메뉴 건너뛰기




Volumn 89, Issue 12, 2010, Pages 965-973

Component interactions, regulation and mechanisms of chloroplast signal recognition particle-dependent protein transport

Author keywords

Alb3; Chloroplast; LHCP; Protein transport; Signal recognition particle; SRP GTPases; SRP RNA; Thylakoid membrane

Indexed keywords

BINDING PROTEIN; CHLOROPHYLL; MEMBRANE PROTEIN; SIGNAL RECOGNITION PARTICLE;

EID: 78149406333     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2010.06.020     Document Type: Short Survey
Times cited : (49)

References (122)
  • 1
    • 60349103651 scopus 로고    scopus 로고
    • Protein transport in organelles: the Toc complex way of preprotein import
    • Agne B., Kessler F Protein transport in organelles: the Toc complex way of preprotein import. FEBS J 2009, 276:1156-1165.
    • (2009) FEBS J , vol.276 , pp. 1156-1165
    • Agne, B.1    Kessler, F.2
  • 2
    • 67650330566 scopus 로고    scopus 로고
    • Conformational change of Escherichia coli signal recognition particle Ffh is affected by the functionality of signal peptides of ribose-binding protein
    • Ahn T., Ko J.H., Cho E.Y., Yun C.H. Conformational change of Escherichia coli signal recognition particle Ffh is affected by the functionality of signal peptides of ribose-binding protein. Mol Cells 2009, 27:681-687.
    • (2009) Mol Cells , vol.27 , pp. 681-687
    • Ahn, T.1    Ko, J.H.2    Cho, E.Y.3    Yun, C.H.4
  • 3
    • 60349123961 scopus 로고    scopus 로고
    • Protein transport in organelles: protein transport into and across the thylakoid membrane
    • Aldridge C., Cain P., Robinson C. Protein transport in organelles: protein transport into and across the thylakoid membrane. FEBS J 2009, 276:1177-1186.
    • (2009) FEBS J , vol.276 , pp. 1177-1186
    • Aldridge, C.1    Cain, P.2    Robinson, C.3
  • 4
    • 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., Hoffman N.E. Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes. Plant Physiol 1999, 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
  • 5
    • 20044388542 scopus 로고    scopus 로고
    • FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon
    • Angelini S., Deitermann S., Koch H.G. FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon. EMBO Rep 2005, 6:476-481.
    • (2005) EMBO Rep , vol.6 , pp. 476-481
    • Angelini, S.1    Deitermann, S.2    Koch, H.G.3
  • 6
    • 57549094142 scopus 로고    scopus 로고
    • Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis
    • Asakura Y., Kikuchi S., Nakai M. Non-identical contributions of two membrane-bound cpSRP components, cpFtsY and Alb3, to thylakoid biogenesis. Plant J 2008, 56:1007-1017.
    • (2008) Plant J , vol.56 , pp. 1007-1017
    • Asakura, Y.1    Kikuchi, S.2    Nakai, M.3
  • 7
    • 36049049032 scopus 로고    scopus 로고
    • Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY
    • Bahari L., Parlitz R., Eitan A., Stjepanovic G., Bochkareva E.S., Sinning I., Bibi E. Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY. J Biol Chem 2007, 282:32168-32175.
    • (2007) J Biol Chem , vol.282 , pp. 32168-32175
    • Bahari, L.1    Parlitz, R.2    Eitan, A.3    Stjepanovic, G.4    Bochkareva, E.S.5    Sinning, I.6    Bibi, E.7
  • 8
    • 66449120007 scopus 로고    scopus 로고
    • Crystallisation, structure and function of plant light-harvesting Complex II
    • Barros T., Kühlbrandt W. Crystallisation, structure and function of plant light-harvesting Complex II. Biochim Biophys Acta 2009, 1787:753-772.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 753-772
    • Barros, T.1    Kühlbrandt, W.2
  • 9
    • 0034681490 scopus 로고    scopus 로고
    • Crystal structure of the ribonucleoprotein core of the signal recognition particle
    • Batey R.T., Rambo R.P., Lucast L., Rha B., Doudna J.A. Crystal structure of the ribonucleoprotein core of the signal recognition particle. Science 2000, 287:1232-1239.
    • (2000) Science , vol.287 , pp. 1232-1239
    • Batey, R.T.1    Rambo, R.P.2    Lucast, L.3    Rha, B.4    Doudna, J.A.5
  • 10
    • 0036737470 scopus 로고    scopus 로고
    • Loss of Albino3 leads to the specific depletion of the light-harvesting system
    • Bellafiore S., Ferris P., Naver H., Gohre V., Rochaix J.D. Loss of Albino3 leads to the specific depletion of the light-harvesting system. Plant Cell 2002, 14:2303-2314.
    • (2002) Plant Cell , vol.14 , pp. 2303-2314
    • Bellafiore, S.1    Ferris, P.2    Naver, H.3    Gohre, V.4    Rochaix, J.D.5
  • 11
    • 60349119636 scopus 로고    scopus 로고
    • Protein transport in organelles: the composition, function and regulation of the Tic complex in chloroplast protein import
    • Benz J.P., Soll J., Bolter B. Protein transport in organelles: the composition, function and regulation of the Tic complex in chloroplast protein import. FEBS J 2009, 276:1166-1176.
    • (2009) FEBS J , vol.276 , pp. 1166-1176
    • Benz, J.P.1    Soll, J.2    Bolter, B.3
  • 12
    • 71249147710 scopus 로고    scopus 로고
    • Alb4 of Arabidopsis promotes assembly and stabilization of a non chlorophyll-binding photosynthetic complex, the CF1CF0-ATP synthase
    • Benz M., Bals T., Gugel I.L., Piotrowski M., Kuhn A., Schünemann D., Soll J., Ankele E. Alb4 of Arabidopsis promotes assembly and stabilization of a non chlorophyll-binding photosynthetic complex, the CF1CF0-ATP synthase. Mol Plant 2009, 2:1410-1424.
    • (2009) Mol Plant , vol.2 , pp. 1410-1424
    • Benz, M.1    Bals, T.2    Gugel, I.L.3    Piotrowski, M.4    Kuhn, A.5    Schünemann, D.6    Soll, J.7    Ankele, E.8
  • 13
    • 58149264965 scopus 로고    scopus 로고
    • Signal sequences activate the catalytic switch of SRP RNA
    • Bradshaw N., Neher S.B., Booth D.S., Walter P. Signal sequences activate the catalytic switch of SRP RNA. Science 2009, 323:127-130.
    • (2009) Science , vol.323 , pp. 127-130
    • Bradshaw, N.1    Neher, S.B.2    Booth, D.S.3    Walter, P.4
  • 14
    • 34347399347 scopus 로고    scopus 로고
    • The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting
    • Bradshaw N., Walter P. The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting. Mol Biol Cell 2007, 18:2728-2734.
    • (2007) Mol Biol Cell , vol.18 , pp. 2728-2734
    • Bradshaw, N.1    Walter, P.2
  • 15
    • 0021645935 scopus 로고
    • The 4.5 S RNA gene of Escherichia coli is essential for cell growth
    • Brown S., Fournier M.J. The 4.5 S RNA gene of Escherichia coli is essential for cell growth. J Mol Biol 1984, 178:533-550.
    • (1984) J Mol Biol , vol.178 , pp. 533-550
    • Brown, S.1    Fournier, M.J.2
  • 16
    • 36549025508 scopus 로고    scopus 로고
    • Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction
    • Chandrasekar S., Chartron J., Jaru-Ampornpan P., Shan S.O. Structure of the chloroplast signal recognition particle (SRP) receptor: domain arrangement modulates SRP-receptor interaction. J Mol Biol 2008, 375:425-436.
    • (2008) J Mol Biol , vol.375 , pp. 425-436
    • Chandrasekar, S.1    Chartron, J.2    Jaru-Ampornpan, P.3    Shan, S.O.4
  • 17
  • 20
    • 0034652118 scopus 로고    scopus 로고
    • A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts
    • DeLille J., Peterson E.C., Johnson T., Moore M., Kight A., Henry R. A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts. Proc Natl Acad Sci USA 2000, 97:1926-1931.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1926-1931
    • DeLille, J.1    Peterson, E.C.2    Johnson, T.3    Moore, M.4    Kight, A.5    Henry, R.6
  • 21
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • Egea P.F., Shan S.O., Napetschnig J., Savage D.F., Walter P., Stroud R.M. Substrate twinning activates the signal recognition particle and its receptor. Nature 2004, 427:215-221.
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1    Shan, S.O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 22
    • 0034124897 scopus 로고    scopus 로고
    • Investigations on gene copy number, introns and chromosomal arrangement of genes encoding the fucoxanthin chlorophyll a/c-binding proteins of the centric diatom Cyclotella cryptica
    • Eppard M., Rhiel E. Investigations on gene copy number, introns and chromosomal arrangement of genes encoding the fucoxanthin chlorophyll a/c-binding proteins of the centric diatom Cyclotella cryptica. Protist 2000, 151:27-39.
    • (2000) Protist , vol.151 , pp. 27-39
    • Eppard, M.1    Rhiel, E.2
  • 23
    • 77949332515 scopus 로고    scopus 로고
    • The C-terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane
    • Falk S., Ravaud S., Koch J., Sinning I. The C-terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. J Biol Chem 2010, 285:5954-5962.
    • (2010) J Biol Chem , vol.285 , pp. 5954-5962
    • Falk, S.1    Ravaud, S.2    Koch, J.3    Sinning, I.4
  • 26
    • 0027377619 scopus 로고
    • Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle
    • Franklin A.E., Hoffman N.E. Characterization of a chloroplast homologue of the 54-kDa subunit of the signal recognition particle. J Biol Chem 1993, 268:22175-22180.
    • (1993) J Biol Chem , vol.268 , pp. 22175-22180
    • Franklin, A.E.1    Hoffman, N.E.2
  • 27
    • 15744389218 scopus 로고    scopus 로고
    • A unique sequence motif in the 54-kDa subunit of the chloroplast signal recognition particle mediates binding to the 43-kDa subunit
    • Funke S., Knechten T., Ollesch J., Schünemann D. A unique sequence motif in the 54-kDa subunit of the chloroplast signal recognition particle mediates binding to the 43-kDa subunit. J Biol Chem 2005, 280:8912-8917.
    • (2005) J Biol Chem , vol.280 , pp. 8912-8917
    • Funke, S.1    Knechten, T.2    Ollesch, J.3    Schünemann, D.4
  • 29
    • 33745207364 scopus 로고    scopus 로고
    • A second thylakoid membrane-localized Alb3/OxaI/YidC homologue is involved in proper chloroplast biogenesis in Arabidopsis thaliana
    • Gerdes L., Bals T., Klostermann E., Karl M., Philippar K., Hunken M., Soll J., Schünemann D. A second thylakoid membrane-localized Alb3/OxaI/YidC homologue is involved in proper chloroplast biogenesis in Arabidopsis thaliana. J Biol Chem 2006, 281:16632-16642.
    • (2006) J Biol Chem , vol.281 , pp. 16632-16642
    • Gerdes, L.1    Bals, T.2    Klostermann, E.3    Karl, M.4    Philippar, K.5    Hunken, M.6    Soll, J.7    Schünemann, D.8
  • 30
    • 0030460146 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mitochondria lack a bacterial-type sec machinery
    • Glick B.S., von Heijne G. Saccharomyces cerevisiae mitochondria lack a bacterial-type sec machinery. Protein Sci 1996, 5:2651-2652.
    • (1996) Protein Sci , vol.5 , pp. 2651-2652
    • Glick, B.S.1    von Heijne, G.2
  • 31
    • 5644297077 scopus 로고    scopus 로고
    • Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43
    • Goforth R.L., Peterson E.C., Yuan J., Moore M.J., Kight A.D., Lohse M.B., Sakon J., Henry R.L. Regulation of the GTPase cycle in post-translational signal recognition particle-based protein targeting involves cpSRP43. J Biol Chem 2004, 279:43077-43084.
    • (2004) J Biol Chem , vol.279 , pp. 43077-43084
    • Goforth, R.L.1    Peterson, E.C.2    Yuan, J.3    Moore, M.J.4    Kight, A.D.5    Lohse, M.B.6    Sakon, J.7    Henry, R.L.8
  • 32
    • 33745438296 scopus 로고    scopus 로고
    • One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas
    • Göhre V., Ossenbühl F., Crevecoeur M., Eichacker L.A., Rochaix J.D. One of two alb3 proteins is essential for the assembly of the photosystems and for cell survival in Chlamydomonas. Plant Cell 2006, 18:1454-1466.
    • (2006) Plant Cell , vol.18 , pp. 1454-1466
    • Göhre, V.1    Ossenbühl, F.2    Crevecoeur, M.3    Eichacker, L.A.4    Rochaix, J.D.5
  • 33
    • 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., Sinning I. Functional characterization of recombinant chloroplast signal recognition particle. J Biol Chem 2001, 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
  • 34
    • 70349595267 scopus 로고    scopus 로고
    • Protein targeting by the signal recognition particle
    • Grudnik P., Bange G., Sinning I. Protein targeting by the signal recognition particle. Biol Chem 2009, 390:775-782.
    • (2009) Biol Chem , vol.390 , pp. 775-782
    • Grudnik, P.1    Bange, G.2    Sinning, I.3
  • 35
    • 35448950462 scopus 로고    scopus 로고
    • Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle
    • Hainzl T., Huang S., Sauer-Eriksson A.E. Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle. Proc Natl Acad Sci USA 2007, 104:14911-14916.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14911-14916
    • Hainzl, T.1    Huang, S.2    Sauer-Eriksson, A.E.3
  • 36
    • 33751325296 scopus 로고    scopus 로고
    • Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    • Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I., Beckmann R. Following the signal sequence from ribosomal tunnel exit to signal recognition particle. Nature 2006, 444:507-511.
    • (2006) Nature , vol.444 , pp. 507-511
    • Halic, M.1    Blau, M.2    Becker, T.3    Mielke, T.4    Pool, M.R.5    Wild, K.6    Sinning, I.7    Beckmann, R.8
  • 37
    • 28444498828 scopus 로고    scopus 로고
    • Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2
    • Hasona A., Crowley P.J., Levesque C.M., Mair R.W., Cvitkovitch D.G., Bleiweis A.S., Brady L.J. Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2. Proc Natl Acad Sci USA 2005, 102:17466-17471.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17466-17471
    • Hasona, A.1    Crowley, P.J.2    Levesque, C.M.3    Mair, R.W.4    Cvitkovitch, D.G.5    Bleiweis, A.S.6    Brady, L.J.7
  • 38
    • 0032478139 scopus 로고    scopus 로고
    • Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
    • Hell K., Herrmann J.M., Pratje E., Neupert W., Stuart R.A. Oxa1p, an essential component of the N-tail protein export machinery in mitochondria. Proc Natl Acad Sci USA 1998, 95:2250-2255.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2250-2255
    • Hell, K.1    Herrmann, J.M.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 39
    • 0035868763 scopus 로고    scopus 로고
    • Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA
    • Hell K., Neupert W., Stuart R.A. Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA. EMBO J 2001, 20:1281-1288.
    • (2001) EMBO J , vol.20 , pp. 1281-1288
    • Hell, K.1    Neupert, W.2    Stuart, R.A.3
  • 41
    • 33646577139 scopus 로고    scopus 로고
    • The alpha-helix of the second chromodomain of the 43kDa subunit of the chloroplast signal recognition particle facilitates binding to the 54kDa subunit
    • Hermkes R., Funke S., Richter C., Kuhlmann J., Schünemann D. The alpha-helix of the second chromodomain of the 43kDa subunit of the chloroplast signal recognition particle facilitates binding to the 54kDa subunit. FEBS Lett 2006, 580:3107-3111.
    • (2006) FEBS Lett , vol.580 , pp. 3107-3111
    • Hermkes, R.1    Funke, S.2    Richter, C.3    Kuhlmann, J.4    Schünemann, D.5
  • 43
    • 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., Franklin A.E. Evidence for a stromal GTP requirement for the integration of a chlorophyll a/b-binding polypeptide into thylakoid membranes. Plant Physiol 1994, 105:295-304.
    • (1994) Plant Physiol , vol.105 , pp. 295-304
    • Hoffman, N.E.1    Franklin, A.E.2
  • 44
    • 36849007028 scopus 로고    scopus 로고
    • Chlorophylls, ligands and assembly of light-harvesting complexes in chloroplasts
    • Hoober J.K., Eggink L.L., Chen M. Chlorophylls, ligands and assembly of light-harvesting complexes in chloroplasts. Photosynth Res 2007, 94:387-400.
    • (2007) Photosynth Res , vol.94 , pp. 387-400
    • Hoober, J.K.1    Eggink, L.L.2    Chen, M.3
  • 45
    • 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., Nussaume L. Double mutation cpSRP43--/cpSRP54-- is necessary to abolish the cpSRP pathway required for thylakoid targeting of the light-harvesting chlorophyll proteins. Plant J 2002, 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
  • 46
    • 34347374732 scopus 로고    scopus 로고
    • Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA
    • Jaru-Ampornpan P., Chandrasekar S., Shan S.O. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. Mol Biol Cell 2007, 18:2636-2645.
    • (2007) Mol Biol Cell , vol.18 , pp. 2636-2645
    • Jaru-Ampornpan, P.1    Chandrasekar, S.2    Shan, S.O.3
  • 47
    • 70349315419 scopus 로고    scopus 로고
    • A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway
    • Jaru-Ampornpan P., Nguyen T.X., Shan S.O. A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway. Mol Biol Cell 2009, 20:3965-3973.
    • (2009) Mol Biol Cell , vol.20 , pp. 3965-3973
    • Jaru-Ampornpan, P.1    Nguyen, T.X.2    Shan, S.O.3
  • 48
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • Jarvis P. Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol 2008, 179:257-285.
    • (2008) New Phytol , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 49
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1
    • Jia L., Dienhart M., Schramp M., McCauley M., Hell K., Stuart R.A. Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1. EMBO J 2003, 22:6438-6447.
    • (2003) EMBO J , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 50
    • 34248138912 scopus 로고    scopus 로고
    • Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex
    • Jia L., Dienhart M.K., Stuart R.A. Oxa1 directly interacts with Atp9 and mediates its assembly into the mitochondrial F1Fo-ATP synthase complex. Mol Biol Cell 2007, 18:1897-1908.
    • (2007) Mol Biol Cell , vol.18 , pp. 1897-1908
    • Jia, L.1    Dienhart, M.K.2    Stuart, R.A.3
  • 51
    • 0035816712 scopus 로고    scopus 로고
    • Functional analysis of the protein-interacting domains of chloroplast SRP43
    • Jonas-Straube E., Hutin C., Hoffman N.E., Schünemann D. Functional analysis of the protein-interacting domains of chloroplast SRP43. J Biol Chem 2001, 276:24654-24660.
    • (2001) J Biol Chem , vol.276 , pp. 24654-24660
    • Jonas-Straube, E.1    Hutin, C.2    Hoffman, N.E.3    Schünemann, D.4
  • 54
    • 0037115768 scopus 로고    scopus 로고
    • The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
    • Klostermann E., Droste Gen Helling I., Carde J.P., Schünemann D. The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana. Biochem J 2002, 368:777-781.
    • (2002) Biochem J , vol.368 , pp. 777-781
    • Klostermann, E.1    Droste Gen Helling, I.2    Carde, J.P.3    Schünemann, D.4
  • 55
    • 0032973271 scopus 로고    scopus 로고
    • Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakoids
    • Kogata N., Nishio K., Hirohashi T., Kikuchi S., Nakai M. Involvement of a chloroplast homologue of the signal recognition particle receptor protein, FtsY, in protein targeting to thylakoids. FEBS Lett 1999, 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
  • 58
    • 34249814314 scopus 로고    scopus 로고
    • Tracing the evolution of the light-harvesting antennae in chlorophyll a/b-containing organisms
    • Koziol A.G., Borza T., Ishida K., Keeling P., Lee R.W., Durnford D.G. Tracing the evolution of the light-harvesting antennae in chlorophyll a/b-containing organisms. Plant Physiol 2007, 143:1802-1816.
    • (2007) Plant Physiol , vol.143 , pp. 1802-1816
    • Koziol, A.G.1    Borza, T.2    Ishida, K.3    Keeling, P.4    Lee, R.W.5    Durnford, D.G.6
  • 59
    • 70349459701 scopus 로고    scopus 로고
    • From the Sec complex to the membrane insertase YidC
    • Kuhn A. From the Sec complex to the membrane insertase YidC. Biol Chem 2009, 390:701-706.
    • (2009) Biol Chem , vol.390 , pp. 701-706
    • Kuhn, A.1
  • 60
    • 0347157958 scopus 로고    scopus 로고
    • The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?
    • Kuhn A., Stuart R., Henry R., Dalbey R.E. The Alb3/Oxa1/YidC protein family: membrane-localized chaperones facilitating membrane protein insertion?. Trends Cell Biol 2003, 13:510-516.
    • (2003) Trends Cell Biol , vol.13 , pp. 510-516
    • Kuhn, A.1    Stuart, R.2    Henry, R.3    Dalbey, R.E.4
  • 61
    • 15844397001 scopus 로고    scopus 로고
    • Identification of a region of Bacillus subtilis Ffh, a homologue of mammalian SRP54 protein, that is essential for binding to small cytoplasmic RNA
    • Kurita K., Honda K., Suzuma S., Takamatsu H., Nakamura K., Yamane K. Identification of a region of Bacillus subtilis Ffh, a homologue of mammalian SRP54 protein, that is essential for binding to small cytoplasmic RNA. J Biol Chem 1996, 271:13140-13146.
    • (1996) J Biol Chem , vol.271 , pp. 13140-13146
    • Kurita, K.1    Honda, K.2    Suzuma, S.3    Takamatsu, H.4    Nakamura, K.5    Yamane, K.6
  • 63
    • 67649354632 scopus 로고    scopus 로고
    • The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity
    • Marty N.J., Rajalingam D., Kight A.D., Lewis N.E., Fologea D., Kumar T.K., Henry R.L., Goforth R.L. The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity. J Biol Chem 2009, 284:14891-14903.
    • (2009) J Biol Chem , vol.284 , pp. 14891-14903
    • Marty, N.J.1    Rajalingam, D.2    Kight, A.D.3    Lewis, N.E.4    Fologea, D.5    Kumar, T.K.6    Henry, R.L.7    Goforth, R.L.8
  • 64
    • 71049179930 scopus 로고    scopus 로고
    • Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor
    • Mircheva M., Boy D., Weiche B., Hucke F., Graumann P., Koch H.G. Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor. BMC Biol 2009, 7:76.
    • (2009) BMC Biol , vol.7 , pp. 76
    • Mircheva, M.1    Boy, D.2    Weiche, B.3    Hucke, F.4    Graumann, P.5    Koch, H.G.6
  • 65
    • 0141530036 scopus 로고    scopus 로고
    • Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required
    • Moore M., Goforth R.L., Mori H., Henry R. Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required. J Cell Biol 2003, 162:1245-1254.
    • (2003) J Cell Biol , vol.162 , pp. 1245-1254
    • Moore, M.1    Goforth, R.L.2    Mori, H.3    Henry, R.4
  • 66
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxa1p 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.C., Henry R. Chloroplast Oxa1p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J Biol Chem 2000, 275:1529-1532.
    • (2000) J Biol Chem , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, M.S.2    Peterson, E.C.3    Henry, R.4
  • 67
    • 0033549567 scopus 로고    scopus 로고
    • Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways
    • Mori H., Summer E.J., Ma X., Cline K. Component specificity for the thylakoidal Sec and Delta pH-dependent protein transport pathways. J Cell Biol 1999, 146:45-56.
    • (1999) J Cell Biol , vol.146 , pp. 45-56
    • Mori, H.1    Summer, E.J.2    Ma, X.3    Cline, K.4
  • 68
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., Cammett T.J., Desrosiers D.C., Peng Z.Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci 2004, 13:1435-1448.
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 69
    • 0030845258 scopus 로고    scopus 로고
    • The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain
    • Moser C., Mol O., Goody R.S., Sinning I. The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain. Proc Natl Acad Sci USA 1997, 94:11339-11344.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11339-11344
    • Moser, C.1    Mol, O.2    Goody, R.S.3    Sinning, I.4
  • 70
    • 0035173051 scopus 로고    scopus 로고
    • Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway
    • Mutka S.C., Walter P. Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol Biol Cell 2001, 12:577-588.
    • (2001) Mol Biol Cell , vol.12 , pp. 577-588
    • Mutka, S.C.1    Walter, P.2
  • 71
    • 51349165658 scopus 로고    scopus 로고
    • SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction
    • Neher S.B., Bradshaw N., Floor S.N., Gross J.D., Walter P. SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction. Nat Struct Mol Biol 2008, 15:916-923.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 916-923
    • Neher, S.B.1    Bradshaw, N.2    Floor, S.N.3    Gross, J.D.4    Walter, P.5
  • 72
    • 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., van Wijk K.J. Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54. EMBO J 1999, 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
  • 73
    • 0037205751 scopus 로고    scopus 로고
    • Transient interaction of cpSRP54 with elongating nascent chains of the chloroplast-encoded D1 protein; 'cpSRP54 caught in the act'
    • Nilsson R., van Wijk K.J. Transient interaction of cpSRP54 with elongating nascent chains of the chloroplast-encoded D1 protein; 'cpSRP54 caught in the act'. FEBS Lett 2002, 524:127-133.
    • (2002) FEBS Lett , vol.524 , pp. 127-133
    • Nilsson, R.1    van Wijk, K.J.2
  • 74
    • 0030590083 scopus 로고    scopus 로고
    • Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway
    • Nohara T., Asai T., Nakai M., Sugiura M., Endo T. Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway. Biochem Biophys Res Commun 1996, 224:474-478.
    • (1996) Biochem Biophys Res Commun , vol.224 , pp. 474-478
    • Nohara, T.1    Asai, T.2    Nakai, M.3    Sugiura, M.4    Endo, T.5
  • 75
    • 49949100960 scopus 로고    scopus 로고
    • Chloroplast SRP takes another road
    • Nussaume L. Chloroplast SRP takes another road. Nat Chem Biol 2008, 4:529-531.
    • (2008) Nat Chem Biol , vol.4 , pp. 529-531
    • Nussaume, L.1
  • 76
    • 3142782909 scopus 로고    scopus 로고
    • Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3. 1p, a homolog of Arabidopsis ALBINO3
    • Ossenbühl F., Göhre V., Meurer J., Krieger-Liszkay A., Rochaix J.D., Eichacker L.A. Efficient assembly of photosystem II in Chlamydomonas reinhardtii requires Alb3. 1p, a homolog of Arabidopsis ALBINO3. Plant Cell 2004, 16:1790-1800.
    • (2004) Plant Cell , vol.16 , pp. 1790-1800
    • Ossenbühl, F.1    Göhre, V.2    Meurer, J.3    Krieger-Liszkay, A.4    Rochaix, J.D.5    Eichacker, L.A.6
  • 77
    • 0031963286 scopus 로고    scopus 로고
    • Algal plastid genomes encode homologues of the SRP-associated RNA
    • Packer J.C., Howe C.J. Algal plastid genomes encode homologues of the SRP-associated RNA. Mol Microbiol 1998, 27:508-510.
    • (1998) Mol Microbiol , vol.27 , pp. 508-510
    • Packer, J.C.1    Howe, C.J.2
  • 78
    • 36148937889 scopus 로고    scopus 로고
    • Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
    • Parlitz R., Eitan A., Stjepanovic G., Bahari L., Bange G., Bibi E., Sinning I. Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J Biol Chem 2007, 282:32176-32184.
    • (2007) J Biol Chem , vol.282 , pp. 32176-32184
    • Parlitz, R.1    Eitan, A.2    Stjepanovic, G.3    Bahari, L.4    Bange, G.5    Bibi, E.6    Sinning, I.7
  • 79
    • 28444458466 scopus 로고    scopus 로고
    • The yeast split-ubiquitin system to study chloroplast membrane protein interactions
    • Pasch J.C., Nickelsen J., Schünemann D. The yeast split-ubiquitin system to study chloroplast membrane protein interactions. Appl Microbiol Biotechnol 2005, 69:440-447.
    • (2005) Appl Microbiol Biotechnol , vol.69 , pp. 440-447
    • Pasch, J.C.1    Nickelsen, J.2    Schünemann, D.3
  • 81
    • 0026794697 scopus 로고
    • The E. coli ffh gene is necessary for viability and efficient protein export
    • Phillips G.J., Silhavy T.J. The E. coli ffh gene is necessary for viability and efficient protein export. Nature 1992, 359:744-746.
    • (1992) Nature , vol.359 , pp. 744-746
    • Phillips, G.J.1    Silhavy, T.J.2
  • 82
    • 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., Hoffman N.E. Expression of a dominant negative form of cpSRP54 inhibits chloroplast biogenesis in Arabidopsis. Plant J 1998, 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
  • 83
    • 18844387083 scopus 로고    scopus 로고
    • Signal recognition particles in chloroplasts, bacteria, yeast and mammals
    • (Review)
    • Pool M.R. Signal recognition particles in chloroplasts, bacteria, yeast and mammals. Mol Membr Biol 2005, 22:3-15. (Review).
    • (2005) Mol Membr Biol , vol.22 , pp. 3-15
    • Pool, M.R.1
  • 84
    • 16844375031 scopus 로고    scopus 로고
    • Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery
    • Preuss M., Ott M., Funes S., Luirink J., Herrmann J.M. Evolution of mitochondrial oxa proteins from bacterial YidC. Inherited and acquired functions of a conserved protein insertion machinery. J Biol Chem 2005, 280:13004-13011.
    • (2005) J Biol Chem , vol.280 , pp. 13004-13011
    • Preuss, M.1    Ott, M.2    Funes, S.3    Luirink, J.4    Herrmann, J.M.5
  • 86
    • 51249104242 scopus 로고    scopus 로고
    • Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA
    • Richter C.V., Träger C., Schünemann D. Evolutionary substitution of two amino acids in chloroplast SRP54 of higher plants cause its inability to bind SRP RNA. FEBS Lett 2008, 582:3223-3229.
    • (2008) FEBS Lett , vol.582 , pp. 3223-3229
    • Richter, C.V.1    Träger, C.2    Schünemann, D.3
  • 87
    • 0035929632 scopus 로고    scopus 로고
    • In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system
    • Röhl T., van Wijk K.J. In vitro reconstitution of insertion and processing of cytochrome f in a homologous chloroplast translation system. J Biol Chem 2001, 276:35465-35472.
    • (2001) J Biol Chem , vol.276 , pp. 35465-35472
    • Röhl, T.1    van Wijk, K.J.2
  • 89
    • 11144351763 scopus 로고    scopus 로고
    • Identification of chloroplast signal recognition particle RNA genes
    • Rosenblad M.A., Samuelsson T. Identification of chloroplast signal recognition particle RNA genes. Plant Cell Physiol 2004, 45:1633-1639.
    • (2004) Plant Cell Physiol , vol.45 , pp. 1633-1639
    • Rosenblad, M.A.1    Samuelsson, T.2
  • 90
    • 55549091437 scopus 로고    scopus 로고
    • Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis
    • Rutschow H., Ytterberg A.J., Friso G., Nilsson R., van Wijk K.J. Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol 2008, 148:156-175.
    • (2008) Plant Physiol , vol.148 , pp. 156-175
    • Rutschow, H.1    Ytterberg, A.J.2    Friso, G.3    Nilsson, R.4    van Wijk, K.J.5
  • 91
    • 1642473879 scopus 로고    scopus 로고
    • Structure and function of the chloroplast signal recognition particle
    • Schünemann D. Structure and function of the chloroplast signal recognition particle. Curr Genet 2004, 44:295-304.
    • (2004) Curr Genet , vol.44 , pp. 295-304
    • Schünemann, D.1
  • 92
    • 34547924871 scopus 로고    scopus 로고
    • Mechanisms of protein import into thylakoids of chloroplasts
    • Schünemann D. Mechanisms of protein import into thylakoids of chloroplasts. Biol Chem 2007, 388:907-915.
    • (2007) Biol Chem , vol.388 , pp. 907-915
    • Schünemann, D.1
  • 93
    • 0033534784 scopus 로고    scopus 로고
    • Functional divergence of the plastid and cytosolic forms of the 54-kDa subunit of signal recognition particle
    • Schünemann D., Amin P., Hoffman N.E. Functional divergence of the plastid and cytosolic forms of the 54-kDa subunit of signal recognition particle. Biochem Biophys Res Commun 1999, 254:253-258.
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 253-258
    • Schünemann, D.1    Amin, P.2    Hoffman, N.E.3
  • 96
    • 67651230544 scopus 로고    scopus 로고
    • Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases
    • Shan S.O., Schmid S.L., Zhang X. Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases. Biochemistry 2009, 48:6696-6704.
    • (2009) Biochemistry , vol.48 , pp. 6696-6704
    • Shan, S.O.1    Schmid, S.L.2    Zhang, X.3
  • 98
    • 33846456974 scopus 로고    scopus 로고
    • SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting
    • Siu F.Y., Spanggord R.J., Doudna J.A. SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting. RNA 2007, 13:240-250.
    • (2007) RNA , vol.13 , pp. 240-250
    • Siu, F.Y.1    Spanggord, R.J.2    Doudna, J.A.3
  • 99
    • 26444574927 scopus 로고    scopus 로고
    • New insights into the nature and phylogeny of prasinophyte antenna proteins: Ostreococcus tauri, a case study
    • Six C., Worden A.Z., Rodriguez F., Moreau H., Partensky F. New insights into the nature and phylogeny of prasinophyte antenna proteins: Ostreococcus tauri, a case study. Mol Biol Evol 2005, 22:2217-2230.
    • (2005) Mol Biol Evol , vol.22 , pp. 2217-2230
    • Six, C.1    Worden, A.Z.2    Rodriguez, F.3    Moreau, H.4    Partensky, F.5
  • 100
    • 70349451648 scopus 로고    scopus 로고
    • Molecular interactions within the plant TOC complex
    • Sommer M.S., Schleiff E. Molecular interactions within the plant TOC complex. Biol Chem 2009, 390:739-744.
    • (2009) Biol Chem , vol.390 , pp. 739-744
    • Sommer, M.S.1    Schleiff, E.2
  • 101
    • 47249160767 scopus 로고    scopus 로고
    • Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43
    • Stengel K.F., Holdermann I., Cain P., Robinson C., Wild K., Sinning I. Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43. Science 2008, 321:253-256.
    • (2008) Science , vol.321 , pp. 253-256
    • Stengel, K.F.1    Holdermann, I.2    Cain, P.3    Robinson, C.4    Wild, K.5    Sinning, I.6
  • 102
    • 36549073183 scopus 로고    scopus 로고
    • The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site
    • Stengel K.F., Holdermann I., Wild K., Sinning I. The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site. FEBS Lett 2007, 581:5671-5676.
    • (2007) FEBS Lett , vol.581 , pp. 5671-5676
    • Stengel, K.F.1    Holdermann, I.2    Wild, K.3    Sinning, I.4
  • 104
    • 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., Coupland G. 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 1997, 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
  • 105
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • Szyrach G., Ott M., Bonnefoy N., Neupert W., Herrmann J.M. Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria. EMBO J 2003, 22:6448-6457.
    • (2003) EMBO J , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 106
    • 77952367483 scopus 로고    scopus 로고
    • The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence
    • Trevino J., Perez N., Sumby P. The 4.5S RNA component of the signal recognition particle is required for group A Streptococcus virulence. Microbiology 2010, 156:1342-1350.
    • (2010) Microbiology , vol.156 , pp. 1342-1350
    • Trevino, J.1    Perez, N.2    Sumby, P.3
  • 107
    • 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., Hoffman N.E. 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 1999, 274:27219-27224.
    • (1999) J Biol Chem , vol.274 , pp. 27219-27224
    • Tu, C.J.1    Schuenemann, D.2    Hoffman, N.E.3
  • 110
    • 35448929095 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Cox18 complements the essential Sec-independent function of Escherichia coli YidC
    • van Bloois E., Koningstein G., Bauerschmitt H., Herrmann J.M., Luirink J. Saccharomyces cerevisiae Cox18 complements the essential Sec-independent function of Escherichia coli YidC. FEBS J 2007, 274:5704-5713.
    • (2007) FEBS J , vol.274 , pp. 5704-5713
    • van Bloois, E.1    Koningstein, G.2    Bauerschmitt, H.3    Herrmann, J.M.4    Luirink, J.5
  • 112
    • 2142705713 scopus 로고    scopus 로고
    • F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
    • van der Laan M., Bechtluft P., Kol S., Nouwen N., Driessen A.J. F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis. J Cell Biol 2004, 165:213-222.
    • (2004) J Cell Biol , vol.165 , pp. 213-222
    • van der Laan, M.1    Bechtluft, P.2    Kol, S.3    Nouwen, N.4    Driessen, A.J.5
  • 113
    • 40649093985 scopus 로고    scopus 로고
    • A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor
    • Weiche B., Burk J., Angelini S., Schiltz E., Thumfart J.O., Koch H.G. A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor. J Mol Biol 2008, 377:761-773.
    • (2008) J Mol Biol , vol.377 , pp. 761-773
    • Weiche, B.1    Burk, J.2    Angelini, S.3    Schiltz, E.4    Thumfart, J.O.5    Koch, H.G.6
  • 114
    • 0027957259 scopus 로고
    • Evidence for a common origin of chloroplasts with light-harvesting complexes of different pigmentation
    • Wolfe G.R., Cunningham F.X., Durnfordt D., Green B.R., Gantt E. Evidence for a common origin of chloroplasts with light-harvesting complexes of different pigmentation. Nature 1994, 367:566-568.
    • (1994) Nature , vol.367 , pp. 566-568
    • Wolfe, G.R.1    Cunningham, F.X.2    Durnfordt, D.3    Green, B.R.4    Gantt, E.5
  • 115
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K., Dalbey R.E. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat Rev Microbiol 2008, 6:234-244.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 116
    • 18844444516 scopus 로고    scopus 로고
    • Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria
    • (Review)
    • Yi L., Dalbey R.E. Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria. Mol Membr Biol 2005, 22:101-111. (Review).
    • (2005) Mol Membr Biol , vol.22 , pp. 101-111
    • Yi, L.1    Dalbey, R.E.2
  • 117
    • 0037200125 scopus 로고    scopus 로고
    • ATP stimulates signal recognition particle (SRP)/FtsY-supported protein integration in chloroplasts
    • Yuan J., Kight A., Goforth R.L., Moore M., Peterson E.C., Sakon J., Henry R. ATP stimulates signal recognition particle (SRP)/FtsY-supported protein integration in chloroplasts. J Biol Chem 2002, 277:32400-32404.
    • (2002) J Biol Chem , vol.277 , pp. 32400-32404
    • Yuan, J.1    Kight, A.2    Goforth, R.L.3    Moore, M.4    Peterson, E.C.5    Sakon, J.6    Henry, R.7
  • 118
    • 0035851097 scopus 로고    scopus 로고
    • A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis
    • Zhang L., Paakkarinen V., Suorsa M., Aro E.M. A SecY homologue is involved in chloroplast-encoded D1 protein biogenesis. J Biol Chem 2001, 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
  • 119
    • 60549083291 scopus 로고    scopus 로고
    • Multiple conformational switches in a GTPase complex control co-translational protein targeting
    • Zhang X., Schaffitzel C., Ban N., Shan S.O. Multiple conformational switches in a GTPase complex control co-translational protein targeting. Proc Natl Acad Sci USA 2009, 106:1754-1759.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1754-1759
    • Zhang, X.1    Schaffitzel, C.2    Ban, N.3    Shan, S.O.4
  • 120
    • 67650280920 scopus 로고    scopus 로고
    • The evolution of YidC/Oxa/Alb3 family in the three domains of life: a phylogenomic analysis
    • Zhang Y.J., Tian H.F., Wen J.F. The evolution of YidC/Oxa/Alb3 family in the three domains of life: a phylogenomic analysis. BMC Evol Biol 2009, 9:137.
    • (2009) BMC Evol Biol , vol.9 , pp. 137
    • Zhang, Y.J.1    Tian, H.F.2    Wen, J.F.3
  • 121
    • 0025601549 scopus 로고
    • The methionine-rich domain of the 54kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence
    • Zopf D., Bernstein H.D., Johnson A.E., Walter P. The methionine-rich domain of the 54kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 1990, 9:4511-4517.
    • (1990) EMBO J , vol.9 , pp. 4511-4517
    • Zopf, D.1    Bernstein, H.D.2    Johnson, A.E.3    Walter, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.