메뉴 건너뛰기




Volumn 19, Issue 8, 2007, Pages 2606-2623

A ribonuclease III domain protein functions in group II intron splicing in maize chloroplasts

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; ENZYMES; GENES; IMMUNOLOGY; MUTAGENESIS; RNA;

EID: 35348861922     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.107.053736     Document Type: Article
Times cited : (94)

References (63)
  • 1
    • 33845674625 scopus 로고    scopus 로고
    • Arabidopsis orthologs of maize chloroplast splicing factors promote splicing of orthologous and species-specific group II introns
    • Asakura, Y., and Barkan, A. (2006). Arabidopsis orthologs of maize chloroplast splicing factors promote splicing of orthologous and species-specific group II introns. Plant Physiol. 142: 1656-1663.
    • (2006) Plant Physiol , vol.142 , pp. 1656-1663
    • Asakura, Y.1    Barkan, A.2
  • 2
    • 0001829914 scopus 로고
    • Nuclear mutants of maize with defects in chloroplast polysome assembly have altered RNA metabolism
    • Barkan, A. (1993). Nuclear mutants of maize with defects in chloroplast polysome assembly have altered RNA metabolism. Plant Cell 5: 389-402.
    • (1993) Plant Cell , vol.5 , pp. 389-402
    • Barkan, A.1
  • 3
    • 0031721059 scopus 로고    scopus 로고
    • Approaches to investigating nuclear genes that function in chloroplast biogenesis in land plants
    • Barkan, A. (1998). Approaches to investigating nuclear genes that function in chloroplast biogenesis in land plants. Methods Enzymol. 297: 38-57.
    • (1998) Methods Enzymol , vol.297 , pp. 38-57
    • Barkan, A.1
  • 4
    • 33845895281 scopus 로고    scopus 로고
    • The CRM domain: An RNA binding module derived from an ancient ribosome-associated protein
    • Barkan, A., Klipcan, L., Ostersetzer, O., Kawamura, T., Asakura, Y., and Watkins, K. (2007). The CRM domain: An RNA binding module derived from an ancient ribosome-associated protein. RNA 13: 55-64.
    • (2007) RNA , vol.13 , pp. 55-64
    • Barkan, A.1    Klipcan, L.2    Ostersetzer, O.3    Kawamura, T.4    Asakura, Y.5    Watkins, K.6
  • 5
    • 0028272427 scopus 로고
    • A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms
    • Barkan, A., Walker, M., Nolasco, M., and Johnson, D. (1994). A nuclear mutation in maize blocks the processing and translation of several chloroplast mRNAs and provides evidence for the differential translation of alternative mRNA forms. EMBO J. 13: 3170-3181.
    • (1994) EMBO J , vol.13 , pp. 3170-3181
    • Barkan, A.1    Walker, M.2    Nolasco, M.3    Johnson, D.4
  • 6
    • 0035662491 scopus 로고    scopus 로고
    • Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage
    • Blaszczyk, J., Tropea, J.E., Bubunenko, M., Routzahn, K.M., Waugh, D.S., Court, D.L., and Ji, X. (2001). Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. Structure 9: 1225-1236.
    • (2001) Structure , vol.9 , pp. 1225-1236
    • Blaszczyk, J.1    Tropea, J.E.2    Bubunenko, M.3    Routzahn, K.M.4    Waugh, D.S.5    Court, D.L.6    Ji, X.7
  • 7
    • 0035368207 scopus 로고    scopus 로고
    • The ins and outs of group II introns
    • Bonen, L., and Vogel, J. (2001). The ins and outs of group II introns. Trends Genet. 17: 322-331.
    • (2001) Trends Genet , vol.17 , pp. 322-331
    • Bonen, L.1    Vogel, J.2
  • 8
    • 33645008830 scopus 로고    scopus 로고
    • Structural perspective on the activation of RNase P RNA by protein
    • Buck, A., Kazantsev, A., Dalby, A., and Pace, N. (2005). Structural perspective on the activation of RNase P RNA by protein. Nat. Struct. Mol. Biol. 12: 958-964.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 958-964
    • Buck, A.1    Kazantsev, A.2    Dalby, A.3    Pace, N.4
  • 9
    • 0038054468 scopus 로고    scopus 로고
    • RNAse III-mediated degradation of unspliced pre-mRNAs and lariat introns
    • Danin-Kreiselman, M., Lee, C.Y., and Chanfreau, G. (2003). RNAse III-mediated degradation of unspliced pre-mRNAs and lariat introns. Mol. Cell 11: 1279-1289.
    • (2003) Mol. Cell , vol.11 , pp. 1279-1289
    • Danin-Kreiselman, M.1    Lee, C.Y.2    Chanfreau, G.3
  • 10
    • 0035852328 scopus 로고    scopus 로고
    • Prediction of organellar targeting signals
    • Emanuelsson, O., and von Heijne, G. (2001). Prediction of organellar targeting signals. Biochim. Biophys. Acta 1541: 114-119.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 114-119
    • Emanuelsson, O.1    von Heijne, G.2
  • 11
    • 31044448524 scopus 로고    scopus 로고
    • Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
    • Gan, J., Tropea, J.E., Austin, B.P., Court, D.L., Waugh, D.S., and Ji, X. (2006). Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell 124: 355-366.
    • (2006) Cell , vol.124 , pp. 355-366
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 13
    • 33947362880 scopus 로고    scopus 로고
    • Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA
    • Grohman, J.K., DelCampo, M., Bhaskaran, H., Tijerina, P., Lambowitz, A.M., and Russell, R. (2007). Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA. Biochemistry 46: 3013-3022.
    • (2007) Biochemistry , vol.46 , pp. 3013-3022
    • Grohman, J.K.1    DelCampo, M.2    Bhaskaran, H.3    Tijerina, P.4    Lambowitz, A.M.5    Russell, R.6
  • 14
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls, C., Mohr, S., Del Campo, M., Yang, Q., Jankowsky, E., and Lambowitz, A.M. (2007). Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J. Mol. Biol. 365: 835-855.
    • (2007) J. Mol. Biol , vol.365 , pp. 835-855
    • Halls, C.1    Mohr, S.2    Del Campo, M.3    Yang, Q.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 15
    • 0000196802 scopus 로고
    • Aberrations in plastid transcripts and deficiency of plastid DNA in striped and albino mutants in maize
    • Han, C.-D., Patrie, W., Polacco, M., and Coe, E.H. (1993). Aberrations in plastid transcripts and deficiency of plastid DNA in striped and albino mutants in maize. Planta 191: 552-563.
    • (1993) Planta , vol.191 , pp. 552-563
    • Han, C.-D.1    Patrie, W.2    Polacco, M.3    Coe, E.H.4
  • 16
    • 10644234841 scopus 로고    scopus 로고
    • The Drosha-DGCR8 complex in primary microRNA processing
    • Han, J., Lee, Y., Yeom, K.H., Kim, Y.K., Jin, H., and Kim, V.N. (2004). The Drosha-DGCR8 complex in primary microRNA processing. Genes Dev. 18: 3016-3027.
    • (2004) Genes Dev , vol.18 , pp. 3016-3027
    • Han, J.1    Lee, Y.2    Yeom, K.H.3    Kim, Y.K.4    Jin, H.5    Kim, V.N.6
  • 17
    • 0028520705 scopus 로고
    • Inefficient rpl2 splicing in barley mutants with ribosome-deficient plastids
    • Hess, W.R., Hoch, B., Zeltz, P., Huebschmann, T., Koessel, H., and Boerner, T. (1994). Inefficient rpl2 splicing in barley mutants with ribosome-deficient plastids. Plant Cell 6: 1455-1465.
    • (1994) Plant Cell , vol.6 , pp. 1455-1465
    • Hess, W.R.1    Hoch, B.2    Zeltz, P.3    Huebschmann, T.4    Koessel, H.5    Boerner, T.6
  • 18
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang, H.R., Rowe, C.E., Mohr, S., Jiang, Y., Lambowitz, A.M., and Perlman, P.S. (2005). The splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc. Natl. Acad. Sci. USA 102: 163-168.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 163-168
    • Huang, H.R.1    Rowe, C.E.2    Mohr, S.3    Jiang, Y.4    Lambowitz, A.M.5    Perlman, P.S.6
  • 19
    • 0035865141 scopus 로고    scopus 로고
    • Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts
    • Jenkins, B., and Barkan, A. (2001). Recruitment of a peptidyl-tRNA hydrolase as a facilitator of group II intron splicing in chloroplasts. EMBO J. 20: 872-879.
    • (2001) EMBO J , vol.20 , pp. 872-879
    • Jenkins, B.1    Barkan, A.2
  • 20
    • 0031106356 scopus 로고    scopus 로고
    • Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors
    • Jenkins, B., Kulhanek, D., and Barkan, A. (1997). Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors. Plant Cell 9: 283-296.
    • (1997) Plant Cell , vol.9 , pp. 283-296
    • Jenkins, B.1    Kulhanek, D.2    Barkan, A.3
  • 21
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust, R., Tözsér, K., Fox, J., Anderson, D., Cherry, S., Copeland, T., and Waugh, D. (2001). Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng. 14: 993-1000.
    • (2001) Protein Eng , vol.14 , pp. 993-1000
    • Kapust, R.1    Tözsér, K.2    Fox, J.3    Anderson, D.4    Cherry, S.5    Copeland, T.6    Waugh, D.7
  • 22
    • 0002671710 scopus 로고    scopus 로고
    • Group I and group II ribozymes as RNPs: Clues to the past and guides to the future
    • In The, R. Gesteland, T. Cech, and J. Atkins, eds Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp
    • Lambowitz, A., Caprara, M., Zimmerly, S., and Perlman, P. (1999). Group I and group II ribozymes as RNPs: Clues to the past and guides to the future. In The RNA World, R. Gesteland, T. Cech, and J. Atkins, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 451-485.
    • (1999) RNA World , pp. 451-485
    • Lambowitz, A.1    Caprara, M.2    Zimmerly, S.3    Perlman, P.4
  • 24
    • 33846927800 scopus 로고    scopus 로고
    • Ribonuclease revisited: Structural insights into ribonuclease III family enzymes
    • MacRae, I.J., and Doudna, J.A. (2007). Ribonuclease revisited: Structural insights into ribonuclease III family enzymes. Curr. Opin. Struct. Biol. 17: 138-145.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 138-145
    • MacRae, I.J.1    Doudna, J.A.2
  • 25
    • 0025264862 scopus 로고
    • Somatically heritable switches in the DNA modification of Mu transposable elements monitored with a suppressible mutant in maize
    • Martienssen, R., Barkan, A., Taylor, W., and Freeling, M. (1990). Somatically heritable switches in the DNA modification of Mu transposable elements monitored with a suppressible mutant in maize. Genes Dev. 4: 331-343.
    • (1990) Genes Dev , vol.4 , pp. 331-343
    • Martienssen, R.1    Barkan, A.2    Taylor, W.3    Freeling, M.4
  • 26
    • 0037126592 scopus 로고    scopus 로고
    • Mechanism of maturase-promoted group II intron splicing
    • Matsuura, M., Noah, J., and Lambowitz, A. (2001). Mechanism of maturase-promoted group II intron splicing. EMBO J. 20: 7259-7270.
    • (2001) EMBO J , vol.20 , pp. 7259-7270
    • Matsuura, M.1    Noah, J.2    Lambowitz, A.3
  • 27
    • 0038457836 scopus 로고    scopus 로고
    • HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs
    • Meierhoff, K., Felder, S., Nakamura, T., Bechtold, N., and Schuster, G. (2003). HCF152, an Arabidopsis RNA binding pentatricopeptide repeat protein involved in the processing of chloroplast psbB-psbT-psbH-petB-petD RNAs. Plant Cell 15: 1480-1495.
    • (2003) Plant Cell , vol.15 , pp. 1480-1495
    • Meierhoff, K.1    Felder, S.2    Nakamura, T.3    Bechtold, N.4    Schuster, G.5
  • 29
    • 0024428420 scopus 로고
    • Comparative and functional anatomy of group II catalytic introns - A review
    • Michel, F., Umesono, K., and Ozeki, H. (1989). Comparative and functional anatomy of group II catalytic introns - A review. Gene 82: 5-30.
    • (1989) Gene , vol.82 , pp. 5-30
    • Michel, F.1    Umesono, K.2    Ozeki, H.3
  • 30
    • 7044272280 scopus 로고    scopus 로고
    • Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses
    • Mili, S., and Steitz, J.A. (2004). Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. RNA 10: 1692-1694.
    • (2004) RNA , vol.10 , pp. 1692-1694
    • Mili, S.1    Steitz, J.A.2
  • 31
    • 33644852160 scopus 로고    scopus 로고
    • A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone
    • Mohr, S., Matsuura, M., Perlman, P.S., and Lambowitz, A.M. (2006). A DEAD-box protein alone promotes group II intron splicing and reverse splicing by acting as an RNA chaperone. Proc. Natl. Acad. Sci. USA 103: 3569-3574.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3569-3574
    • Mohr, S.1    Matsuura, M.2    Perlman, P.S.3    Lambowitz, A.M.4
  • 32
    • 0242381359 scopus 로고    scopus 로고
    • 2+ concentration on group II intron RNA folding investigated by UV cross-linking
    • 2+ concentration on group II intron RNA folding investigated by UV cross-linking. Biochemistry 42: 12466-12480.
    • (2003) Biochemistry , vol.42 , pp. 12466-12480
    • Noah, J.1    Lambowitz, A.2
  • 33
    • 26944458557 scopus 로고    scopus 로고
    • CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains
    • Ostersetzer, O., Watkins, K., Cooke, A., and Barkan, A. (2005). CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains. Plant Cell 17: 241-255.
    • (2005) Plant Cell , vol.17 , pp. 241-255
    • Ostersetzer, O.1    Watkins, K.2    Cooke, A.3    Barkan, A.4
  • 34
    • 0042525906 scopus 로고    scopus 로고
    • Group II intron splicing factors derived by diversification of an ancient RNA binding module
    • Ostheimer, G., Williams-Carrier, R., Belcher, S., Osborne, E., Gierke, J., and Barkan, A. (2003). Group II intron splicing factors derived by diversification of an ancient RNA binding module. EMBO J. 22: 3919-3929.
    • (2003) EMBO J , vol.22 , pp. 3919-3929
    • Ostheimer, G.1    Williams-Carrier, R.2    Belcher, S.3    Osborne, E.4    Gierke, J.5    Barkan, A.6
  • 35
    • 9744285756 scopus 로고    scopus 로고
    • Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces
    • Ostheimer, G.J., Hadjivassiliou, H., Kloer, D.P., Barkan, A., and Matthews, B.W. (2005). Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. J. Mol. Biol. 345: 51-68.
    • (2005) J. Mol. Biol , vol.345 , pp. 51-68
    • Ostheimer, G.J.1    Hadjivassiliou, H.2    Kloer, D.P.3    Barkan, A.4    Matthews, B.W.5
  • 36
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 11: 2411-2423.
    • (1995) Protein Sci , vol.11 , pp. 2411-2423
    • Pace, C.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 37
    • 0033571587 scopus 로고    scopus 로고
    • A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • Perron, K., Goldschmidt-Clermont, M., and Rochaix, J.-D. (1999). A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J. 18: 6481-6490.
    • (1999) EMBO J , vol.18 , pp. 6481-6490
    • Perron, K.1    Goldschmidt-Clermont, M.2    Rochaix, J.-D.3
  • 38
    • 27844569938 scopus 로고    scopus 로고
    • Group II introns: Ribozymes that splice RNA and invade DNA
    • In The, R. Gesteland, T. Cech, and J. Atkins, eds Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp
    • Pyle, A., and Lambowitz, A. (2006). Group II introns: Ribozymes that splice RNA and invade DNA. In The RNA World, R. Gesteland, T. Cech, and J. Atkins, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 469-506.
    • (2006) RNA World , pp. 469-506
    • Pyle, A.1    Lambowitz, A.2
  • 39
    • 33847676447 scopus 로고    scopus 로고
    • Folding of group II introns: A model system for large, multidomain RNAs?
    • Pyle, A.M., Fedorova, O., and Waldsich, C. (2007). Folding of group II introns: A model system for large, multidomain RNAs? Trends Biochem. Sci. 32: 138-145.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 138-145
    • Pyle, A.M.1    Fedorova, O.2    Waldsich, C.3
  • 41
    • 2542540696 scopus 로고    scopus 로고
    • Assembly of an active group II intron-maturase complex by protein dimerization
    • Rambo, R.P., and Doudna, J.A. (2004). Assembly of an active group II intron-maturase complex by protein dimerization. Biochemistry 43: 6486-6497.
    • (2004) Biochemistry , vol.43 , pp. 6486-6497
    • Rambo, R.P.1    Doudna, J.A.2
  • 42
    • 0035794689 scopus 로고    scopus 로고
    • Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • Rivier, C., Goldschmidt-Clermont, M., and Rochaix, J. (2001). Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J. 20: 1765-1773.
    • (2001) EMBO J , vol.20 , pp. 1765-1773
    • Rivier, C.1    Goldschmidt-Clermont, M.2    Rochaix, J.3
  • 43
    • 31544432771 scopus 로고    scopus 로고
    • RNA immunoprecipitation and microarray analysis show a chloroplast pentatricopeptide repeat protein to be associated with the 5′-region of mRNAs whose translation it activates
    • Schmitz-Linneweber, C., Williams-Carrier, R., and Barkan, A. (2005). RNA immunoprecipitation and microarray analysis show a chloroplast pentatricopeptide repeat protein to be associated with the 5′-region of mRNAs whose translation it activates. Plant Cell 17: 2791-2804.
    • (2005) Plant Cell , vol.17 , pp. 2791-2804
    • Schmitz-Linneweber, C.1    Williams-Carrier, R.2    Barkan, A.3
  • 45
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained in polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996). Mass spectrometric sequencing of proteins silver-stained in polyacrylamide gels. Anal. Chem. 68: 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 46
    • 0033965922 scopus 로고    scopus 로고
    • The PPR motif - A TPR-related motif prevalent in plant organellar proteins
    • Small, I., and Peeters, N. (2000). The PPR motif - A TPR-related motif prevalent in plant organellar proteins. Trends Biochem. Sci. 25: 46-47.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 46-47
    • Small, I.1    Peeters, N.2
  • 47
    • 0036233276 scopus 로고    scopus 로고
    • A novel mechanism for protein-assisted group I intron splicing
    • Solem, A., Chatterjee, P., and Caprara, M. (2002). A novel mechanism for protein-assisted group I intron splicing. RNA 8: 412-425.
    • (2002) RNA , vol.8 , pp. 412-425
    • Solem, A.1    Chatterjee, P.2    Caprara, M.3
  • 48
    • 33847652952 scopus 로고    scopus 로고
    • A DEAD protein that activates intron self-splicing without unwinding RNA
    • Solem, A., Zingler, N., and Pyle, A.M. (2006). A DEAD protein that activates intron self-splicing without unwinding RNA. Mol. Cell 24: 611-617.
    • (2006) Mol. Cell , vol.24 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.3
  • 49
    • 2642512446 scopus 로고    scopus 로고
    • Genetics and genomics of chloroplast biogenesis: Maize as a model system
    • Stern, D., Hanson, M., and Barkan, A. (2004). Genetics and genomics of chloroplast biogenesis: Maize as a model system. Trends Plant Sci. 9: 293-301.
    • (2004) Trends Plant Sci , vol.9 , pp. 293-301
    • Stern, D.1    Hanson, M.2    Barkan, A.3
  • 50
    • 0035846580 scopus 로고    scopus 로고
    • Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain
    • Sun, W., Jun, E., and Nicholson, A.W. (2001). Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain. Biochemistry 40: 14976-14984.
    • (2001) Biochemistry , vol.40 , pp. 14976-14984
    • Sun, W.1    Jun, E.2    Nicholson, A.W.3
  • 51
    • 5444237407 scopus 로고    scopus 로고
    • Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III. Identification of conserved acidic residues that are important for catalytic function in vitro
    • Sun, W., Li, G., and Nicholson, A.W. (2004). Mutational analysis of the nuclease domain of Escherichia coli ribonuclease III. Identification of conserved acidic residues that are important for catalytic function in vitro. Biochemistry 43: 13054-13062.
    • (2004) Biochemistry , vol.43 , pp. 13054-13062
    • Sun, W.1    Li, G.2    Nicholson, A.W.3
  • 52
    • 0035942357 scopus 로고    scopus 로고
    • 2+ rescue of the Glu117Asp mutant
    • 2+ rescue of the Glu117Asp mutant. Biochemistry 40: 5102-5110.
    • (2001) Biochemistry , vol.40 , pp. 5102-5110
    • Sun, W.1    Nicholson, A.W.2
  • 53
    • 0034844560 scopus 로고    scopus 로고
    • CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin
    • Till, B., Schmitz-Linneweber, C., Williams-Carrier, R., and Barkan, A. (2001). CRS1 is a novel group II intron splicing factor that was derived from a domain of ancient origin. RNA 7: 1227-1238.
    • (2001) RNA , vol.7 , pp. 1227-1238
    • Till, B.1    Schmitz-Linneweber, C.2    Williams-Carrier, R.3    Barkan, A.4
  • 54
    • 0029087927 scopus 로고
    • Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid
    • Voelker, R., and Barkan, A. (1995). Two nuclear mutations disrupt distinct pathways for targeting proteins to the chloroplast thylakoid. EMBO J. 14: 3905-3914.
    • (1995) EMBO J , vol.14 , pp. 3905-3914
    • Voelker, R.1    Barkan, A.2
  • 55
    • 0345062264 scopus 로고    scopus 로고
    • Comparative analysis of splicing of the complete set of chloroplast group II introns in three higher plant mutants
    • Vogel, J., Boerner, T., and Hess, W. (1999). Comparative analysis of splicing of the complete set of chloroplast group II introns in three higher plant mutants. Nucleic Acids Res. 27: 3866-3874.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3866-3874
    • Vogel, J.1    Boerner, T.2    Hess, W.3
  • 56
    • 17044461720 scopus 로고    scopus 로고
    • Splicing and intron-internal RNA editing of trnK-matK transcripts in barley plastids: Support for MatK as an essential splice factor
    • Vogel, J., Hubschmann, T., Borner, T., and Hess, W. (1997). Splicing and intron-internal RNA editing of trnK-matK transcripts in barley plastids: Support for MatK as an essential splice factor. J. Mol. Biol. 270: 179-187.
    • (1997) J. Mol. Biol , vol.270 , pp. 179-187
    • Vogel, J.1    Hubschmann, T.2    Borner, T.3    Hess, W.4
  • 57
    • 0018421338 scopus 로고
    • Nuclear gene iojap conditions a programmed change to ribosome-less plastids in Zea mays
    • Walbot, V., and Coe, E.H. (1979). Nuclear gene iojap conditions a programmed change to ribosome-less plastids in Zea mays. Proc. Natl. Acad. Sci. USA 76: 2760-2764.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2760-2764
    • Walbot, V.1    Coe, E.H.2
  • 58
    • 33846102840 scopus 로고    scopus 로고
    • POGs/PlantRBP: A resource for comparative genomics in plants
    • Walker, N.S., Stiffler, N., and Barkan, A. (2007). POGs/PlantRBP: A resource for comparative genomics in plants. Nucleic Acids Res. 35: D852-D856.
    • (2007) Nucleic Acids Res , vol.35
    • Walker, N.S.1    Stiffler, N.2    Barkan, A.3
  • 59
    • 0029050588 scopus 로고
    • Efficient protein-facilitated splicing of the yeast mitochondrial bI5 intron
    • Weeks, K.M., and Cech, T.R. (1995). Efficient protein-facilitated splicing of the yeast mitochondrial bI5 intron. Biochemistry 34: 7728-7738.
    • (1995) Biochemistry , vol.34 , pp. 7728-7738
    • Weeks, K.M.1    Cech, T.R.2
  • 60
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D., and Flugge, U.I. (1984). A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138: 141-143.
    • (1984) Anal. Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 61
    • 0344237359 scopus 로고    scopus 로고
    • A chloroplast-localized PPR protein required for plastid ribosome accumulation
    • Williams, P., and Barkan, A. (2003). A chloroplast-localized PPR protein required for plastid ribosome accumulation. Plant J. 36: 675-686.
    • (2003) Plant J , vol.36 , pp. 675-686
    • Williams, P.1    Barkan, A.2
  • 62
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong, I., and Lohman, T. (1993). A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions. Proc. Natl. Acad. Sci. USA 90: 5428-5432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.2
  • 63
    • 3142613181 scopus 로고    scopus 로고
    • Single processing center models for human Dicer and bacterial RNase III
    • Zhang, H., Kolb, F.A., Jaskiewicz, L., Westhof, E., and Filipowicz, W. (2004). Single processing center models for human Dicer and bacterial RNase III. Cell 118: 57-68.
    • (2004) Cell , vol.118 , pp. 57-68
    • Zhang, H.1    Kolb, F.A.2    Jaskiewicz, L.3    Westhof, E.4    Filipowicz, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.