , vol.266 , pp. 12152-12156
    • Shackleton, J.B.1    Robinson, C.2
  • 19
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B, Sander C (1993) Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 232: 584-599
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 20
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19: 55-77
    • (1994) Proteins , vol.19 , pp. 55-77
    • Rost, B.1    Sander, C.2
  • 22
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G, Steppuhn J, Herrmann RG (1989) Domain structure of mitochondrial and chloroplast targeting peptides. Eur J Biochem 180: 535-545
    • (1989) Eur J Biochem , vol.180 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 23
    • 0027961026 scopus 로고
    • SecA homolog in protein transport within chloroplasts: Evidence for endosymbiont-derived sorting
    • Yuan J, Henry R, McCaffery M, Cline K (1994) SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting. Science 266: 796-798
    • (1994) Science , vol.266 , pp. 796-798
    • Yuan, J.1    Henry, R.2    McCaffery, M.3    Cline, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.