메뉴 건너뛰기




Volumn 80, Issue 4, 2014, Pages 592-603

Plastidic type i signal peptidase 1 is a redox-dependent thylakoidal processing peptidase

Author keywords

Arabidopsis thaliana; disulfide; plastidic type I signal peptidase 1; Plsp1; signal peptidase; thylakoid; thylakoid lumen; thylakoidal processing peptidase

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; COVALENT BONDS; ELECTRON TRANSPORT PROPERTIES; ESCHERICHIA COLI; PLANTS (BOTANY); PROTEINS; REDOX REACTIONS; SUBSTRATES; SULFUR COMPOUNDS; GENE ENCODING; PHOTOSYNTHETIC MEMBRANES;

EID: 84907988941     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12655     Document Type: Article
Times cited : (16)

References (70)
  • 1
    • 84857973737 scopus 로고    scopus 로고
    • Targeting of lumenal proteins across the thylakoid membrane
    • Albiniak, A.M., Baglieri, J., and, Robinson, C., (2012) Targeting of lumenal proteins across the thylakoid membrane. J. Exp. Bot. 63, 1689-1698.
    • (2012) J. Exp. Bot. , vol.63 , pp. 1689-1698
    • Albiniak, A.M.1    Baglieri, J.2    Robinson, C.3
  • 2
    • 0030566823 scopus 로고    scopus 로고
    • Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids
    • Barbrook, A.C., Packer, J.C., and, Howe, C.J., (1996) Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids. FEBS Lett. 398, 198-200.
    • (1996) FEBS Lett. , vol.398 , pp. 198-200
    • Barbrook, A.C.1    Packer, J.C.2    Howe, C.J.3
  • 3
    • 84880348278 scopus 로고    scopus 로고
    • A thioredoxin-like/beta-propeller protein maintains the efficiency of light harvesting in Arabidopsis
    • Brooks, M.D., Sylak-Glassman, E.J., Fleming, G.R., and, Niyogi, K.K., (2013) A thioredoxin-like/beta-propeller protein maintains the efficiency of light harvesting in Arabidopsis. Proc. Natl Acad. Sci. USA, 110, E2733-E2740.
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E2733-E2740
    • Brooks, M.D.1    Sylak-Glassman, E.J.2    Fleming, G.R.3    Niyogi, K.K.4
  • 4
    • 84871734172 scopus 로고    scopus 로고
    • Intra-plastid protein trafficking: How plant cells adapted prokaryotic mechanisms to the eukaryotic condition
    • Celedon, J.M., and, Cline, K., (2013) Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition. Biochim. Biophys. Acta, 1833, 341-351.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 341-351
    • Celedon, J.M.1    Cline, K.2
  • 5
    • 0031975202 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme
    • Chaal, B.K., Mould, R.M., Barbrook, A.C., Gray, J.C., and, Howe, C.J., (1998) Characterization of a cDNA encoding the thylakoidal processing peptidase from Arabidopsis thaliana. Implications for the origin and catalytic mechanism of the enzyme. J. Biol. Chem. 273, 689-692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 689-692
    • Chaal, B.K.1    Mould, R.M.2    Barbrook, A.C.3    Gray, J.C.4    Howe, C.J.5
  • 6
    • 0028986871 scopus 로고
    • Determination of Km and kcat for signal peptidase i using a full length secretory precursor, Pro-OmpA-nuclease A
    • Chatterjee, S., Suciu, D., Dalbey, R.E., Kahn, P.C., and, Inouye, M., (1995) Determination of Km and kcat for signal peptidase I using a full length secretory precursor, Pro-OmpA-nuclease A. J. Mol. Biol. 245, 311-314.
    • (1995) J. Mol. Biol. , vol.245 , pp. 311-314
    • Chatterjee, S.1    Suciu, D.2    Dalbey, R.E.3    Kahn, P.C.4    Inouye, M.5
  • 8
    • 84862577056 scopus 로고    scopus 로고
    • Membrane proteases in the bacterial protein secretion and quality control pathway
    • Dalbey, R.E., Wang, P., and, van Dijl, J.M., (2012) Membrane proteases in the bacterial protein secretion and quality control pathway. Microbiol. Mol. Biol. Rev. 76, 311-330.
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 311-330
    • Dalbey, R.E.1    Wang, P.2    Van Dijl, J.M.3
  • 9
    • 77956438350 scopus 로고    scopus 로고
    • Intramolecular Suzuki-Miyaura reaction for the total synthesis of signal peptidase inhibitors, arylomycins A(2) and B(2)
    • Dufour, J., Neuville, L., and, Zhu, J., (2010) Intramolecular Suzuki-Miyaura reaction for the total synthesis of signal peptidase inhibitors, arylomycins A(2) and B(2). Chemistry, 16, 10523-10534.
    • (2010) Chemistry , vol.16 , pp. 10523-10534
    • Dufour, J.1    Neuville, L.2    Zhu, J.3
  • 10
    • 84879684497 scopus 로고    scopus 로고
    • Stable complex formation of thylakoidal processing peptidase and PGRL1
    • Endow, J.K., and, Inoue, K., (2013) Stable complex formation of thylakoidal processing peptidase and PGRL1. FEBS Lett. 587, 2226-2231.
    • (2013) FEBS Lett. , vol.587 , pp. 2226-2231
    • Endow, J.K.1    Inoue, K.2
  • 11
    • 80052502918 scopus 로고    scopus 로고
    • A protein oxidase catalysing disulfide bond formation is localized to the chloroplast thylakoids
    • Feng, W.K., Wang, L., Lu, Y., and, Wang, X.Y., (2011) A protein oxidase catalysing disulfide bond formation is localized to the chloroplast thylakoids. FEBS J. 278, 3419-3430.
    • (2011) FEBS J. , vol.278 , pp. 3419-3430
    • Feng, W.K.1    Wang, L.2    Lu, Y.3    Wang, X.Y.4
  • 12
    • 0025216609 scopus 로고
    • Maturation of Escherichia coli maltose-binding protein by signal peptidase i in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site
    • Fikes, J.D., Barkocy-Gallagher, G.A., Klapper, D.G., and, Bassford, P.J. Jr, (1990) Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site. J. Biol. Chem. 265, 3417-3423.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3417-3423
    • Fikes, J.D.1    Barkocy-Gallagher, G.A.2    Klapper, D.G.3    Bassford, Jr.P.J.4
  • 13
    • 79955769112 scopus 로고    scopus 로고
    • Comprehensive transcriptome analysis of the highly complex Pisum sativum genome using next generation sequencing
    • Franssen, S.U., Shrestha, R.P., Brautigam, A., Bornberg-Bauer, E., and, Weber, A.P., (2011) Comprehensive transcriptome analysis of the highly complex Pisum sativum genome using next generation sequencing. BMC Genomics, 12, 227.
    • (2011) BMC Genomics , vol.12 , pp. 227
    • Franssen, S.U.1    Shrestha, R.P.2    Brautigam, A.3    Bornberg-Bauer, E.4    Weber, A.P.5
  • 14
    • 0035956267 scopus 로고    scopus 로고
    • Kinetic constants of signal peptidase i using cytochrome b5 as a precursor substrate
    • Gallagher, J., Kaderbhai, N.N., and, Kaderbhai, M.A., (2001) Kinetic constants of signal peptidase I using cytochrome b5 as a precursor substrate. Biochim. Biophys. Acta, 1550, 1-5.
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 1-5
    • Gallagher, J.1    Kaderbhai, N.N.2    Kaderbhai, M.A.3
  • 16
    • 0001610085 scopus 로고
    • A thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin
    • Hageman, J., Robinson, C., Smeekens, S., and, Weisbeek, P., (1986) A thylakoid processing protease is required for complete maturation of the lumen protein plastocyanin. Nature, 324, 567-569.
    • (1986) Nature , vol.324 , pp. 567-569
    • Hageman, J.1    Robinson, C.2    Smeekens, S.3    Weisbeek, P.4
  • 18
    • 0024852098 scopus 로고
    • The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical
    • Halpin, C., Elderfield, P.D., James, H.E., Zimmermann, R., Dunbar, B., and, Robinson, C., (1989) The reaction specificities of the thylakoidal processing peptidase and Escherichia coli leader peptidase are identical. EMBO J. 8, 3917-3921.
    • (1989) EMBO J. , vol.8 , pp. 3917-3921
    • Halpin, C.1    Elderfield, P.D.2    James, H.E.3    Zimmermann, R.4    Dunbar, B.5    Robinson, C.6
  • 19
    • 0028360823 scopus 로고
    • A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol
    • Han, J.C., and, Han, G.Y., (1994) A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odorless reducing agent more stable and effective than dithiothreitol. Anal. Biochem. 220, 5-10.
    • (1994) Anal. Biochem. , vol.220 , pp. 5-10
    • Han, J.C.1    Han, G.Y.2
  • 20
    • 36349025687 scopus 로고    scopus 로고
    • Chloroplast and mitochondrial type i signal peptidases
    • In XXII. (Dalbey, R.E. and Sigman, D.S. eds). San Diego, CA: Academic Press
    • Howe, C.J., and, Floyd, K.A., (2001) Chloroplast and mitochondrial type I signal peptidases. In Co- and Posttranslational Proteolysis of Proteins: The Enzymes Vol. XXII. (, Dalbey, R.E., and, Sigman, D.S., eds). San Diego, CA: Academic Press, pp. 101-125.
    • (2001) Co- And Posttranslational Proteolysis of Proteins: The Enzymes , pp. 101-125
    • Howe, C.J.1    Floyd, K.A.2
  • 21
    • 80455174456 scopus 로고    scopus 로고
    • Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana
    • Hsu, S.C., Endow, J.K., Ruppel, N.J., Roston, R.L., Baldwin, A.J., and, Inoue, K., (2011) Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana. PLoS ONE, 6, e27258.
    • (2011) PLoS ONE , vol.6 , pp. e27258
    • Hsu, S.C.1    Endow, J.K.2    Ruppel, N.J.3    Roston, R.L.4    Baldwin, A.J.5    Inoue, K.6
  • 22
    • 82755194799 scopus 로고    scopus 로고
    • OEP80, an essential protein paralogous to the chloroplast protein translocation channel Toc75, exists as a 70-kD protein in the Arabidopsis thaliana chloroplast outer envelope
    • Hsu, S.C., Nafati, M., and, Inoue, K., (2012) OEP80, an essential protein paralogous to the chloroplast protein translocation channel Toc75, exists as a 70-kD protein in the Arabidopsis thaliana chloroplast outer envelope. Plant Mol. Biol. 78, 147-158.
    • (2012) Plant Mol. Biol. , vol.78 , pp. 147-158
    • Hsu, S.C.1    Nafati, M.2    Inoue, K.3
  • 23
    • 0038129640 scopus 로고    scopus 로고
    • A polyglycine stretch is necessary for proper targeting of the protein translocation channel precursor to the outer envelope membrane of chloroplasts
    • Inoue, K., and, Keegstra, K., (2003) A polyglycine stretch is necessary for proper targeting of the protein translocation channel precursor to the outer envelope membrane of chloroplasts. Plant J. 34, 661-669.
    • (2003) Plant J. , vol.34 , pp. 661-669
    • Inoue, K.1    Keegstra, K.2
  • 24
    • 0034827035 scopus 로고    scopus 로고
    • The N-terminal portion of the preToc75 transit peptide interacts with membrane lipids and inhibits binding and import of precursor proteins into isolated chloroplasts
    • Inoue, K., Demel, R., de Kruijff, B., and, Keegstra, K., (2001) The N-terminal portion of the preToc75 transit peptide interacts with membrane lipids and inhibits binding and import of precursor proteins into isolated chloroplasts. Eur. J. Biochem. 268, 4036-4043.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4036-4043
    • Inoue, K.1    Demel, R.2    De Kruijff, B.3    Keegstra, K.4
  • 25
    • 27744459930 scopus 로고    scopus 로고
    • Complete maturation of the plastid protein translocation channel requires a type i signal peptidase
    • Inoue, K., Baldwin, A.J., Shipman, R.L., Matsui, K., Theg, S.M., and, Ohme-Takagi, M., (2005a) Complete maturation of the plastid protein translocation channel requires a type I signal peptidase. J. Cell Biol. 171, 425-430.
    • (2005) J. Cell Biol. , vol.171 , pp. 425-430
    • Inoue, K.1    Baldwin, A.J.2    Shipman, R.L.3    Matsui, K.4    Theg, S.M.5    Ohme-Takagi, M.6
  • 26
    • 27744451465 scopus 로고    scopus 로고
    • Involvement of a type i signal peptidase in biogenesis of chloroplasts-towards identification of the enzyme for maturation of the chloroplast protein translocation channel
    • In (van der Est, A. and Bruce, D. eds). Lawrence, KS: Allen Press
    • Inoue, K., Potter, D., Shipman, R.L., Perea, J.V., and, Theg, S.M., (2005b) Involvement of a type I signal peptidase in biogenesis of chloroplasts-towards identification of the enzyme for maturation of the chloroplast protein translocation channel. In Photosynthesis: Fundamental Aspects to Global Perspectives (, van der Est, A., and, Bruce, D., eds). Lawrence, KS: Allen Press, pp. 933-935.
    • (2005) Photosynthesis: Fundamental Aspects to Global Perspectives , pp. 933-935
    • Inoue, K.1    Potter, D.2    Shipman, R.L.3    Perea, J.V.4    Theg, S.M.5
  • 27
    • 0024341170 scopus 로고
    • Transport of proteins into chloroplasts. Import and maturation of precursors to the 33-, 23-, and 16-kDa proteins of the photosynthetic oxygen-evolving complex
    • James, H.E., Bartling, D., Musgrove, J.E., Kirwin, P.M., Herrmann, R.G., and, Robinson, C., (1989) Transport of proteins into chloroplasts. Import and maturation of precursors to the 33-, 23-, and 16-kDa proteins of the photosynthetic oxygen-evolving complex. J. Biol. Chem. 264, 19573-19576.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19573-19576
    • James, H.E.1    Bartling, D.2    Musgrove, J.E.3    Kirwin, P.M.4    Herrmann, R.G.5    Robinson, C.6
  • 28
    • 84899001325 scopus 로고    scopus 로고
    • Understanding the roles of the thylakoid lumen in photosynthesis regulation
    • Jarvi, S., Gollan, P.J., and, Aro, E.M., (2013) Understanding the roles of the thylakoid lumen in photosynthesis regulation. Front. Plant Sci. 4, 434.
    • (2013) Front. Plant Sci. , vol.4 , pp. 434
    • Jarvi, S.1    Gollan, P.J.2    Aro, E.M.3
  • 29
    • 84856487868 scopus 로고    scopus 로고
    • Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis
    • Karamoko, M., Cline, S., Redding, K., Ruiz, N., and, Hamel, P.P., (2011) Lumen Thiol Oxidoreductase1, a disulfide bond-forming catalyst, is required for the assembly of photosystem II in Arabidopsis. Plant Cell, 23, 4462-4475.
    • (2011) Plant Cell , vol.23 , pp. 4462-4475
    • Karamoko, M.1    Cline, S.2    Redding, K.3    Ruiz, N.4    Hamel, P.P.5
  • 30
    • 0032502929 scopus 로고    scopus 로고
    • Processing of Escherichia coli alkaline phosphatase: Role of the primary structure of the signal peptide cleavage region
    • Karamyshev, A.L., Karamysheva, Z.N., Kajava, A.V., Ksenzenko, V.N., and, Nesmeyanova, M.A., (1998) Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. J. Mol. Biol. 277, 859-870.
    • (1998) J. Mol. Biol. , vol.277 , pp. 859-870
    • Karamyshev, A.L.1    Karamysheva, Z.N.2    Kajava, A.V.3    Ksenzenko, V.N.4    Nesmeyanova, M.A.5
  • 31
    • 84878823130 scopus 로고    scopus 로고
    • Oxidative folding in chloroplasts
    • Kieselbach, T., (2013) Oxidative folding in chloroplasts. Antioxid. Redox Signal. 19, 72-82.
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 72-82
    • Kieselbach, T.1
  • 32
    • 0023646043 scopus 로고
    • Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis
    • Kirwin, P.M., Elderfield, P.D., and, Robinson, C., (1987) Transport of proteins into chloroplasts. Partial purification of a thylakoidal processing peptidase involved in plastocyanin biogenesis. J. Biol. Chem. 262, 16386-16390.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16386-16390
    • Kirwin, P.M.1    Elderfield, P.D.2    Robinson, C.3
  • 33
    • 0024279608 scopus 로고
    • Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network
    • Kirwin, P.M., Elderfield, P.D., Williams, R.S., and, Robinson, C., (1988) Transport of proteins into chloroplasts. Organization, orientation, and lateral distribution of the plastocyanin processing peptidase in the thylakoid network. J. Biol. Chem. 263, 18128-18132.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18128-18132
    • Kirwin, P.M.1    Elderfield, P.D.2    Williams, R.S.3    Robinson, C.4
  • 35
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • Kranz, R.G., Richard-Fogal, C., Taylor, J.S., and, Frawley, E.R., (2009) Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control. Microbiol. Mol. Biol. Rev. 73, 510-528.
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.S.3    Frawley, E.R.4
  • 36
    • 0027287556 scopus 로고
    • Escherichia coli leader peptidase: Production of an active form lacking a requirement for detergent and development of peptide substrates
    • Kuo, D.W., Chan, H.K., Wilson, C.J., Griffin, P.R., Williams, H., and, Knight, W.B., (1993) Escherichia coli leader peptidase: production of an active form lacking a requirement for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274-280.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 274-280
    • Kuo, D.W.1    Chan, H.K.2    Wilson, C.J.3    Griffin, P.R.4    Williams, H.5    Knight, W.B.6
  • 37
    • 0035209897 scopus 로고    scopus 로고
    • HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis
    • Lennartz, K., Plucken, H., Seidler, A., Westhoff, P., Bechtold, N., and, Meierhoff, K., (2001) HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis. Plant Cell, 13, 2539-2551.
    • (2001) Plant Cell , vol.13 , pp. 2539-2551
    • Lennartz, K.1    Plucken, H.2    Seidler, A.3    Westhoff, P.4    Bechtold, N.5    Meierhoff, K.6
  • 38
    • 63349083179 scopus 로고    scopus 로고
    • Disulphide proteomes and interactions with thioredoxin on the track towards understanding redox regulation in chloroplasts and cyanobacteria
    • Lindahl, M., and, Kieselbach, T., (2009) Disulphide proteomes and interactions with thioredoxin on the track towards understanding redox regulation in chloroplasts and cyanobacteria. J. Proteomics, 72, 416-438.
    • (2009) J. Proteomics , vol.72 , pp. 416-438
    • Lindahl, M.1    Kieselbach, T.2
  • 39
    • 84881608273 scopus 로고    scopus 로고
    • A chloroplast membrane protein LTO1/AtVKOR involving in redox regulation and ROS homeostasis
    • Lu, Y., Wang, H.R., Li, H., Cui, H.R., Feng, Y.G., and, Wang, X.Y., (2013) A chloroplast membrane protein LTO1/AtVKOR involving in redox regulation and ROS homeostasis. Plant Cell Rep. 32, 1427-1440.
    • (2013) Plant Cell Rep. , vol.32 , pp. 1427-1440
    • Lu, Y.1    Wang, H.R.2    Li, H.3    Cui, H.R.4    Feng, Y.G.5    Wang, X.Y.6
  • 40
    • 84900837239 scopus 로고    scopus 로고
    • Redox regulation of the Calvin-Benson cycle: Something old, something new
    • Michelet, L., Zaffagnini, M., Morisse, S., et al. (2013) Redox regulation of the Calvin-Benson cycle: something old, something new. Front. Plant Sci. 4, 470.
    • (2013) Front. Plant Sci. , vol.4 , pp. 470
    • Michelet, L.1    Zaffagnini, M.2    Morisse, S.3
  • 41
    • 84884910720 scopus 로고    scopus 로고
    • Multiple fates of non-mature lumenal proteins in thylakoids
    • Midorikawa, T., and, Inoue, K., (2013) Multiple fates of non-mature lumenal proteins in thylakoids. Plant J. 76, 73-86.
    • (2013) Plant J. , vol.76 , pp. 73-86
    • Midorikawa, T.1    Inoue, K.2
  • 42
    • 70349650807 scopus 로고    scopus 로고
    • An Rrf2-type transcriptional regulator is required for expression of psaAB genes in the cyanobacterium Synechocystis sp. PCC 6803
    • Midorikawa, T., Matsumoto, K., Narikawa, R., and, Ikeuchi, M., (2009) An Rrf2-type transcriptional regulator is required for expression of psaAB genes in the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 151, 882-892.
    • (2009) Plant Physiol. , vol.151 , pp. 882-892
    • Midorikawa, T.1    Matsumoto, K.2    Narikawa, R.3    Ikeuchi, M.4
  • 43
    • 33845939598 scopus 로고    scopus 로고
    • HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen
    • Motohashi, K., and, Hisabori, T., (2006) HCF164 receives reducing equivalents from stromal thioredoxin across the thylakoid membrane and mediates reduction of target proteins in the thylakoid lumen. J. Biol. Chem. 281, 35039-35047.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35039-35047
    • Motohashi, K.1    Hisabori, T.2
  • 44
    • 77956319563 scopus 로고    scopus 로고
    • CcdA is a thylakoid membrane protein required for the transfer of reducing equivalents from stroma to thylakoid lumen in the higher plant chloroplast
    • Motohashi, K., and, Hisabori, T., (2010) CcdA is a thylakoid membrane protein required for the transfer of reducing equivalents from stroma to thylakoid lumen in the higher plant chloroplast. Antioxid. Redox Signal. 13, 1169-1176.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1169-1176
    • Motohashi, K.1    Hisabori, T.2
  • 45
    • 57849108459 scopus 로고    scopus 로고
    • Importance of a single disulfide bond for the PsbO protein of photosystem II: Protein structure stability and soluble overexpression in Escherichia coli
    • Nikitina, J., Shutova, T., Melnik, B., Chernyshov, S., Marchenkov, V., Semisotnov, G., Klimov, V., and, Samuelsson, G., (2008) Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli. Photosynth. Res. 98, 391-403.
    • (2008) Photosynth. Res. , vol.98 , pp. 391-403
    • Nikitina, J.1    Shutova, T.2    Melnik, B.3    Chernyshov, S.4    Marchenkov, V.5    Semisotnov, G.6    Klimov, V.7    Samuelsson, G.8
  • 46
    • 84902299780 scopus 로고    scopus 로고
    • Structure and mechanism of Escherichia coli type i signal peptidase
    • Paetzel, M., (2014) Structure and mechanism of Escherichia coli type I signal peptidase. Biochim. Biophys. Acta, 1843, 1497-1508.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1497-1508
    • Paetzel, M.1
  • 47
    • 0030934282 scopus 로고    scopus 로고
    • Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase
    • Paetzel, M., Strynadka, N.C., Tschantz, W.R., Casareno, R., Bullinger, P.R., and, Dalbey, R.E., (1997) Use of site-directed chemical modification to study an essential lysine in Escherichia coli leader peptidase. J. Biol. Chem. 272, 9994-10003.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9994-10003
    • Paetzel, M.1    Strynadka, N.C.2    Tschantz, W.R.3    Casareno, R.4    Bullinger, P.R.5    Dalbey, R.E.6
  • 48
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel, M., Dalbey, R.E., and, Strynadka, N.C., (1998) Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature, 396, 186-190.
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 49
    • 0033866745 scopus 로고    scopus 로고
    • The structure and mechanism of bacterial type i signal peptidases. A novel antibiotic target
    • Paetzel, M., Dalbey, R.E., and, Strynadka, N.C., (2000) The structure and mechanism of bacterial type I signal peptidases. A novel antibiotic target. Pharmacol. Ther. 87, 27-49.
    • (2000) Pharmacol. Ther. , vol.87 , pp. 27-49
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 50
    • 0037088648 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase apoenzyme - Implications for signal peptide binding and the Ser-Lys dyad mechanism
    • Paetzel, M., Dalbey, R.E., and, Strynadka, N.C.J., (2002a) Crystal structure of a bacterial signal peptidase apoenzyme-Implications for signal peptide binding and the Ser-Lys dyad mechanism. J. Biol. Chem. 277, 9512-9519.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9512-9519
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 52
    • 3142715940 scopus 로고    scopus 로고
    • Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor
    • Paetzel, M., Goodall, J.J., Kania, M., Dalbey, R.E., and, Page, M.G., (2004) Crystallographic and biophysical analysis of a bacterial signal peptidase in complex with a lipopeptide-based inhibitor. J. Biol. Chem. 279, 30781-30790.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30781-30790
    • Paetzel, M.1    Goodall, J.J.2    Kania, M.3    Dalbey, R.E.4    Page, M.G.5
  • 53
  • 54
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and, Dobberstein, B., (1996) Common principles of protein translocation across membranes. Science, 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 55
    • 0036308911 scopus 로고    scopus 로고
    • Arylomycins A and B, new biaryl-bridged lipopeptide antibiotics produced by Streptomyces sp. Tu 6075. I. Taxonomy, fermentation, isolation and biological activities
    • Schimana, J., Gebhardt, K., Holtzel, A., Schmid, D.G., Sussmuth, R., Muller, J., Pukall, R., and, Fiedler, H.P., (2002) Arylomycins A and B, new biaryl-bridged lipopeptide antibiotics produced by Streptomyces sp. Tu 6075. I. Taxonomy, fermentation, isolation and biological activities. J. Antibiot. 55, 565-570.
    • (2002) J. Antibiot. , vol.55 , pp. 565-570
    • Schimana, J.1    Gebhardt, K.2    Holtzel, A.3    Schmid, D.G.4    Sussmuth, R.5    Muller, J.6    Pukall, R.7    Fiedler, H.P.8
  • 56
    • 0000103040 scopus 로고    scopus 로고
    • A consensus nomenclature for the protein-import components of the chloroplast envelope
    • Schnell, D.J., Blobel, G., Keegstra, K., Kessler, F., Ko, K., and, Soll, J., (1997) A consensus nomenclature for the protein-import components of the chloroplast envelope. Trends Cell Biol. 7, 303-304.
    • (1997) Trends Cell Biol. , vol.7 , pp. 303-304
    • Schnell, D.J.1    Blobel, G.2    Keegstra, K.3    Kessler, F.4    Ko, K.5    Soll, J.6
  • 58
    • 0025830411 scopus 로고
    • Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton, J.B., and, Robinson, C., (1991) Transport of proteins into chloroplasts. 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
  • 59
    • 60749118851 scopus 로고    scopus 로고
    • Suborganellar localization of plastidic type i signal peptidase 1 depends on chloroplast development
    • Shipman, R.L., and, Inoue, K., (2009) Suborganellar localization of plastidic type I signal peptidase 1 depends on chloroplast development. FEBS Lett. 583, 938-942.
    • (2009) FEBS Lett. , vol.583 , pp. 938-942
    • Shipman, R.L.1    Inoue, K.2
  • 60
    • 77949516026 scopus 로고    scopus 로고
    • The significance of protein maturation by plastidic type i signal peptidase 1 for thylakoid development in Arabidopsis chloroplasts
    • Shipman-Roston, R.L., Ruppel, N.J., Damoc, C., Phinney, B.S., and, Inoue, K., (2010) The significance of protein maturation by plastidic type I signal peptidase 1 for thylakoid development in Arabidopsis chloroplasts. Plant Physiol. 152, 1297-1308.
    • (2010) Plant Physiol. , vol.152 , pp. 1297-1308
    • Shipman-Roston, R.L.1    Ruppel, N.J.2    Damoc, C.3    Phinney, B.S.4    Inoue, K.5
  • 61
    • 47049096139 scopus 로고    scopus 로고
    • Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms
    • Singh, A.K., Bhattacharyya-Pakrasi, M., and, Pakrasi, H.B., (2008) Identification of an atypical membrane protein involved in the formation of protein disulfide bonds in oxygenic photosynthetic organisms. J. Biol. Chem. 283, 15762-15770.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15762-15770
    • Singh, A.K.1    Bhattacharyya-Pakrasi, M.2    Pakrasi, H.B.3
  • 62
    • 84866314697 scopus 로고    scopus 로고
    • Mechanism of action of the arylomycin antibiotics and effects of signal peptidase i inhibition
    • Smith, P.A., and, Romesberg, F.E., (2012) Mechanism of action of the arylomycin antibiotics and effects of signal peptidase I inhibition. Antimicrob. Agents Chemother. 56, 5054-5060.
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5054-5060
    • Smith, P.A.1    Romesberg, F.E.2
  • 63
    • 0026631514 scopus 로고
    • Identification of potential active-site residues in the Escherichia coli leader peptidase
    • Sung, M., and, Dalbey, R.E., (1992) Identification of potential active-site residues in the Escherichia coli leader peptidase. J. Biol. Chem. 267, 13154-13159.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13154-13159
    • Sung, M.1    Dalbey, R.E.2
  • 64
    • 34848863975 scopus 로고    scopus 로고
    • The thylakoid proton motive force in vivo. Quantitative, non-invasive probes, energetics, and regulatory consequences of light-induced pmf
    • Takizawa, K., Cruz, J.A., Kanazawa, A., and, Kramer, D.M., (2007) The thylakoid proton motive force in vivo. Quantitative, non-invasive probes, energetics, and regulatory consequences of light-induced pmf. Biochim. Biophys. Acta, 1767, 1233-1244.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1233-1244
    • Takizawa, K.1    Cruz, J.A.2    Kanazawa, A.3    Kramer, D.M.4
  • 65
    • 0027733662 scopus 로고
    • A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase
    • Tschantz, W.R., Sung, M., Delgado-Partin, V.M., and, Dalbey, R.E., (1993) A serine and a lysine residue implicated in the catalytic mechanism of the Escherichia coli leader peptidase. J. Biol. Chem. 268, 27349-27354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27349-27354
    • Tschantz, W.R.1    Sung, M.2    Delgado-Partin, V.M.3    Dalbey, R.E.4
  • 66
    • 0028942966 scopus 로고
    • Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: Requirement of detergent or phospholipid for optimal activity
    • Tschantz, W.R., Paetzel, M., Cao, G., Suciu, D., Inouye, M., and, Dalbey, R.E., (1995) Characterization of a soluble, catalytically active form of Escherichia coli leader peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry, 34, 3935-3941.
    • (1995) Biochemistry , vol.34 , pp. 3935-3941
    • Tschantz, W.R.1    Paetzel, M.2    Cao, G.3    Suciu, D.4    Inouye, M.5    Dalbey, R.E.6
  • 67
    • 0025088924 scopus 로고
    • The reaction specificities of the pea and a cyanobacterial thylakoid processing peptidase are similar but not identical
    • Wallace, T.P., Robinson, C., and, Howe, C.J., (1990) The reaction specificities of the pea and a cyanobacterial thylakoid processing peptidase are similar but not identical. FEBS Lett. 272, 141-144.
    • (1990) FEBS Lett. , vol.272 , pp. 141-144
    • Wallace, T.P.1    Robinson, C.2    Howe, C.J.3
  • 68
    • 77954714026 scopus 로고    scopus 로고
    • In vitro and in vivo approaches to studying the bacterial signal peptide processing
    • Wang, P., and, Dalbey, R.E., (2010) In vitro and in vivo approaches to studying the bacterial signal peptide processing. Methods Mol. Biol. 619, 21-37.
    • (2010) Methods Mol. Biol. , vol.619 , pp. 21-37
    • Wang, P.1    Dalbey, R.E.2
  • 69
    • 0031128430 scopus 로고    scopus 로고
    • High mobility group proteins HMG-1 and HMG-I/Y bind to a positive regulatory region of the pea plastocyanin gene promoter
    • Webster, C.I., Packman, L.C., Pwee, K.H., and, Gray, J.C., (1997) High mobility group proteins HMG-1 and HMG-I/Y bind to a positive regulatory region of the pea plastocyanin gene promoter. Plant J. 11, 703-715.
    • (1997) Plant J. , vol.11 , pp. 703-715
    • Webster, C.I.1    Packman, L.C.2    Pwee, K.H.3    Gray, J.C.4
  • 70
    • 0242300620 scopus 로고    scopus 로고
    • Empirical analysis of transcriptional activity in the Arabidopsis genome
    • Yamada, K., Lim, J., Dale, J.M., et al. (2003) Empirical analysis of transcriptional activity in the Arabidopsis genome. Science, 302, 842-846.
    • (2003) Science , vol.302 , pp. 842-846
    • Yamada, K.1    Lim, J.2    Dale, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.