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Volumn 228, Issue 1, 2003, Pages 121-128

Transcriptional regulation and structural modelling of the Synechocystis sp. PCC 6803 carboxyl-terminal endoprotease family

Author keywords

CtpA; CtpB; CtpC; PDZ domain; Precursor D1; Synechocystis 6803

Indexed keywords

BACTERIAL ENZYME; GENE PRODUCT; PRIMER DNA; PROTEINASE; RNA; VIRUS ENVELOPE PROTEIN;

EID: 0242637463     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00744-4     Document Type: Article
Times cited : (11)

References (43)
  • 2
    • 0036935397 scopus 로고    scopus 로고
    • The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplast
    • Sokolenko A., Pojidaeva E., Zinchenko V., Panichin V., Glaser V.M., Herrmann R.G., Shestakov S.V. The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplast. Curr. Genet. 41:2002;291-310.
    • (2002) Curr. Genet. , vol.41 , pp. 291-310
    • Sokolenko, A.1    Pojidaeva, E.2    Zinchenko, V.3    Panichin, V.4    Glaser, V.M.5    Herrmann, R.G.6    Shestakov, S.V.7
  • 3
    • 0031033450 scopus 로고    scopus 로고
    • Catalytic hydroxyl/amine dyads within serine proteases
    • Paetzel M., Dalbey R.E. Catalytic hydroxyl/amine dyads within serine proteases. Trends Biochem. Sci. 22:1997;28-31.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 28-31
    • Paetzel, M.1    Dalbey, R.E.2
  • 4
    • 0028064901 scopus 로고
    • Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease: Analysis of a spontaneous Photosystem II deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803
    • Shestakov S.V., Anbudurai P.R., Stanbekova G.E., Gadzhiev A., Lind L.K., Pakrasi H.B. Molecular cloning and characterization of the ctpA gene encoding a carboxyl-terminal processing protease: Analysis of a spontaneous Photosystem II deficient mutant strain of the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 269:1994;19354-19359.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19354-19359
    • Shestakov, S.V.1    Anbudurai, P.R.2    Stanbekova, G.E.3    Gadzhiev, A.4    Lind, L.K.5    Pakrasi, H.B.6
  • 5
    • 0026513218 scopus 로고
    • Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini
    • Silber K.R., Keiler K.C., Sauer R.T. Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. Proc. Natl. Acad. Sci. USA. 89:1992;295-299.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 295-299
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 6
    • 0036651420 scopus 로고    scopus 로고
    • Investigation of the functional role of Ctp proteins in the cyanobacterium Synechocystis sp. PCC 6803
    • Ivleva N.B., Sidoruk K.V., Pakrasi H.B., Shestakov S.V. Investigation of the functional role of Ctp proteins in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology. 71:2002;509-513.
    • (2002) Microbiology , vol.71 , pp. 509-513
    • Ivleva, N.B.1    Sidoruk, K.V.2    Pakrasi, H.B.3    Shestakov, S.V.4
  • 7
    • 0033797930 scopus 로고    scopus 로고
    • Proteomics of Synechocystis sp. strain 6803. Identification of periplasmic proteins grown at low and high salt concentrations
    • Fulda S., Huang F., Nilsson F., Hagemann M., Norling B. Proteomics of Synechocystis sp. strain 6803. Identification of periplasmic proteins grown at low and high salt concentrations. Eur. J. Biochem. 267:2000;5900-5907.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5900-5907
    • Fulda, S.1    Huang, F.2    Nilsson, F.3    Hagemann, M.4    Norling, B.5
  • 8
    • 0036858807 scopus 로고    scopus 로고
    • Localisation and processing of the precursor form of photosystem II protein D1 in Synechocystis 6803
    • Jansén T., Kanervo E., Aro E.-M., Mäenpää P. Localisation and processing of the precursor form of photosystem II protein D1 in Synechocystis 6803. J. Plant Physiol. 159:2002;1205-1211.
    • (2002) J. Plant Physiol. , vol.159 , pp. 1205-1211
    • Jansén, T.1    Kanervo, E.2    Aro, E.-M.3    Mäenpää, P.4
  • 11
    • 77957024978 scopus 로고
    • Construction of specific mutations in PSII photosynthetic reaction center by genetic engineering
    • Williams J.K.G. Construction of specific mutations in PSII photosynthetic reaction center by genetic engineering. Methods Enzymol. 167:1988;766-778.
    • (1988) Methods Enzymol. , vol.167 , pp. 766-778
    • Williams, J.K.G.1
  • 12
    • 0001394554 scopus 로고
    • Sedimentation characteristics of rapidly labelled RNA from HeLa cells
    • Schrerrer K., Darnell J.E. Sedimentation characteristics of rapidly labelled RNA from HeLa cells. Biochem. Biophys. Res. Commun. 7:1962;486-490.
    • (1962) Biochem. Biophys. Res. Commun. , vol.7 , pp. 486-490
    • Schrerrer, K.1    Darnell, J.E.2
  • 13
    • 0027361123 scopus 로고
    • A structural basis for the comparison of sequences: An evaluation of scoring methodologies
    • Johnson M.S., Overington J.P. A structural basis for the comparison of sequences: an evaluation of scoring methodologies. J. Mol. Biol. 233:1993;716-738.
    • (1993) J. Mol. Biol. , vol.233 , pp. 716-738
    • Johnson, M.S.1    Overington, J.P.2
  • 14
    • 0029884429 scopus 로고    scopus 로고
    • Discrimination of common protein folds: Applications of structural information to sequence/structure comparisons
    • Johnson M.S., May A.C.W., Rodionov M.A., Overington J.P. Discrimination of common protein folds: applications of structural information to sequence/structure comparisons. Methods Enzymol. 266:1996;575-598.
    • (1996) Methods Enzymol. , vol.266 , pp. 575-598
    • Johnson, M.S.1    May, A.C.W.2    Rodionov, M.A.3    Overington, J.P.4
  • 15
    • 85030946968 scopus 로고    scopus 로고
    • http://www.abo.fi/fak/mnf/bkf/research/johnson/bodil.html.
  • 16
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 17
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: The colony energy and its application to the problem of loop prediction
    • Xiang Z., Soto C.S., Honig B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl. Acad. Sci. USA. 11:2002;7432-7437.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.11 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 18
    • 0001817941 scopus 로고    scopus 로고
    • Comparison of protein three dimensional structures
    • Higgins, D. and Taylor, W., Eds. Oxford University Press, Oxford
    • Johnson, M.S. and Lehtonen, J.V. (2000) Comparison of protein three dimensional structures. In: Bioinformatics: Sequence, Structure and Databanks (Higgins, D. and Taylor, W., Eds.), pp. 15-50. Oxford University Press, Oxford.
    • (2000) Bioinformatics: Sequence, Structure and Databanks , pp. 15-50
    • Johnson, M.S.1    Lehtonen, J.V.2
  • 19
    • 0027412196 scopus 로고
    • ALSCRIPT - a tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT - a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic Molecular Graphics
    • Merritt E.A., Bacon D.J. Raster3D: Photorealistic Molecular Graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 23
    • 0032719331 scopus 로고    scopus 로고
    • Identification of salt-regulated genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 by subtractive RNA hybridisation
    • Vinnemeier J., Hagemann M. Identification of salt-regulated genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 by subtractive RNA hybridisation. Arch. Microbiol. 172:1999;377-386.
    • (1999) Arch. Microbiol. , vol.172 , pp. 377-386
    • Vinnemeier, J.1    Hagemann, M.2
  • 24
    • 0035037364 scopus 로고    scopus 로고
    • DNA microarray analysis of cyanobacterial gene expression during acclimation to high light
    • Hihara Y., Kamei A., Kanehisha M., Kaplan A., Ikeuchi M. DNA microarray analysis of cyanobacterial gene expression during acclimation to high light. Plant Cell. 13:2001;793-806.
    • (2001) Plant Cell , vol.13 , pp. 793-806
    • Hihara, Y.1    Kamei, A.2    Kanehisha, M.3    Kaplan, A.4    Ikeuchi, M.5
  • 25
    • 0035788620 scopus 로고    scopus 로고
    • How do cyanobacteria sense and respond to light?
    • Mullineaux C.W. How do cyanobacteria sense and respond to light? Mol. Microbiol. 41:2001;965-971.
    • (2001) Mol. Microbiol. , vol.41 , pp. 965-971
    • Mullineaux, C.W.1
  • 27
    • 0037369852 scopus 로고    scopus 로고
    • DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803
    • Hihara Y., Sonoike K., Kanehisha M., Ikeuchi M. DNA microarray analysis of redox-responsive genes in the genome of the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 185:2003;1719-1725.
    • (2003) J. Bacteriol. , vol.185 , pp. 1719-1725
    • Hihara, Y.1    Sonoike, K.2    Kanehisha, M.3    Ikeuchi, M.4
  • 28
    • 0036947251 scopus 로고    scopus 로고
    • Global gene expression of the cyanobacterium Synechocystis sp. strain PCC 6803 in response to irradiation with UV-B and white light
    • Huang L., McCluskey P., Hao N., LaRossa R. Global gene expression of the cyanobacterium Synechocystis sp. strain PCC 6803 in response to irradiation with UV-B and white light. J. Bacteriol. 184:2002;6845-6858.
    • (2002) J. Bacteriol. , vol.184 , pp. 6845-6858
    • Huang, L.1    McCluskey, P.2    Hao, N.3    LaRossa, R.4
  • 29
    • 0024869570 scopus 로고
    • Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803
    • Mohamed A., Jansson C. Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803. Plant Mol. Biol. 13:1989;693-700.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 693-700
    • Mohamed, A.1    Jansson, C.2
  • 31
    • 17144472877 scopus 로고    scopus 로고
    • Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803
    • Navarro F., Martin-Figueroa E., Florencio F.J. Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 43:2000;23-32.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 23-32
    • Navarro, F.1    Martin-Figueroa, E.2    Florencio, F.J.3
  • 32
    • 0036289674 scopus 로고    scopus 로고
    • Salt stress and hyperosmotic stress regulate the expression of different sets of genes in Synechocystis sp. PCC 6803
    • Kanesaki Y., Suzuki I., Allakhverdiev S.I., Mikami K., Murata N. Salt stress and hyperosmotic stress regulate the expression of different sets of genes in Synechocystis sp. PCC 6803. Biochem. Biophys. Res. Commun. 290:2002;339-348.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 339-348
    • Kanesaki, Y.1    Suzuki, I.2    Allakhverdiev, S.I.3    Mikami, K.4    Murata, N.5
  • 33
    • 0036548759 scopus 로고    scopus 로고
    • Regulation of the desaturation of fatty acids and its role in tolerance to cold and salt stress
    • Sakamoto T., Murata N. Regulation of the desaturation of fatty acids and its role in tolerance to cold and salt stress. Curr. Opin. Microbiol. 5:2002;208-210.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 208-210
    • Sakamoto, T.1    Murata, N.2
  • 35
    • 0037309151 scopus 로고    scopus 로고
    • Expression of primary sigma factor (PSF) and PSF-like sigma factors in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Tuominen I., Tyystjärvi E., Tyystjärvi T. Expression of primary sigma factor (PSF) and PSF-like sigma factors in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 185:2003;1116-1119.
    • (2003) J. Bacteriol. , vol.185 , pp. 1116-1119
    • Tuominen, I.1    Tyystjärvi, E.2    Tyystjärvi, T.3
  • 36
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in yeast, bacteria and plants
    • Ponting C.P. Evidence for PDZ domains in yeast, bacteria and plants. Protein Sci. 6:1997;464-468.
    • (1997) Protein Sci. , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 37
    • 0035040683 scopus 로고    scopus 로고
    • Regulation of translation elongation in cyanobacteria: Membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein
    • Tyystjärvi T., Herranen M., Aro E.-M. Regulation of translation elongation in cyanobacteria: membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein. Mol. Microbiol. 40:2001;1-10.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1-10
    • Tyystjärvi, T.1    Herranen, M.2    Aro, E.-M.3
  • 39
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel M., Dalbey R.E., Strynadka N.C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature. 12:1998;186-190.
    • (1998) Nature , vol.12 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 42
    • 0034705320 scopus 로고    scopus 로고
    • Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding
    • Bell C.E., Frescura P., Hochschild A., Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell. 101:2000;801-811.
    • (2000) Cell , vol.101 , pp. 801-811
    • Bell, C.E.1    Frescura, P.2    Hochschild, A.3    Lewis, M.4
  • 43
    • 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., Strynadka N.C. Crystal structure of a bacterial signal peptidase apoenzyme: implications for signal peptide binding and the Ser-Lys dyad mechanism. J. Biol. Chem. 15:2002;9512-9519.
    • (2002) J. Biol. Chem. , vol.15 , pp. 9512-9519
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3


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