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Volumn 65, Issue 12, 2004, Pages 1785-1793

Proteomics-based sequence analysis of plant gene expression - The chloroplast transcription apparatus

Author keywords

CK2, casein kinase 2 (EC 2.7.1.37); CSP41, chloroplast stem loop binding 3 RNA processing endonuclease of 41 kDa (EC 3.1.25.X); ESI QTOF, electrospray ionization quadrupole time of flight; GSH, glutathione (reduced form)

Indexed keywords

CASEIN KINASE II; GLUTATHIONE; PROTEIN KINASE; RNA BINDING PROTEIN; RNA POLYMERASE;

EID: 3242749140     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2004.04.034     Document Type: Article
Times cited : (25)

References (36)
  • 2
    • 0034161452 scopus 로고    scopus 로고
    • SAP - A putative DNA-binding motif involved in chromosomal organization
    • Aravind L., Koonin E.V. SAP - a putative DNA-binding motif involved in chromosomal organization. Trends Biochem. Sci. 25:2000;112-114
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 112-114
    • Aravind, L.1    Koonin, E.V.2
  • 3
    • 0037298310 scopus 로고    scopus 로고
    • Redox regulation of thylakoid protein phosphorylation
    • Aro E.M., Ohad I. Redox regulation of thylakoid protein phosphorylation. Antiox. Redox Signal. 5:2003;55-67
    • (2003) Antiox. Redox Signal , vol.5 , pp. 55-67
    • Aro, E.M.1    Ohad, I.2
  • 4
    • 0035197586 scopus 로고    scopus 로고
    • Chloroplast transcription at different light intensities. Glutathione-mediated phosphorylation of the major RNA polymerase involved in redox-regulated organellar gene expression
    • Baena-González E., Baginsky S., Mulo P., Summer H., Aro E.-M., Link G. Chloroplast transcription at different light intensities. Glutathione-mediated phosphorylation of the major RNA polymerase involved in redox-regulated organellar gene expression. Plant Physiol. 127:2001;1044-1052
    • (2001) Plant Physiol. , vol.127 , pp. 1044-1052
    • Baena-González, E.1    Baginsky, S.2    Mulo, P.3    Summer, H.4    Aro, E.-M.5    Link, G.6
  • 5
    • 0031148893 scopus 로고    scopus 로고
    • Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba)
    • Baginsky S., Tiller K., Link G. Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba). Plant Mol. Biol. 34:1997;181-189
    • (1997) Plant Mol. Biol. , vol.34 , pp. 181-189
    • Baginsky, S.1    Tiller, K.2    Link, G.3
  • 6
    • 0033103027 scopus 로고    scopus 로고
    • PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription
    • Baginsky S., Tiller K., Pfannschmidt T., Link G. PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription. Plant Mol. Biol. 39:1999;1013-1023
    • (1999) Plant Mol. Biol. , vol.39 , pp. 1013-1023
    • Baginsky, S.1    Tiller, K.2    Pfannschmidt, T.3    Link, G.4
  • 7
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N., Gammeltoft S., Brunak S. Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294:1999;1351-1362
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 8
    • 0002804652 scopus 로고
    • Replication and transcription of plastid DNA
    • L. Bogorad, & I.K. Vasil. San Diego: Academic Press
    • Bogorad L. Replication and transcription of plastid DNA. Bogorad L., Vasil I.K. The Molecular Biology of Plastids. 1991;93-124 Academic Press, San Diego
    • (1991) The Molecular Biology of Plastids , pp. 93-124
    • Bogorad, L.1
  • 9
    • 0037493295 scopus 로고    scopus 로고
    • ′- untranslated regions direct cleavage by CSP41, an endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily
    • ′ -untranslated regions direct cleavage by CSP41, an endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily J. Biol. Chem. 278:2003;25832-25838
    • (2003) J. Biol. Chem. , vol.278 , pp. 25832-25838
    • Bollenbach, T.J.1    Stern, D.B.2
  • 10
    • 0043163808 scopus 로고    scopus 로고
    • Divalent metal-dependent catalysis and cleavage specificity of CSP41, a chloroplast endoribonuclease belonging to the short chain dehydrogenase/ reductase superfamily
    • Bollenbach T.J., Stern D.B. Divalent metal-dependent catalysis and cleavage specificity of CSP41, a chloroplast endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily. Nucleic Acids Res. 31:2003;17-25
    • (2003) Nucleic Acids Res. , vol.31 , pp. 17-25
    • Bollenbach, T.J.1    Stern, D.B.2
  • 11
    • 0346056732 scopus 로고    scopus 로고
    • CSP41, a multifunctional RNA-binding protein, initiates mRNA turnover in tobacco chloroplasts
    • Bollenbach T.J., Tatman D.A., Stern D.B. CSP41, a multifunctional RNA-binding protein, initiates mRNA turnover in tobacco chloroplasts. Plant J. 36:2003;842-852
    • (2003) Plant J. , vol.36 , pp. 842-852
    • Bollenbach, T.J.1    Tatman, D.A.2    Stern, D.B.3
  • 12
    • 0035205438 scopus 로고    scopus 로고
    • Plastid transcription: A menage à trois
    • Cahoon A.B., Stern D.B. Plastid transcription: a menage à trois. Trends Plant Sci. 6:2001;45-46
    • (2001) Trends Plant Sci. , vol.6 , pp. 45-46
    • Cahoon, A.B.1    Stern, D.B.2
  • 13
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O., Nielsen H., Von Heijne G. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8:1999;978-984
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 14
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J.K., McCormack A.L., Yates III J.R. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5:1994;976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 15
    • 0032903448 scopus 로고    scopus 로고
    • Organellar RNA polymerases of higher plants
    • Hess W.R., Börner T. Organellar RNA polymerases of higher plants. Int. Rev. Cytol. 190:1999;1-59
    • (1999) Int. Rev. Cytol. , vol.190 , pp. 1-59
    • Hess, W.R.1    Börner, T.2
  • 16
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg C.I., Tran S.E.F., Eriksson J.E., Sistonen L. Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem. Sci. 27:2002;619-627
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 619-627
    • Holmberg, C.I.1    Tran, S.E.F.2    Eriksson, J.E.3    Sistonen, L.4
  • 17
    • 0037353231 scopus 로고    scopus 로고
    • DNA-binding and transcription characteristics of three cloned sigma factors from mustard (Sinapis alba L.) suggest overlapping and distinct roles in plastid gene expression
    • Homann A., Link G. DNA-binding and transcription characteristics of three cloned sigma factors from mustard (Sinapis alba L.) suggest overlapping and distinct roles in plastid gene expression. Eur. J. Biochem. 270:2003;1288-1300
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1288-1300
    • Homann, A.1    Link, G.2
  • 18
    • 0025189863 scopus 로고
    • Maize chloroplast RNA polymerase: The 180-,120-, and 38-kDa polypeptides are encoded in chloroplast genes
    • Hu J., Bogorad L. Maize chloroplast RNA polymerase: The 180-,120-, and 38-kDa polypeptides are encoded in chloroplast genes. Proc. Natl. Acad. Sci. USA. 87:1990;1531-1535
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1531-1535
    • Hu, J.1    Bogorad, L.2
  • 19
    • 0025834037 scopus 로고
    • Maize chloroplast RNA polymerase: The 78-kDa polypeptide is encoded by the plastid rpoC1 gene
    • Hu J., Troxler R.F., Bogorad L. Maize chloroplast RNA polymerase: The 78-kDa polypeptide is encoded by the plastid rpoC1 gene. Nucleic Acids Res. 19:1991;3431-3434
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3431-3434
    • Hu, J.1    Troxler, R.F.2    Bogorad, L.3
  • 20
    • 0037296184 scopus 로고    scopus 로고
    • Redox regulation of chloroplast transcription
    • Link G. Redox regulation of chloroplast transcription. Antiox. Redox Signal. 5:2003;79-88
    • (2003) Antiox. Redox Signal , vol.5 , pp. 79-88
    • Link, G.1
  • 21
    • 0031934554 scopus 로고    scopus 로고
    • Two plastid RNA polymerases of higher plants: An evolving story
    • Maliga P. Two plastid RNA polymerases of higher plants: an evolving story. Trends Plant Sci. 3:1998;4-6
    • (1998) Trends Plant Sci. , vol.3 , pp. 4-6
    • Maliga, P.1
  • 22
    • 0033861250 scopus 로고    scopus 로고
    • Processing and degradation of chloroplast mRNA
    • Monde R.A., Schuster G., Stern D.B. Processing and degradation of chloroplast mRNA. Biochimie. 82:2000;573-582
    • (2000) Biochimie , vol.82 , pp. 573-582
    • Monde, R.A.1    Schuster, G.2    Stern, D.B.3
  • 23
    • 0027105007 scopus 로고
    • A knowledge base for prediction of protein localization sites in eukaryotic cells
    • Nakai K., Kanehisa M. A knowledge base for prediction of protein localization sites in eukaryotic cells. Genomics. 14:1992;897-911
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 24
    • 0035476623 scopus 로고    scopus 로고
    • Crystal structure of human protein kinase CK2: Insights into basic properties of the CK2 holoenzyme
    • Niefind K., Guerra B., Ermakowa I., Issinger O.G. Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20:2001;5320-5331
    • (2001) EMBO J. , vol.20 , pp. 5320-5331
    • Niefind, K.1    Guerra, B.2    Ermakowa, I.3    Issinger, O.G.4
  • 25
    • 0032079650 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 Å resolution
    • Niefind K., Guerra B., Pinna L.A., Issinger O.G., Schomburg D. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 Å resolution. EMBO J. 17:1998;2451-2462
    • (1998) EMBO J. , vol.17 , pp. 2451-2462
    • Niefind, K.1    Guerra, B.2    Pinna, L.A.3    Issinger, O.G.4    Schomburg, D.5
  • 26
    • 0036302161 scopus 로고    scopus 로고
    • The plastid transcription kinase from mustard (Sinapis alba L.) - A nuclear-encoded CK2-type chloroplast enzyme with redox-sensitive function
    • Ogrzewalla K., Piotrowski M., Reinbothe S., Link G. The plastid transcription kinase from mustard (Sinapis alba L.) - a nuclear-encoded CK2-type chloroplast enzyme with redox-sensitive function. Eur. J. Biochem. 269:2002;3329-3337
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3329-3337
    • Ogrzewalla, K.1    Piotrowski, M.2    Reinbothe, S.3    Link, G.4
  • 27
    • 0028408167 scopus 로고
    • Separation of two classes of plastid DNA-dependent RNA polymerases that are differentially expressed in mustard (Sinapis alba L.) seedlings
    • Pfannschmidt T., Link G. Separation of two classes of plastid DNA-dependent RNA polymerases that are differentially expressed in mustard (Sinapis alba L.) seedlings. Plant Mol. Biol. 25:1994;69-81
    • (1994) Plant Mol. Biol. , vol.25 , pp. 69-81
    • Pfannschmidt, T.1    Link, G.2
  • 28
    • 0033962832 scopus 로고    scopus 로고
    • The multisubunit chloroplast RNA polymerase a from mustard (Sinapis alba L.): Integration of a prokaryotic core into a larger complex with organelle-specific functions
    • Pfannschmidt T., Ogrzewalla K., Baginsky S., Sickmann A., Meyer H.E., Link G. The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba L.): integration of a prokaryotic core into a larger complex with organelle-specific functions. Eur. J. Biochem. 267:2000;253-261
    • (2000) Eur. J. Biochem. , vol.267 , pp. 253-261
    • Pfannschmidt, T.1    Ogrzewalla, K.2    Baginsky, S.3    Sickmann, A.4    Meyer, H.E.5    Link, G.6
  • 29
    • 0030919235 scopus 로고    scopus 로고
    • Molecules in focus: Protein kinase CK2
    • Pinna L.A. Molecules in focus: protein kinase CK2. Int. J. Biochem. Cell Biol. 29:1997;551-554
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 551-554
    • Pinna, L.A.1
  • 30
    • 0025948994 scopus 로고
    • Identification of phosphorylation sites in peptides using a microsequencer
    • Roach P.J., Wang Y. Identification of phosphorylation sites in peptides using a microsequencer. Methods Enzymol. 201:1991;200-206
    • (1991) Methods Enzymol. , vol.201 , pp. 200-206
    • Roach, P.J.1    Wang, Y.2
  • 31
    • 17344395359 scopus 로고    scopus 로고
    • Chloroplast transit peptide prediction: A peek inside the black box
    • Schein A.I., Kissinger J.C., Ungar L.H. Chloroplast transit peptide prediction: a peek inside the black box. Nucleic Acids Res. 29:2001;e82
    • (2001) Nucleic Acids Res. , vol.29 , pp. 82
    • Schein, A.I.1    Kissinger, J.C.2    Ungar, L.H.3
  • 32
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA. 95:1998;5857-5864
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 33
    • 0029310678 scopus 로고
    • Plant protein kinase families and signal transduction
    • Stone J.M., Walker J.C. Plant protein kinase families and signal transduction. Plant Physiol. 108:1995;451-457
    • (1995) Plant Physiol. , vol.108 , pp. 451-457
    • Stone, J.M.1    Walker, J.C.2
  • 34
    • 0030267939 scopus 로고    scopus 로고
    • Regulation of gene expression in chloroplasts of higher plants
    • Sugita M., Sugiura M. Regulation of gene expression in chloroplasts of higher plants. Plant Mol. Biol. 32:1996;315-326
    • (1996) Plant Mol. Biol. , vol.32 , pp. 315-326
    • Sugita, M.1    Sugiura, M.2
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0030221344 scopus 로고    scopus 로고
    • CSP41, a sequence-specific chloroplast mRNA-binding protein, is an endoribonuclease
    • Yang J.J., Schuster G., Stern D.B. CSP41, a sequence-specific chloroplast mRNA-binding protein, is an endoribonuclease. Plant Cell. 8:1996;1409-1420
    • (1996) Plant Cell , vol.8 , pp. 1409-1420
    • Yang, J.J.1    Schuster, G.2    Stern, D.B.3


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