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Volumn 95, Issue 2, 2013, Pages 400-409

Protein phosphorylation regulates in vitro spinach chloroplast petD mRNA 3′-untranslated region stability, processing, and degradation

Author keywords

Chloroplast; mRNA 3 UTR processing; mRNA degradation; Phosphorylation; RNA binding proteins

Indexed keywords

ADENOSINE TRIPHOSPHATE; MESSENGER RNA;

EID: 84872764411     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.10.012     Document Type: Article
Times cited : (7)

References (40)
  • 2
    • 0033861250 scopus 로고    scopus 로고
    • Processing and degradation of chloroplast mRNA
    • R.A. Monde, G. Schuster, and D.B. Stern 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
  • 3
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins
    • R. Hayes, J. Kudla, G. Schuster, L. Gabay, P. Maliga, and W. Gruissem Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins EMBO J. 15 1996 1132 1141
    • (1996) EMBO J. , vol.15 , pp. 1132-1141
    • Hayes, R.1    Kudla, J.2    Schuster, G.3    Gabay, L.4    Maliga, P.5    Gruissem, W.6
  • 5
    • 0025775279 scopus 로고
    • Chloroplast mRNA 3′-end processing requires a nuclear-encoded RNA-binding protein
    • G. Schuster, and W. Gruissem Chloroplast mRNA 3′-end processing requires a nuclear-encoded RNA-binding protein EMBO J. 10 1991 1493 1502
    • (1991) EMBO J. , vol.10 , pp. 1493-1502
    • Schuster, G.1    Gruissem, W.2
  • 6
    • 0024962578 scopus 로고
    • Function of plastid mRNA 3′ inverted repeats. RNA stabilization and gene-specific protein binding
    • D.B. Stern, H. Jones, and W. Gruissem Function of plastid mRNA 3′ inverted repeats. RNA stabilization and gene-specific protein binding J. Biol. Chem. 264 1989 18742 18750
    • (1989) J. Biol. Chem. , vol.264 , pp. 18742-18750
    • Stern, D.B.1    Jones, H.2    Gruissem, W.3
  • 7
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • B.M. Lunde, C. Moore, and G. Varani RNA-binding proteins: modular design for efficient function Nat. Rev. Mol. Cell. Biol. 8 2007 479 490
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 8
    • 0035808422 scopus 로고    scopus 로고
    • Chloroplasts ribonucleoproteins function as a stabilizing factor of ribosome-free mRNA in the stroma
    • T. Nakamura, M. Ohta, M. Sugiura, and M. Sugita Chloroplasts ribonucleoproteins function as a stabilizing factor of ribosome-free mRNA in the stroma J. Biol. Chem. 276 2001 147 152
    • (2001) J. Biol. Chem. , vol.276 , pp. 147-152
    • Nakamura, T.1    Ohta, M.2    Sugiura, M.3    Sugita, M.4
  • 9
    • 0032755049 scopus 로고    scopus 로고
    • Chloroplast ribonucleoproteins are associated with both mRNAs and intron-containing precursor tRNAs
    • T. Nakamura, M. Ohta, M. Sugiura, and M. Sugita Chloroplast ribonucleoproteins are associated with both mRNAs and intron-containing precursor tRNAs FEBS Lett. 460 1999 437 441
    • (1999) FEBS Lett. , vol.460 , pp. 437-441
    • Nakamura, T.1    Ohta, M.2    Sugiura, M.3    Sugita, M.4
  • 10
    • 0035282916 scopus 로고    scopus 로고
    • Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: Development of a chloroplast in vitro RNA editing system
    • T. Hirose, and M. Sugiura Involvement of a site-specific trans-acting factor and a common RNA-binding protein in the editing of chloroplast mRNAs: development of a chloroplast in vitro RNA editing system EMBO J. 20 2001 1144 1152
    • (2001) EMBO J. , vol.20 , pp. 1144-1152
    • Hirose, T.1    Sugiura, M.2
  • 12
    • 77953796346 scopus 로고    scopus 로고
    • Chloroplast RNA-binding proteins: Repair and regulation of chloroplast transcripts
    • M. Tillich, S. Beick, and C. Schmitz-Linneweber Chloroplast RNA-binding proteins: repair and regulation of chloroplast transcripts RNA Biol. 7 2010 172 178
    • (2010) RNA Biol. , vol.7 , pp. 172-178
    • Tillich, M.1    Beick, S.2    Schmitz-Linneweber, C.3
  • 14
    • 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
    • E. Baena-Gonzalez, S. Baginsky, P. Mulo, H. Summer, E.M. Aro, and G. Link 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-Gonzalez, E.1    Baginsky, S.2    Mulo, P.3    Summer, H.4    Aro, E.M.5    Link, G.6
  • 15
    • 0027173145 scopus 로고
    • Phosphorylation and dephosphorylation affect functional characteristics of chloroplast and etioplast transcription systems from mustard (Sinapis alba L.)
    • K. Tiller, and G. Link Phosphorylation and dephosphorylation affect functional characteristics of chloroplast and etioplast transcription systems from mustard (Sinapis alba L.) EMBO J. 12 1993 1745 1753
    • (1993) EMBO J. , vol.12 , pp. 1745-1753
    • Tiller, K.1    Link, G.2
  • 16
    • 0028222184 scopus 로고
    • ADP-dependent phosphorylation regulates RNA-binding in vitro: Implications in light-modulated translation
    • A. Danon, and S.P. Mayfield ADP-dependent phosphorylation regulates RNA-binding in vitro: implications in light-modulated translation EMBO J. 13 1994 2227 2235
    • (1994) EMBO J. , vol.13 , pp. 2227-2235
    • Danon, A.1    Mayfield, S.P.2
  • 18
    • 0030795521 scopus 로고    scopus 로고
    • Chloroplast endoribonuclease p54 involved in RNA 3′-end processing is regulated by phosphorylation and redox state
    • K. Liere, and G. Link Chloroplast endoribonuclease p54 involved in RNA 3′-end processing is regulated by phosphorylation and redox state Nucleic Acids Res. 25 1997 2403 2408
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2403-2408
    • Liere, K.1    Link, G.2
  • 19
    • 0029061736 scopus 로고
    • Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA
    • I. Lisitsky, and G. Schuster Phosphorylation of a chloroplast RNA-binding protein changes its affinity to RNA Nucleic Acids Res. 23 1995 2506 2511
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2506-2511
    • Lisitsky, I.1    Schuster, G.2
  • 21
    • 0024673605 scopus 로고
    • Post-transcriptional control of plastid mRNA accumulation during adaptation of chloroplasts to different light quality environments
    • X.W. Deng, J.C. Tonkyn, G.F. Peter, J.P. Thomber, and W. Gruissem Post-transcriptional control of plastid mRNA accumulation during adaptation of chloroplasts to different light quality environments Plant Cell 1 1989 645 654
    • (1989) Plant Cell , vol.1 , pp. 645-654
    • Deng, X.W.1    Tonkyn, J.C.2    Peter, G.F.3    Thomber, J.P.4    Gruissem, W.5
  • 22
    • 0022603813 scopus 로고
    • Chloroplast gene expression and promoter identification in chloroplast extracts
    • W. Gruissem, B.M. Greenberg, G. Zurawski, and R.B. Hallick Chloroplast gene expression and promoter identification in chloroplast extracts Methods Enzymol. 118 1986 253 270
    • (1986) Methods Enzymol. , vol.118 , pp. 253-270
    • Gruissem, W.1    Greenberg, B.M.2    Zurawski, G.3    Hallick, R.B.4
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0023663880 scopus 로고
    • Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription
    • D.B. Stern, and W. Gruissem Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription Cell 51 1987 1145 1157
    • (1987) Cell , vol.51 , pp. 1145-1157
    • Stern, D.B.1    Gruissem, W.2
  • 25
    • 33751021696 scopus 로고    scopus 로고
    • Purification and characterization of a calcium-dependent protein kinase from beetroot plasma membranes
    • B. Lino, M.T. Carrillo-Rayas, A. Chagolla, and L.E. González de la Vara Purification and characterization of a calcium-dependent protein kinase from beetroot plasma membranes Planta 225 2006 255 268
    • (2006) Planta , vol.225 , pp. 255-268
    • Lino, B.1    Carrillo-Rayas, M.T.2    Chagolla, A.3    González De La Vara, L.E.4
  • 27
    • 0025784440 scopus 로고
    • Specific binding of chloroplast proteins in vitro to the 3′ untranslated region of spinach chloroplast petD mRNA
    • Ch Hsu-Ching, and D.B. Stern Specific binding of chloroplast proteins in vitro to the 3′ untranslated region of spinach chloroplast petD mRNA Mol. Cell. Biol. 11 1991 4380 4388
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4380-4388
    • Hsu-Ching, C.1    Stern, D.B.2
  • 31
    • 1642371610 scopus 로고    scopus 로고
    • Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts
    • Y. Balmer, A. Koller, G.D. Va, P. Schürmann, and B.B. Buchanan Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts Photosynth. Res. 79 2004 275 280
    • (2004) Photosynth. Res. , vol.79 , pp. 275-280
    • Balmer, Y.1    Koller, A.2    Va, G.D.3    Schürmann, P.4    Buchanan, B.B.5
  • 33
    • 84872812828 scopus 로고
    • Level of photosynthetic intermediates in isolated spinach chloroplasts
    • E. Latzko, and M. Gibbs Level of photosynthetic intermediates in isolated spinach chloroplasts Plant Physiol. 44 1969 396 402
    • (1969) Plant Physiol. , vol.44 , pp. 396-402
    • Latzko, E.1    Gibbs, M.2
  • 34
    • 0001060481 scopus 로고
    • Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplasts, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L.
    • R. Hampp, M. Goller, and H. Ziegler Adenylate levels, energy charge, and phosphorylation potential during dark-light and light-dark transition in chloroplasts, mitochondria, and cytosol of mesophyll protoplasts from Avena sativa L. Plant Physiol. 69 1982 448 455
    • (1982) Plant Physiol. , vol.69 , pp. 448-455
    • Hampp, R.1    Goller, M.2    Ziegler, H.3
  • 35
    • 0037109210 scopus 로고    scopus 로고
    • Endonucleolytic activation directs dark-induced chloroplast mRNA degradation
    • S. Baginsky, and W. Gruissem Endonucleolytic activation directs dark-induced chloroplast mRNA degradation Nucleic Acids Res. 30 2002 4527 4533
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4527-4533
    • Baginsky, S.1    Gruissem, W.2
  • 37
    • 77953284100 scopus 로고    scopus 로고
    • Molecular mechanisms of pre-mRNA 3′ end processing regulation
    • S. Millevoi, and S. Vagner Molecular mechanisms of pre-mRNA 3′ end processing regulation Nucleic Acids Res. 38 2010 2757 2774
    • (2010) Nucleic Acids Res. , vol.38 , pp. 2757-2774
    • Millevoi, S.1    Vagner, S.2
  • 38
    • 0034625414 scopus 로고    scopus 로고
    • The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B
    • H. Le, K.S. Browning, and D.R. Gallie The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B J. Biol. Chem. 275 2000 17452 17462
    • (2000) J. Biol. Chem. , vol.275 , pp. 17452-17462
    • Le, H.1    Browning, K.S.2    Gallie, D.R.3
  • 39
    • 37749052472 scopus 로고    scopus 로고
    • Control of protein translation by phosphorylation of the mRNA 5′-cap-binding complex
    • O.A. Pierrat, V. Mikitova, M.S. Bush, K.S. Browning, and J.H. Doonan Control of protein translation by phosphorylation of the mRNA 5′-cap-binding complex Biochem. Soc. Trans. 35 2007 1634 1637
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1634-1637
    • Pierrat, O.A.1    Mikitova, V.2    Bush, M.S.3    Browning, K.S.4    Doonan, J.H.5
  • 40
    • 0033579464 scopus 로고    scopus 로고
    • Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites
    • N. Blom, S. Gammeltoft, and S. Brunak 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


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