메뉴 건너뛰기




Volumn 368, Issue 4, 2007, Pages 1087-1100

DEAD-box-protein-assisted RNA Structure Conversion Towards and Against Thermodynamic Equilibrium Values

Author keywords

ATPase; DEAD box; helicase; RNA chaperone; RNA structure

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DEAD BOX PROTEIN; DED1 PROTEIN; UNCLASSIFIED DRUG;

EID: 34147111663     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.02.071     Document Type: Article
Times cited : (31)

References (35)
  • 2
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley J.P., and Guthrie C. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92 (1998) 315-326
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 4
    • 20444502087 scopus 로고    scopus 로고
    • Structure, folding and mechanisms of ribozymes
    • Lilley D.M. Structure, folding and mechanisms of ribozymes. Curr. Opin. Struct. Biol. 15 (2005) 313-323
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 313-323
    • Lilley, D.M.1
  • 5
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases. From generic motors to specific dissociation functions
    • Tanner N.K., and Linder P. DExD/H box RNA helicases. From generic motors to specific dissociation functions. Mol. Cell 8 (2001) 251-261
    • (2001) Mol. Cell , vol.8 , pp. 251-261
    • Tanner, N.K.1    Linder, P.2
  • 7
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: the driving forces behind RNA metabolism
    • Rocak S., and Linder P. DEAD-box proteins: the driving forces behind RNA metabolism. Nature Rev. Mol. Cell Biol. 5 (2004) 232-241
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 9
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., and Linder P. The DEAD-box protein family of RNA helicases. Gene 367 (2006) 17-37
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 10
    • 26644450709 scopus 로고    scopus 로고
    • ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
    • Yang Q., and Jankowsky E. ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry 44 (2005) 13591-13601
    • (2005) Biochemistry , vol.44 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2
  • 11
    • 33847652952 scopus 로고    scopus 로고
    • A DEAD protein that activates intron self-splicing without unwinding RNA
    • Solem A., Zingler N., and Pyle A.M. A DEAD protein that activates intron self-splicing without unwinding RNA. Mol. Cell 24 (2006) 611-617
    • (2006) Mol. Cell , vol.24 , pp. 611-617
    • Solem, A.1    Zingler, N.2    Pyle, A.M.3
  • 12
    • 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. 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 (2007) 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
  • 13
    • 16344371778 scopus 로고    scopus 로고
    • RNA and protein folding: common themes and variations
    • Thirumalai D., and Hyeon C. RNA and protein folding: common themes and variations. Biochemistry 44 (2005) 4957-4970
    • (2005) Biochemistry , vol.44 , pp. 4957-4970
    • Thirumalai, D.1    Hyeon, C.2
  • 14
    • 0037781588 scopus 로고    scopus 로고
    • Yeast RNA helicases of the DEAD-box family involved in translation initiation
    • Linder P. Yeast RNA helicases of the DEAD-box family involved in translation initiation. Biol. Cell 95 (2003) 157-167
    • (2003) Biol. Cell , vol.95 , pp. 157-167
    • Linder, P.1
  • 15
    • 0033580840 scopus 로고    scopus 로고
    • Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase
    • Iost I., Dreyfus M., and Linder P. Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J. Biol. Chem. 274 (1999) 17677-17683
    • (1999) J. Biol. Chem. , vol.274 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 16
    • 33750593917 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
    • Yang Q., and Jankowsky E. The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nature Struct. Mol. Biol. 13 (2006) 981-986
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 17
    • 0036281361 scopus 로고    scopus 로고
    • Glucose-sensing and -signalling mechanisms in yeast
    • Rolland F., Winderickx J., and Thevelein J.M. Glucose-sensing and -signalling mechanisms in yeast. FEMS Yeast Res. 2 (2002) 183-201
    • (2002) FEMS Yeast Res. , vol.2 , pp. 183-201
    • Rolland, F.1    Winderickx, J.2    Thevelein, J.M.3
  • 18
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha T. Single-molecule fluorescence resonance energy transfer. Methods 25 (2001) 78-86
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 21
    • 0035366378 scopus 로고    scopus 로고
    • Single-molecule fluorescence methods for the study of nucleic acids
    • Ha T. Single-molecule fluorescence methods for the study of nucleic acids. Curr. Opin. Struct. Biol. 11 (2001) 287-292
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 287-292
    • Ha, T.1
  • 23
    • 17644373802 scopus 로고    scopus 로고
    • Observing spontaneous branch migration of Holliday junctions one step at a time
    • McKinney S.A., Freeman A.D., Lilley D.M., and Ha T. Observing spontaneous branch migration of Holliday junctions one step at a time. Proc. Natl Acad. Sci. USA 102 (2005) 5715-5720
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5715-5720
    • McKinney, S.A.1    Freeman, A.D.2    Lilley, D.M.3    Ha, T.4
  • 24
    • 0030593036 scopus 로고    scopus 로고
    • Assembly of a ribonucleoprotein catalyst by tertiary structure capture
    • Weeks K.M., and Cech T.R. Assembly of a ribonucleoprotein catalyst by tertiary structure capture. Science 271 (1996) 345-348
    • (1996) Science , vol.271 , pp. 345-348
    • Weeks, K.M.1    Cech, T.R.2
  • 25
    • 0025069836 scopus 로고
    • Complex formed by complementary RNA stem-loops and its stabilization by a protein: function of CoIE1 Rom protein
    • Eguchi Y., and Tomizawa J. Complex formed by complementary RNA stem-loops and its stabilization by a protein: function of CoIE1 Rom protein. Cell 60 (1990) 199-209
    • (1990) Cell , vol.60 , pp. 199-209
    • Eguchi, Y.1    Tomizawa, J.2
  • 27
    • 0030660155 scopus 로고    scopus 로고
    • Implications of RNA structure on the annealing of a potent antisense RNA directed against the human immunodeficiency virus type 1
    • Eckardt S., Romby P., and Sczakiel G. Implications of RNA structure on the annealing of a potent antisense RNA directed against the human immunodeficiency virus type 1. Biochemistry 36 (1997) 12711-12721
    • (1997) Biochemistry , vol.36 , pp. 12711-12721
    • Eckardt, S.1    Romby, P.2    Sczakiel, G.3
  • 30
    • 0036307597 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity
    • Urbaneja M.A., Wu M., Casas-Finet J.R., and Karpel R.L. HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity. J. Mol. Biol. 318 (2002) 749-764
    • (2002) J. Mol. Biol. , vol.318 , pp. 749-764
    • Urbaneja, M.A.1    Wu, M.2    Casas-Finet, J.R.3    Karpel, R.L.4
  • 32
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky E., Gross C.H., Shuman S., and Pyle A.M. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403 (2000) 447-451
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 33
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky E., Gross C.H., Shuman S., and Pyle A.M. Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291 (2001) 121-125
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 34
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and orientations: much to FRET about?
    • Rasnik I., McKinney S.A., and Ha T. Surfaces and orientations: much to FRET about?. Accts Chem. Res. 38 (2005) 542-548
    • (2005) Accts Chem. Res. , vol.38 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 35
    • 0024498315 scopus 로고
    • Analysis of progress curves by simulations generated by numerical integration
    • Zimmerle C.T., and Frieden C. Analysis of progress curves by simulations generated by numerical integration. Biochem. J. 258 (1989) 381-387
    • (1989) Biochem. J. , vol.258 , pp. 381-387
    • Zimmerle, C.T.1    Frieden, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.