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Volumn 56, Issue 3, 2013, Pages 123-129

Regulation of RNA metabolism in plant development and stress responses

Author keywords

Abiotic stress; Development; Posttranscriptional regulation; RNA chaperone; RNA metabolism; RNA binding protein

Indexed keywords


EID: 84879175204     PISSN: 12269239     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12374-013-0906-8     Document Type: Review
Times cited : (49)

References (98)
  • 1
    • 0031890522 scopus 로고    scopus 로고
    • Plant proteins containing the RNA-recognition motif
    • Albà MM, Pagès M (1998) Plant proteins containing the RNA-recognition motif. Trends Plant Sci 3: 15-21.
    • (1998) Trends Plant Sci , vol.3 , pp. 15-21
    • Albà, M.M.1    Pagès, M.2
  • 2
    • 0036387129 scopus 로고    scopus 로고
    • Salinity- and ABAinduced up-regulation and light-mediated modulation of mRNA encoding glycine-rich RNA-binding protein from Sorghum bicolor
    • Aneeta NS-M, Tuteja N, Sopory SK (2002) Salinity- and ABAinduced up-regulation and light-mediated modulation of mRNA encoding glycine-rich RNA-binding protein from Sorghum bicolor. Biochem Biophys Res Commun 296: 1063-1068.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 1063-1068
    • Aneeta, N.-M.1    Tuteja, N.2    Sopory, S.K.3
  • 4
    • 0034608861 scopus 로고    scopus 로고
    • Escherichia coli CspA-family RNA chaperones are transcription antiterminators
    • Bae W, Xia B, Inouye M et al (2000) Escherichia coli CspA-family RNA chaperones are transcription antiterminators. Proc Natl Acad Sci USA 97: 7784-7789.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7784-7789
    • Bae, W.1    Xia, B.2    Inouye, M.3
  • 5
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd CG, Dreyfuss G (1994) Conserved structures and diversity of functions of RNA-binding proteins. Science 265: 615-621.
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.G.1    Dreyfuss, G.2
  • 6
    • 77953393143 scopus 로고    scopus 로고
    • Post-transcriptional control of chloroplast gene expression
    • del Campo M (2009) Post-transcriptional control of chloroplast gene expression. Gene Regul Syst Biol 3: 31-47.
    • (2009) Gene Regul Syst Biol , vol.3 , pp. 31-47
    • del Campo, M.1
  • 7
    • 44949127189 scopus 로고    scopus 로고
    • Functional characterization of two cold shock domain proteins from Oryza sativa
    • Chaikam V, Karlson D (2008) Functional characterization of two cold shock domain proteins from Oryza sativa. Plant Cell Environ 31: 995-1006.
    • (2008) Plant Cell Environ , vol.31 , pp. 995-1006
    • Chaikam, V.1    Karlson, D.2
  • 8
    • 77951932118 scopus 로고    scopus 로고
    • Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins
    • Chaikam V, Karlson D (2010) Comparison of structure, function and regulation of plant cold shock domain proteins to bacterial and animal cold shock domain proteins. Biochem Mol Biol Rep 43: 1-8.
    • (2010) Biochem Mol Biol Rep , vol.43 , pp. 1-8
    • Chaikam, V.1    Karlson, D.2
  • 9
    • 79955857381 scopus 로고    scopus 로고
    • The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida
    • Chambers JR and Bender KS (2011) The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida. PLoS One 6: e19797.
    • (2011) PLoS One , vol.6
    • Chambers, J.R.1    Bender, K.S.2
  • 11
    • 78649360662 scopus 로고    scopus 로고
    • Characterization and expression analysis of four glycine-rich RNA-binding proteins involved in osmotic response in tobacco (Nicotiana tabacum cv. Xanthi)
    • Chen X, Zeng Q-C, Lu X-P, Yu D-Q, Li W-Z (2010) Characterization and expression analysis of four glycine-rich RNA-binding proteins involved in osmotic response in tobacco (Nicotiana tabacum cv. Xanthi). Agric Sci China 9: 1577-1587.
    • (2010) Agric Sci China , vol.9 , pp. 1577-1587
    • Chen, X.1    Zeng, Q.-C.2    Lu, X.-P.3    Yu, D.-Q.4    Li, W.-Z.5
  • 12
    • 0037239887 scopus 로고    scopus 로고
    • Two RNA binding proteins, HEN4 and HUA1, act in the processing of AGAMOUS pre-mRNA in Arabidopsis thaliana
    • Cheng Y, Kato N, Wang W, Li J, Chen X (2003) Two RNA binding proteins, HEN4 and HUA1, act in the processing of AGAMOUS pre-mRNA in Arabidopsis thaliana. Dev Cell 4: 53-66.
    • (2003) Dev Cell , vol.4 , pp. 53-66
    • Cheng, Y.1    Kato, N.2    Wang, W.3    Li, J.4    Chen, X.5
  • 13
    • 67449083443 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the soybean DEAD-box RNA helicase gene induced by low temperature and high salinity stress
    • Chung E, Cho CW, Yun BH, Choi HK, So HA, Lee SW, Lee JH (2009) Molecular cloning and characterization of the soybean DEAD-box RNA helicase gene induced by low temperature and high salinity stress. Gene 443: 91-99.
    • (2009) Gene , vol.443 , pp. 91-99
    • Chung, E.1    Cho, C.W.2    Yun, B.H.3    Choi, H.K.4    So, H.A.5    Lee, S.W.6    Lee, J.H.7
  • 17
    • 0024293872 scopus 로고
    • A gene induced by the plant hormone abscisic acid in response to water stress encodes a glycine-rich protein
    • Gómez J, Sánchez-Martínez D, Stiefel V et al (1988) A gene induced by the plant hormone abscisic acid in response to water stress encodes a glycine-rich protein. Nature 344: 262-264.
    • (1988) Nature , vol.344 , pp. 262-264
    • Gómez, J.1    Sánchez-Martínez, D.2    Stiefel, V.3
  • 18
    • 0037143756 scopus 로고    scopus 로고
    • RNA helicase-like protein as an early regulator of transcription factors for plant chilling and freezing tolerance
    • Gong Z, Lee H, Xiong L, Jagendorf A, Stevenson B, Zhu JK (2002) RNA helicase-like protein as an early regulator of transcription factors for plant chilling and freezing tolerance. Proc Natl Acad Sci USA 99: 11507-11512.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11507-11512
    • Gong, Z.1    Lee, H.2    Xiong, L.3    Jagendorf, A.4    Stevenson, B.5    Zhu, J.K.6
  • 19
    • 21444454906 scopus 로고    scopus 로고
    • A DEAD box RNA helicase is essential for mRNA export and important for development and stress responses in Arabidopsis
    • Gong Z, Dong CH, Lee H, Zhu J, Xiong L, Gong D, Stevenson B, Zhu JK (2005) A DEAD box RNA helicase is essential for mRNA export and important for development and stress responses in Arabidopsis. Plant Cell 17: 256-267.
    • (2005) Plant Cell , vol.17 , pp. 256-267
    • Gong, Z.1    Dong, C.H.2    Lee, H.3    Zhu, J.4    Xiong, L.5    Gong, D.6    Stevenson, B.7    Zhu, J.K.8
  • 20
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann PL, Marahiel MA (1998) A superfamily of proteins that contain the cold-shock domain. Trends Biochem Sci 23: 286-290.
    • (1998) Trends Biochem Sci , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 21
    • 84874517844 scopus 로고    scopus 로고
    • A DEAD box RNA helicase is critical for pre-mRNA splicing, cold-responsive gene regulation, and cold tolerance in Arabidopsis
    • Guan Q, Wu J, Zhang Y, Jiang C, Liu R, Chai C, Zhu J (2013) A DEAD box RNA helicase is critical for pre-mRNA splicing, cold-responsive gene regulation, and cold tolerance in Arabidopsis. Plant Cell 25: 342-56.
    • (2013) Plant Cell , vol.25 , pp. 342-356
    • Guan, Q.1    Wu, J.2    Zhang, Y.3    Jiang, C.4    Liu, R.5    Chai, C.6    Zhu, J.7
  • 22
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag D (1995) RNA chaperones and the RNA folding problem. J Biol Chem 270: 20871-20874.
    • (1995) J Biol Chem , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 23
    • 0027932780 scopus 로고
    • Characterization of a cDNA encoding a novel type of RNA-binding protein in tobacco: its expression and nucleic acid-binding properties
    • Hirose T, Sugita M, Sugiura M (1994) Characterization of a cDNA encoding a novel type of RNA-binding protein in tobacco: its expression and nucleic acid-binding properties. Mol Gen Genet 244: 360-366.
    • (1994) Mol Gen Genet , vol.244 , pp. 360-366
    • Hirose, T.1    Sugita, M.2    Sugiura, M.3
  • 24
    • 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 HR, Rowe CE, Mohr S, Jiang Y, Lambowitz AM, Perlman PS (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
  • 27
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: binding and rearranging
    • Jankowsky E (2011) RNA helicases at work: binding and rearranging. Trends Biochem Sci 36: 19-29.
    • (2011) Trends Biochem Sci , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 28
    • 0031015217 scopus 로고    scopus 로고
    • CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone
    • Jiang W, Hon Y, Inouye M (1997) CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone. J Biol Chem 272: 196-202.
    • (1997) J Biol Chem , vol.272 , pp. 196-202
    • Jiang, W.1    Hon, Y.2    Inouye, M.3
  • 29
    • 84873192633 scopus 로고    scopus 로고
    • Plant RNA chaperones in stress response
    • Kang H, Park SJ, Kwak KJ (2013) Plant RNA chaperones in stress response. Trends Plant Sci 18: 100-106.
    • (2013) Trends Plant Sci , vol.18 , pp. 100-106
    • Kang, H.1    Park, S.J.2    Kwak, K.J.3
  • 30
    • 36248937856 scopus 로고    scopus 로고
    • STRESS RESPONSE SUPPRESSOR1 and STRESS RESPONSE SUPPRESSOR2, two DEAD-box RNA helicases that attenuate Arabidopsis responses to multiple abiotic stresses
    • Kant P, Kant S, Gordon M, Shaked R, Barak S (2007) STRESS RESPONSE SUPPRESSOR1 and STRESS RESPONSE SUPPRESSOR2, two DEAD-box RNA helicases that attenuate Arabidopsis responses to multiple abiotic stresses. Plant Physiol 145: 814-830.
    • (2007) Plant Physiol , vol.145 , pp. 814-830
    • Kant, P.1    Kant, S.2    Gordon, M.3    Shaked, R.4    Barak, S.5
  • 31
    • 0037144529 scopus 로고    scopus 로고
    • A coldregulated nucleic acid-binding protein of winter wheat shares a domain with bacterial cold shock proteins
    • Karlson D, Nakaminami K, Toyomasu T, Imai R (2002) A coldregulated nucleic acid-binding protein of winter wheat shares a domain with bacterial cold shock proteins. J Biol Chem 277: 35248-35256.
    • (2002) J Biol Chem , vol.277 , pp. 35248-35256
    • Karlson, D.1    Nakaminami, K.2    Toyomasu, T.3    Imai, R.4
  • 32
    • 0037253256 scopus 로고    scopus 로고
    • Conservation of the cold shock domain protein family in plants
    • Karlson D, Imai R (2003) Conservation of the cold shock domain protein family in plants. Plant Physiol 131: 12-15.
    • (2003) Plant Physiol , vol.131 , pp. 12-15
    • Karlson, D.1    Imai, R.2
  • 33
    • 0025761656 scopus 로고
    • RNA recognition: towards identifying determinants of specificity
    • Kenan DJ, Query CC, Keene JD (1991) RNA recognition: towards identifying determinants of specificity. Trends Biochem Sci 16: 214-220.
    • (1991) Trends Biochem Sci , vol.16 , pp. 214-220
    • Kenan, D.J.1    Query, C.C.2    Keene, J.D.3
  • 34
    • 34247359545 scopus 로고    scopus 로고
    • Functional characterization of a glycine-rich RNA-binding protein2 in Arabidopsis thaliana under abiotic stress conditions
    • Kim JY, Park SJ, Jang B, Jung C-H, Ahn SJ, Goh C-H, Cho K, Han O, Kang H (2007a) Functional characterization of a glycine-rich RNA-binding protein2 in Arabidopsis thaliana under abiotic stress conditions. Plant J 50: 439-451.
    • (2007) Plant J , vol.50 , pp. 439-451
    • Kim, J.Y.1    Park, S.J.2    Jang, B.3    Jung, C.-H.4    Ahn, S.J.5    Goh, C.-H.6    Cho, K.7    Han, O.8    Kang, H.9
  • 35
    • 47749089005 scopus 로고    scopus 로고
    • Glycine-rich RNA-binding protein7 affects abiotic stress responses by regulating stomata opening and closing in Arabidopsis thaliana
    • Kim JS, Jung HJ, Lee HJ, Kim KA, Goh CH, Woo Y, Oh SH, Han YS, Kang H (2008a) Glycine-rich RNA-binding protein7 affects abiotic stress responses by regulating stomata opening and closing in Arabidopsis thaliana. Plant J 55: 455-466.
    • (2008) Plant J , vol.55 , pp. 455-466
    • Kim, J.S.1    Jung, H.J.2    Lee, H.J.3    Kim, K.A.4    Goh, C.H.5    Woo, Y.6    Oh, S.H.7    Han, Y.S.8    Kang, H.9
  • 36
    • 54149112601 scopus 로고    scopus 로고
    • Functional characterization of DEAD-box RNA helicases in Arabidopsis thaliana under abiotic stress conditions
    • Kim JS, Kim KA, Oh TR, Park CM, Kang H (2008b) Functional characterization of DEAD-box RNA helicases in Arabidopsis thaliana under abiotic stress conditions. Plant Cell Physiol 49: 1563-1571.
    • (2008) Plant Cell Physiol , vol.49 , pp. 1563-1571
    • Kim, J.S.1    Kim, K.A.2    Oh, T.R.3    Park, C.M.4    Kang, H.5
  • 37
    • 33846907791 scopus 로고    scopus 로고
    • Cold shock domain proteins and glycinerich RNA-binding proteins from Arabidopsis thaliana can promote the cold adaptation process in Escherichia coli
    • Kim JS, Park SJ, Kwak KJ, Kim YO, Kim JY, Song J, Jang B, Jung CH, Kang H (2007b) Cold shock domain proteins and glycinerich RNA-binding proteins from Arabidopsis thaliana can promote the cold adaptation process in Escherichia coli. Nucleic Acids Res 35: 506-516.
    • (2007) Nucleic Acids Res , vol.35 , pp. 506-516
    • Kim, J.S.1    Park, S.J.2    Kwak, K.J.3    Kim, Y.O.4    Kim, J.Y.5    Song, J.6    Jang, B.7    Jung, C.H.8    Kang, H.9
  • 38
    • 69949183902 scopus 로고    scopus 로고
    • Cold shock domain protein 3 regulates freezing tolerance in Arabidopsis thaliana
    • Kim M-H, Sasaki K, Imai R (2009) Cold shock domain protein 3 regulates freezing tolerance in Arabidopsis thaliana. J Biol Chem 284: 23454-23460.
    • (2009) J Biol Chem , vol.284 , pp. 23454-23460
    • Kim, M.-H.1    Sasaki, K.2    Imai, R.3
  • 39
    • 21244473310 scopus 로고    scopus 로고
    • Cold-inducible zinc fingercontaining glycine-rich RNA-binding protein contributes to the enhancement of freezing tolerance in Arabidopsis thaliana
    • Kim YO, Kim JS, Kang H (2005) Cold-inducible zinc fingercontaining glycine-rich RNA-binding protein contributes to the enhancement of freezing tolerance in Arabidopsis thaliana. Plant J 42: 890-900.
    • (2005) Plant J , vol.42 , pp. 890-900
    • Kim, Y.O.1    Kim, J.S.2    Kang, H.3
  • 40
    • 33745385727 scopus 로고    scopus 로고
    • The role of a zinc finger-containing glycinerich RNA-binding protein during the cold adaptation process in Arabidopsis thaliana
    • Kim YO, Kang H (2006) The role of a zinc finger-containing glycinerich RNA-binding protein during the cold adaptation process in Arabidopsis thaliana. Plant Cell Physiol 47: 793-798.
    • (2006) Plant Cell Physiol , vol.47 , pp. 793-798
    • Kim, Y.O.1    Kang, H.2
  • 41
    • 77953009768 scopus 로고    scopus 로고
    • Glycine-rich RNA-binding proteins are functionally conserved in Arabidopsis thaliana and Oryza sativa during cold adaptation process
    • Kim JY, Kim WY, Kwak KJ, Oh SH, Han YS, Kang H (2010a) Glycine-rich RNA-binding proteins are functionally conserved in Arabidopsis thaliana and Oryza sativa during cold adaptation process. J Exp Bot 61: 2317-2325.
    • (2010) J Exp Bot , vol.61 , pp. 2317-2325
    • Kim, J.Y.1    Kim, W.Y.2    Kwak, K.J.3    Oh, S.H.4    Han, Y.S.5    Kang, H.6
  • 42
    • 77953227494 scopus 로고    scopus 로고
    • Zinc finger-containing glycine-rich RNA-binding protein in Oryza sativa has an RNA chaperone activity under cold stress conditions
    • Kim JY, Kim WY, Kwak KJ, Oh SH, Han YS, Kang H (2010b) Zinc finger-containing glycine-rich RNA-binding protein in Oryza sativa has an RNA chaperone activity under cold stress conditions. Plant Cell Environ 33: 759-768.
    • (2010) Plant Cell Environ , vol.33 , pp. 759-768
    • Kim, J.Y.1    Kim, W.Y.2    Kwak, K.J.3    Oh, S.H.4    Han, Y.S.5    Kang, H.6
  • 43
    • 77958162049 scopus 로고    scopus 로고
    • Comparative analysis of Arabidopsis zinc finger-containing glycine-rich RNA-binding proteins during cold adaptation
    • Kim WY, Kim JY, Jung HJ, Oh SH, Han YS, Kang H (2010c) Comparative analysis of Arabidopsis zinc finger-containing glycine-rich RNA-binding proteins during cold adaptation. Plant Physiol Biochem 48: 866-872.
    • (2010) Plant Physiol Biochem , vol.48 , pp. 866-872
    • Kim, W.Y.1    Kim, J.Y.2    Jung, H.J.3    Oh, S.H.4    Han, Y.S.5    Kang, H.6
  • 44
    • 79551619256 scopus 로고    scopus 로고
    • The Arabidopsis U12-types spliceosomal protein U11/U12-31K is involved in U12 intron splicing via RNA chaperone activity and affects plant development
    • Kim WY, Jung HJ, Kwak KJ, Kim MK, Oh SH, Han YS, Kang H (2010d) The Arabidopsis U12-types spliceosomal protein U11/U12-31K is involved in U12 intron splicing via RNA chaperone activity and affects plant development. Plant Cell 22: 3951-3962.
    • (2010) Plant Cell , vol.22 , pp. 3951-3962
    • Kim, W.Y.1    Jung, H.J.2    Kwak, K.J.3    Kim, M.K.4    Oh, S.H.5    Han, Y.S.6    Kang, H.7
  • 45
    • 27144497820 scopus 로고    scopus 로고
    • Characterization of transgenic Arabidopsis plants overexpressing GR-RBP4 under high salinity, dehydration, or cold stress
    • Kwak KJ, Kim YO, Kang H (2005) Characterization of transgenic Arabidopsis plants overexpressing GR-RBP4 under high salinity, dehydration, or cold stress. J Exp Bot 56: 3007-3016.
    • (2005) J Exp Bot , vol.56 , pp. 3007-3016
    • Kwak, K.J.1    Kim, Y.O.2    Kang, H.3
  • 46
    • 84865099854 scopus 로고    scopus 로고
    • The minor spliceosomal protein U11/U12-31K is an RNA chaperone crucial for U12 intron splicing and the development of dicot and monocot plants
    • Kwak KJ, Jung HJ, Lee KH, Kim YS, Kim WY, Ahn SJ, Kang H (2012) The minor spliceosomal protein U11/U12-31K is an RNA chaperone crucial for U12 intron splicing and the development of dicot and monocot plants. PLoS ONE 7: e43707.
    • (2012) PLoS ONE , vol.7
    • Kwak, K.J.1    Jung, H.J.2    Lee, K.H.3    Kim, Y.S.4    Kim, W.Y.5    Ahn, S.J.6    Kang, H.7
  • 47
    • 12144286231 scopus 로고    scopus 로고
    • A new Arabidopsis gene, FLK, encodes an RNA binding protein with K homology motif and regulates flowering time via FLOWERING LOCUS C
    • Lim MH, Kim J, Kim YS, Chung KS, Seo YH, Lee I, Kim J, Hong CB, Kim HJ, Park CM (2004) A new Arabidopsis gene, FLK, encodes an RNA binding protein with K homology motif and regulates flowering time via FLOWERING LOCUS C. Plant Cell 16: 731-740.
    • (2004) Plant Cell , vol.16 , pp. 731-740
    • Lim, M.H.1    Kim, J.2    Kim, Y.S.3    Chung, K.S.4    Seo, Y.H.5    Lee, I.6    Kim, J.7    Hong, C.B.8    Kim, H.J.9    Park, C.M.10
  • 48
    • 0026597376 scopus 로고
    • Eschericia coli DNA helicases: mechanism of DNA unwinding
    • Lohman TM (1992) Eschericia coli DNA helicases: mechanism of DNA unwinding. Mol Microbiol 6: 5-14.
    • (1992) Mol Microbiol , vol.6 , pp. 5-14
    • Lohman, T.M.1
  • 49
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP (1996) Mechanisms of helicase-catalyzed DNA unwinding. Ann Rev Biochem 65: 169-214.
    • (1996) Ann Rev Biochem , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 50
    • 63549135467 scopus 로고    scopus 로고
    • Role of plant RNA-binding proteins in development, stress response and genome organization
    • Lorkoviæ ZJ (2009) Role of plant RNA-binding proteins in development, stress response and genome organization. Trends Plant Sci 14: 229-236.
    • (2009) Trends Plant Sci , vol.14 , pp. 229-236
    • Lorkoviæ, Z.J.1
  • 51
    • 0036464536 scopus 로고    scopus 로고
    • Genomic analysis: RNA recognition motif (RRM) and K homology (KH) domain RNA-binding proteins from the flowering plant Arabidopsis thaliana
    • Lorkoviæ ZJ, Barta A (2002) Genomic analysis: RNA recognition motif (RRM) and K homology (KH) domain RNA-binding proteins from the flowering plant Arabidopsis thaliana. Nucleic Acids Res 30: 623-635.
    • (2002) Nucleic Acids Res , vol.30 , pp. 623-635
    • Lorkoviæ, Z.J.1    Barta, A.2
  • 52
    • 0037188887 scopus 로고    scopus 로고
    • RNA chaperones exist and DEAD-box proteins get a life
    • Lorsch JR (2002) RNA chaperones exist and DEAD-box proteins get a life. Cell 109: 797-800.
    • (2002) Cell , vol.109 , pp. 797-800
    • Lorsch, J.R.1
  • 54
    • 77952549857 scopus 로고    scopus 로고
    • Functional diversity of the plant glycine-rich proteins superfamily
    • Mangeon A, Junqueira RM, Sachetto-Martins G (2010) Functional diversity of the plant glycine-rich proteins superfamily. Plant Signal Behav 5: 99-104.
    • (2010) Plant Signal Behav , vol.5 , pp. 99-104
    • Mangeon, A.1    Junqueira, R.M.2    Sachetto-Martins, G.3
  • 55
    • 78751664467 scopus 로고    scopus 로고
    • Nucleic acid chaperone properties of ORF1p from the non-LTR retrotransposon, LINE-1
    • Martin SL (2010) Nucleic acid chaperone properties of ORF1p from the non-LTR retrotransposon, LINE-1. RNA Biol 7: 706-711.
    • (2010) RNA Biol , vol.7 , pp. 706-711
    • Martin, S.L.1
  • 56
    • 0033134643 scopus 로고    scopus 로고
    • Conservation of structure and cold-regulation of RNA-binding proteis in cyanobacteria: probable convergent evolution with eukaryotic glycine-rich RNA-binding proteins
    • Maruyama K, Sato N, Ohta N (1999) Conservation of structure and cold-regulation of RNA-binding proteis in cyanobacteria: probable convergent evolution with eukaryotic glycine-rich RNA-binding proteins. Nucleic Acid Res 27: 2029-2036.
    • (1999) Nucleic Acid Res , vol.27 , pp. 2029-2036
    • Maruyama, K.1    Sato, N.2    Ohta, N.3
  • 57
    • 0026039209 scopus 로고
    • DNA helicases of Escherichia coli
    • Matson SW (1991) DNA helicases of Escherichia coli. Prog Nucleic Acid Res Mol Biol 40: 2029-2036.
    • (1991) Prog Nucleic Acid Res Mol Biol , vol.40 , pp. 2029-2036
    • Matson, S.W.1
  • 58
    • 0027950513 scopus 로고
    • DNA helicases: enzymes with essential roles in all aspects of DNA metabolism
    • Matson SW, Bean D, George JW (1994) DNA helicases: enzymes with essential roles in all aspects of DNA metabolism. BioEssays 16: 13-21.
    • (1994) BioEssays , vol.16 , pp. 13-21
    • Matson, S.W.1    Bean, D.2    George, J.W.3
  • 60
    • 0037077127 scopus 로고    scopus 로고
    • DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr S, Stryker JM, Lambowitz AM (2002) DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell 109: 769-779.
    • (2002) Cell , vol.109 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 61
    • 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 PS, Lambowitz AM (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
  • 62
    • 0028990057 scopus 로고
    • The RNP domain: a sequence specific RNA-binding domain involved in processing and transport of RNA
    • Nagai K, Oubridge C, Ito N, Avis J, Evans P (1995) The RNP domain: a sequence specific RNA-binding domain involved in processing and transport of RNA. Trends Biochem Sci 20: 235-240.
    • (1995) Trends Biochem Sci , vol.20 , pp. 235-240
    • Nagai, K.1    Oubridge, C.2    Ito, N.3    Avis, J.4    Evans, P.5
  • 63
    • 33745627302 scopus 로고    scopus 로고
    • Functional conservation of cold shock domains in bacteria and higher plants
    • Nakaminami K, Karlson D, Imai R (2006) Functional conservation of cold shock domains in bacteria and higher plants. Proc Natl Acad Sci USA 103: 10122-10127.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10122-10127
    • Nakaminami, K.1    Karlson, D.2    Imai, R.3
  • 64
    • 2442577062 scopus 로고    scopus 로고
    • Structural and transcriptional characterization of a salt-responsive gene encoding putative ATP-dependent RNA helicase in barley
    • Nakamura T, Muramoto Y, Takabe T (2004) Structural and transcriptional characterization of a salt-responsive gene encoding putative ATP-dependent RNA helicase in barley. Plant Sci 167: 63-70.
    • (2004) Plant Sci , vol.167 , pp. 63-70
    • Nakamura, T.1    Muramoto, Y.2    Takabe, T.3
  • 65
    • 0027547139 scopus 로고
    • Two cDNAs from Arabidopsis thaliana encode putative RNA binding proteins containing glycinerich domains
    • van Nocker S, Vierstra RD (1993) Two cDNAs from Arabidopsis thaliana encode putative RNA binding proteins containing glycinerich domains. Plant Mol Biol 21: 695-699.
    • (1993) Plant Mol Biol , vol.21 , pp. 695-699
    • van Nocker, S.1    Vierstra, R.D.2
  • 66
    • 1042268308 scopus 로고    scopus 로고
    • Cloning and characterization of glycine-rich RNA-binding protein cDNAs in the moss Physcomitrella patens
    • Nomata T, Kabeya Y, Sato N (2004) Cloning and characterization of glycine-rich RNA-binding protein cDNAs in the moss Physcomitrella patens. Plant Cell Physiol 45: 48-56.
    • (2004) Plant Cell Physiol , vol.45 , pp. 48-56
    • Nomata, T.1    Kabeya, Y.2    Sato, N.3
  • 67
    • 77949637589 scopus 로고    scopus 로고
    • The C-terminal zinc finger domain of Arabidopsis cold shock domain proteins is important for RNA chaperone activity during cold adaptation
    • Park SJ, Kwak KJ, Jung HJ, Lee HJ, Kang H (2010) The C-terminal zinc finger domain of Arabidopsis cold shock domain proteins is important for RNA chaperone activity during cold adaptation. Phytochem 71: 543-547.
    • (2010) Phytochem , vol.71 , pp. 543-547
    • Park, S.J.1    Kwak, K.J.2    Jung, H.J.3    Lee, H.J.4    Kang, H.5
  • 69
    • 0036510774 scopus 로고    scopus 로고
    • The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells
    • Phadtare S, Inouye M, Severinov K (2002) The nucleic acid melting activity of Escherichia coli CspE is critical for transcription antitermination and cold acclimation of cells. J Biol Chem 277: 7239-7245.
    • (2002) J Biol Chem , vol.277 , pp. 7239-7245
    • Phadtare, S.1    Inouye, M.2    Severinov, K.3
  • 70
    • 79960623040 scopus 로고    scopus 로고
    • The Sm-like RNA chaperone Hfq mediates transcription antitermination at Rho-dependent terminators
    • Rabhi M, Espéli O, Schwartz A, Cayrol B, Rahmouni AR, Arluison V, Boudvillain M (2011) The Sm-like RNA chaperone Hfq mediates transcription antitermination at Rho-dependent terminators. EMBO J 30: 2805-2816.
    • (2011) EMBO J , vol.30 , pp. 2805-2816
    • Rabhi, M.1    Espéli, O.2    Schwartz, A.3    Cayrol, B.4    Rahmouni, A.R.5    Arluison, V.6    Boudvillain, M.7
  • 73
    • 30044448211 scopus 로고    scopus 로고
    • PEPPER, a novel K-homology domain gene, regulates vegetative and gynoecium development in Arabidopsis
    • Ripoll JJ, Ferrándiz C, Martínez-Laborda A, Vera A (2006) PEPPER, a novel K-homology domain gene, regulates vegetative and gynoecium development in Arabidopsis. Dev Biol 289: 346-359.
    • (2006) Dev Biol , vol.289 , pp. 346-359
    • Ripoll, J.J.1    Ferrándiz, C.2    Martínez-Laborda, A.3    Vera, A.4
  • 74
    • 33750336226 scopus 로고    scopus 로고
    • An early evolutionary origin for the minor spliceosome
    • Russell AG, Charette JM, Spencer DF, Gray MW (2006) An early evolutionary origin for the minor spliceosome. Nature 443: 863-866.
    • (2006) Nature , vol.443 , pp. 863-866
    • Russell, A.G.1    Charette, J.M.2    Spencer, D.F.3    Gray, M.W.4
  • 75
  • 76
    • 84873122460 scopus 로고    scopus 로고
    • Pleiotropic roles of cold shock domain proteins in plants
    • Sasaki K, Imai R (2012) Pleiotropic roles of cold shock domain proteins in plants. Front Plant Sci 2: 116.
    • (2012) Front Plant Sci , vol.2 , pp. 116
    • Sasaki, K.1    Imai, R.2
  • 77
    • 35648999468 scopus 로고    scopus 로고
    • Arabidopsis cold shock domain protein2 is a RNA chaperone that is regulated by cold and developmental signals
    • Sasaki K, Kim MH, Imai R (2007) Arabidopsis cold shock domain protein2 is a RNA chaperone that is regulated by cold and developmental signals. Biochem Biophys Res Commun 364: 633-638.
    • (2007) Biochem Biophys Res Commun , vol.364 , pp. 633-638
    • Sasaki, K.1    Kim, M.H.2    Imai, R.3
  • 78
    • 56549095978 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins: a socket set for organelle gene expression
    • Schmitz-Linneweber C, Small I (2008) Pentatricopeptide repeat proteins: a socket set for organelle gene expression. Trends Plant Sci 13: 663-670.
    • (2008) Trends Plant Sci , vol.13 , pp. 663-670
    • Schmitz-Linneweber, C.1    Small, I.2
  • 80
    • 79952231350 scopus 로고    scopus 로고
    • Proteins with RNA chaperone activity: A world of diverse proteins with a common task-Impediment of RNA misfolding
    • 532908
    • Semrad K (2011) Proteins with RNA chaperone activity: A world of diverse proteins with a common task-Impediment of RNA misfolding. Biochem Res Int ID 532908: 1-11.
    • (2011) Biochem Res Int ID , pp. 1-11
    • Semrad, K.1
  • 81
    • 33645827987 scopus 로고    scopus 로고
    • Gene expression and genetic mapping analyses of a perennial ryegrass glycine-rich RNA-binding protein gene suggest a role in cold adaptation
    • Shinozuka H, Hisano H, Yoneyama S, Shimamoto Y, Jones ES, Forster JW, Yamada T, Kanazawa A (2006) Gene expression and genetic mapping analyses of a perennial ryegrass glycine-rich RNA-binding protein gene suggest a role in cold adaptation. Mol Genet Genom 275: 399-408.
    • (2006) Mol Genet Genom , vol.275 , pp. 399-408
    • Shinozuka, H.1    Hisano, H.2    Yoneyama, S.3    Shimamoto, Y.4    Jones, E.S.5    Forster, J.W.6    Yamada, T.7    Kanazawa, A.8
  • 82
    • 0030255869 scopus 로고    scopus 로고
    • Splicing of precursors to mRNA in higher plants: mechanism, regulation and sub-nuclear organization of the spliceosomal machinery
    • Simpson GG, Filipowicz W (1996) Splicing of precursors to mRNA in higher plants: mechanism, regulation and sub-nuclear organization of the spliceosomal machinery. Plant Mol Biol 32: 1-41.
    • (1996) Plant Mol Biol , vol.32 , pp. 1-41
    • Simpson, G.G.1    Filipowicz, W.2
  • 83
    • 0242361572 scopus 로고    scopus 로고
    • A cDNA encoding a cold-induced glycine-rich RNA binding protein from Prunus avium expressed in embryonic axes
    • Stephen JR, Dent KC, Finch-Savage WE (2003) A cDNA encoding a cold-induced glycine-rich RNA binding protein from Prunus avium expressed in embryonic axes. Gene 320: 177-183.
    • (2003) Gene , vol.320 , pp. 177-183
    • Stephen, J.R.1    Dent, K.C.2    Finch-Savage, W.E.3
  • 85
    • 53549122472 scopus 로고    scopus 로고
    • The small glycine-rich RNA-binding protein AtGRP7 promotes floral transition in Arabidopsis thaliana
    • Streitner C, Danisman S, Wehrle F, Schöning JC, Alfano JR, Staiger D (2008) The small glycine-rich RNA-binding protein AtGRP7 promotes floral transition in Arabidopsis thaliana. Plant J 56: 239-250.
    • (2008) Plant J , vol.56 , pp. 239-250
    • Streitner, C.1    Danisman, S.2    Wehrle, F.3    Schöning, J.C.4    Alfano, J.R.5    Staiger, D.6
  • 86
    • 80255140515 scopus 로고    scopus 로고
    • Spatial and temporal expression of coldresponsive DEAD-box RNA helicases reveals their functional roles during embryogenesis in Arabidopsis thaliana
    • Tripurani SK, Nakaminami K, Thompson KB, Crowell SV, Guy CL, Karlson DT (2011) Spatial and temporal expression of coldresponsive DEAD-box RNA helicases reveals their functional roles during embryogenesis in Arabidopsis thaliana. Plant Mol Biol Rep 29: 761-768.
    • (2011) Plant Mol Biol Rep , vol.29 , pp. 761-768
    • Tripurani, S.K.1    Nakaminami, K.2    Thompson, K.B.3    Crowell, S.V.4    Guy, C.L.5    Karlson, D.T.6
  • 87
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: from generic motors to specific dissociation functions
    • Tanner NK, Linder P (2001) DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol Cell 8: 251-262.
    • (2001) Mol Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 88
    • 77950597578 scopus 로고    scopus 로고
    • Intrinsically disordered chaperones in plants and animals
    • Tompa P, Kovacs D (2010) Intrinsically disordered chaperones in plants and animals. Biochem Cell Biol 88: 167-174.
    • (2010) Biochem Cell Biol , vol.88 , pp. 167-174
    • Tompa, P.1    Kovacs, D.2
  • 89
    • 80255140515 scopus 로고    scopus 로고
    • Spatial and temporal expression of coldresponsive DEAD-box RNA helicases reveals their functional roles during embryogenesis in Arabidopsis thaliana
    • Tripurani SK, Nakaminami K, Thompson KB, Crowell SV, Guy CL, Karlson DT (2011) Spatial and temporal expression of coldresponsive DEAD-box RNA helicases reveals their functional roles during embryogenesis in Arabidopsis thaliana. Plant Mol Biol Rep 29: 761-768.
    • (2011) Plant Mol Biol Rep , vol.29 , pp. 761-768
    • Tripurani, S.K.1    Nakaminami, K.2    Thompson, K.B.3    Crowell, S.V.4    Guy, C.L.5    Karlson, D.T.6
  • 90
    • 2442706340 scopus 로고    scopus 로고
    • Unraveling DNA helicases. Motif, structure, mechanism and function
    • Tuteja N, Tuteja R (2004) Unraveling DNA helicases. Motif, structure, mechanism and function. Eur J Biochem 271: 1849-1863.
    • (2004) Eur J Biochem , vol.271 , pp. 1849-1863
    • Tuteja, N.1    Tuteja, R.2
  • 91
    • 77953229290 scopus 로고    scopus 로고
    • Genome-wide analysis of helicase gene family from rice and Arabidopsis: a comparison with yeast and human
    • Umate P, Tuteja R, Tuteja N (2010) Genome-wide analysis of helicase gene family from rice and Arabidopsis: a comparison with yeast and human. Plant Mol Biol 73: 449-465.
    • (2010) Plant Mol Biol , vol.73 , pp. 449-465
    • Umate, P.1    Tuteja, R.2    Tuteja, N.3
  • 92
    • 0030602794 scopus 로고    scopus 로고
    • DNA helicases: new breeds of translocating motors and molecular pumps
    • West SC (1996) DNA helicases: new breeds of translocating motors and molecular pumps. Cell 86: 177-180.
    • (1996) Cell , vol.86 , pp. 177-180
    • West, S.C.1
  • 93
  • 94
    • 78751677070 scopus 로고    scopus 로고
    • Taming free energy landscapes with RNA chaperones
    • Woodson SA (2010) Taming free energy landscapes with RNA chaperones. RNA Biol 7: 677-686.
    • (2010) RNA Biol , vol.7 , pp. 677-686
    • Woodson, S.A.1
  • 95
    • 78649360662 scopus 로고    scopus 로고
    • Characterization and expression analysis of four glycinerich RNA-binding proteins involved in osmotic response in Tobacco (Nicotiana tabacum cv. Xanthi)
    • Xuan C, ZENG Qian-chun Z, Xiu-ping L, Di-qiu Y, Wen-zheng L (2010) Characterization and expression analysis of four glycinerich RNA-binding proteins involved in osmotic response in Tobacco (Nicotiana tabacum cv. Xanthi). Agri Sci China 9: 1577-1587.
    • (2010) Agri Sci China , vol.9 , pp. 1577-1587
    • Xuan, C.1    Zeng, Q.-C.Z.2    Xiu-Ping, L.3    Di-Qiu, Y.4    Wen-Zheng, L.5
  • 96
    • 79955548120 scopus 로고    scopus 로고
    • DEAD-box proteins from Escherichia coli exhibit multiple ATP-independent activities
    • Zhao X, Jain C (2011) DEAD-box proteins from Escherichia coli exhibit multiple ATP-independent activities. J Bacteriol 193: 2236-2241.
    • (2011) J Bacteriol , vol.193 , pp. 2236-2241
    • Zhao, X.1    Jain, C.2
  • 97
    • 34248222619 scopus 로고    scopus 로고
    • Interplay between cold-responsive gene regulation, metabolism and RNA processing during plant cold acclimation
    • Zhu J, Dong C-H, Zhu J-K (2007) Interplay between cold-responsive gene regulation, metabolism and RNA processing during plant cold acclimation. Curr Opin Plant Biol 10: 290-295.
    • (2007) Curr Opin Plant Biol , vol.10 , pp. 290-295
    • Zhu, J.1    Dong, C.-H.2    Zhu, J.-K.3
  • 98
    • 70349766117 scopus 로고    scopus 로고
    • Genes encoding novel secreted and transmembrane proteins are temporally and spatially regulated during Drosophila melanogaster embryogenesis
    • Zúñiga A, Hödar C, Hanna P, Ibáñez F, Moreno P, Pulgar R, Pastenes L, González M, Cambiazo V (2009) Genes encoding novel secreted and transmembrane proteins are temporally and spatially regulated during Drosophila melanogaster embryogenesis. BMC Biol 7: 61.
    • (2009) BMC Biol , vol.7 , pp. 61
    • Zúñiga, A.1    Hödar, C.2    Hanna, P.3    Ibáñez, F.4    Moreno, P.5    Pulgar, R.6    Pastenes, L.7    González, M.8    Cambiazo, V.9


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