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Volumn 447, Issue , 2008, Pages 119-129

Chapter 7 New Approaches to Understanding Double-Stranded RNA Processing by Ribonuclease III. Purification and Assays of Homodimeric and Heterodimeric Forms of RNase III from Bacterial Extremophiles and Mesophiles

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; HETERODIMER; HOMODIMER; RIBONUCLEASE III;

EID: 58249086416     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)02207-6     Document Type: Review
Times cited : (4)

References (26)
  • 1
    • 25844471038 scopus 로고    scopus 로고
    • Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 Å resolution
    • Akey D.L., and Berger J.M. Structure of the nuclease domain of ribonuclease III from M. tuberculosis at 2.1 Å resolution. Protein Sci. 14 (2005) 2744-2750
    • (2005) Protein Sci. , vol.14 , pp. 2744-2750
    • Akey, D.L.1    Berger, J.M.2
  • 2
    • 0034804433 scopus 로고    scopus 로고
    • Escherichia coli ribonuclease III: Affinity purification of hexahistidine-tagged enzyme and assays for substrate binding and cleavage
    • Amarasinghe A.K., Calin-Jageman I., Harmouch A., Sun W., and Nicholson A.W. Escherichia coli ribonuclease III: Affinity purification of hexahistidine-tagged enzyme and assays for substrate binding and cleavage. Methods Enzymol. 342 (2001) 143-158
    • (2001) Methods Enzymol. , vol.342 , pp. 143-158
    • Amarasinghe, A.K.1    Calin-Jageman, I.2    Harmouch, A.3    Sun, W.4    Nicholson, A.W.5
  • 3
    • 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. Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. Structure 9 (2001) 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
  • 4
    • 1542581581 scopus 로고    scopus 로고
    • Noncatalytic assembly of ribonuclease III with double-stranded RNA
    • Blaszczyk J., Gan J., Tropea J.E., Court D.L., Waugh D.S., and Ji X. Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure 12 (2004) 457-466
    • (2004) Structure , vol.12 , pp. 457-466
    • Blaszczyk, J.1    Gan, J.2    Tropea, J.E.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 5
    • 0037995439 scopus 로고    scopus 로고
    • Mutational analysis of an RNA internal loop as a reactivity epitope for Escherichia coli ribonuclease III substrates
    • Calin-Jageman I., and Nicholson A.W. Mutational analysis of an RNA internal loop as a reactivity epitope for Escherichia coli ribonuclease III substrates. Biochem. 42 (2003) 5025-5034
    • (2003) Biochem. , vol.42 , pp. 5025-5034
    • Calin-Jageman, I.1    Nicholson, A.W.2
  • 6
    • 0037042215 scopus 로고    scopus 로고
    • One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers
    • Conrad C., Schmitt J.G., Evguenieva-Hackenberg E., and Klug G. One functional subunit is sufficient for catalytic activity and substrate specificity of Escherichia coli endoribonuclease III artificial heterodimers. FEBS Lett. 518 (2002) 93-96
    • (2002) FEBS Lett. , vol.518 , pp. 93-96
    • Conrad, C.1    Schmitt, J.G.2    Evguenieva-Hackenberg, E.3    Klug, G.4
  • 7
    • 34250257369 scopus 로고
    • RNA processing and degradation by RNase III
    • Belasco J.G., and Brawerman G. (Eds), Academic Press, New York
    • Court D. RNA processing and degradation by RNase III. In: Belasco J.G., and Brawerman G. (Eds). Control of Messenger RNA Stability (1993), Academic Press, New York 71-116
    • (1993) Control of Messenger RNA Stability , pp. 71-116
    • Court, D.1
  • 8
    • 0015712886 scopus 로고
    • T7 early RNAs and Escherichia coli ribosomal RNAs are cut from large precursor RNAs in vitro by ribonuclease III
    • Dunn J.J., and Studier F.W. T7 early RNAs and Escherichia coli ribosomal RNAs are cut from large precursor RNAs in vitro by ribonuclease III. Proc. Natl. Acad. Sci. USA 70 (1973) 3296-3300
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3296-3300
    • Dunn, J.J.1    Studier, F.W.2
  • 9
    • 36849013062 scopus 로고    scopus 로고
    • A stepwise model for double-stranded RNA processing by ribonuclease III
    • Gan J., Shaw G., Tropea J.E., Waugh D.S., Court D.L., and Ji X. A stepwise model for double-stranded RNA processing by ribonuclease III. Mol. Microbiol. 67 (2007) 143-154
    • (2007) Mol. Microbiol. , vol.67 , pp. 143-154
    • Gan, J.1    Shaw, G.2    Tropea, J.E.3    Waugh, D.S.4    Court, D.L.5    Ji, X.6
  • 10
    • 26444436343 scopus 로고    scopus 로고
    • Intermediate states of ribonuclease III in complex with double-stranded RNA
    • Gan J., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., and Xi J. Intermediate states of ribonuclease III in complex with double-stranded RNA. Structure 13 (2005) 1435-1442
    • (2005) Structure , vol.13 , pp. 1435-1442
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Xi, J.6
  • 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. Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell 124 (2006) 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
    • 0035155389 scopus 로고    scopus 로고
    • The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism
    • LaMontagne B., Larose S., Boulanger J., and Abou Elela S. The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism. Curr. Issues Mol. Biol. 3 (2001) 71-78
    • (2001) Curr. Issues Mol. Biol. , vol.3 , pp. 71-78
    • LaMontagne, B.1    Larose, S.2    Boulanger, J.3    Abou Elela, S.4
  • 14
    • 42949179593 scopus 로고    scopus 로고
    • In vitro and in vivo assays for the activity of the Drosha complex
    • Lee Y., and Kim V.N. In vitro and in vivo assays for the activity of the Drosha complex. Methods Enzymol. 427 (2007) 87-106
    • (2007) Methods Enzymol. , vol.427 , pp. 87-106
    • Lee, Y.1    Kim, V.N.2
  • 15
    • 33846927800 scopus 로고    scopus 로고
    • Ribonuclease revisited: Structural insights into ribonuclease III family enzymes
    • MacRae I.J., and Doudna J.A. Ribonuclease revisited: Structural insights into ribonuclease III family enzymes. Curr. Opin. Struct. Biol. 17 (2007) 1-8
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 1-8
    • MacRae, I.J.1    Doudna, J.A.2
  • 17
    • 39749139400 scopus 로고    scopus 로고
    • Heterodimer-based analysis of subunit and domain contributions to double-stranded RNA processing by Escherichia coli RNase III in vitro
    • Meng W., and Nicholson A.W. Heterodimer-based analysis of subunit and domain contributions to double-stranded RNA processing by Escherichia coli RNase III in vitro. Biochem. J. 410 (2008) 39-48
    • (2008) Biochem. J. , vol.410 , pp. 39-48
    • Meng, W.1    Nicholson, A.W.2
  • 18
    • 0347224335 scopus 로고    scopus 로고
    • The ribonuclease III superfamily: Forms and functions in RNA maturation, decay, and gene silencing
    • Hannon G. (Ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Nicholson A.W. The ribonuclease III superfamily: Forms and functions in RNA maturation, decay, and gene silencing. In: Hannon G. (Ed). RNAi: A Guide to Gene Silencing (2003), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York 149-174
    • (2003) RNAi: A Guide to Gene Silencing , pp. 149-174
    • Nicholson, A.W.1
  • 19
    • 0015753579 scopus 로고
    • Synthesis of a large precursor to ribosomal RNA in a mutant of Escherichia coli
    • Nikolaev N., Silengo L., and Schlessinger D. Synthesis of a large precursor to ribosomal RNA in a mutant of Escherichia coli. Proc. Natl. Acad. Sci. USA 70 (1973) 3361-3365
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3361-3365
    • Nikolaev, N.1    Silengo, L.2    Schlessinger, D.3
  • 20
    • 33747038694 scopus 로고    scopus 로고
    • Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III
    • Pertzev A.V., and Nicholson A.W. Characterization of RNA sequence determinants and antideterminants of processing reactivity for a minimal substrate of Escherichia coli ribonuclease III. Nucl. Acids Res. 34 (2006) 3708-3721
    • (2006) Nucl. Acids Res. , vol.34 , pp. 3708-3721
    • Pertzev, A.V.1    Nicholson, A.W.2
  • 21
    • 0014408286 scopus 로고
    • Purification and properties of ribonuclease III from Escherichia coli
    • Robertson H.D., Webster R.E., and Zinder N.D. Purification and properties of ribonuclease III from Escherichia coli. J. Biol. Chem. 243 (1968) 82-91
    • (1968) J. Biol. Chem. , vol.243 , pp. 82-91
    • Robertson, H.D.1    Webster, R.E.2    Zinder, N.D.3
  • 22
    • 0029858708 scopus 로고    scopus 로고
    • The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV
    • Wende W., Stahl F., and Pingoud A. The production and characterization of artificial heterodimers of the restriction endonuclease EcoRV. Biol. Chem. 377 (1996) 625-632
    • (1996) Biol. Chem. , vol.377 , pp. 625-632
    • Wende, W.1    Stahl, F.2    Pingoud, A.3
  • 24
    • 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. Single processing center models for human Dicer and bacterial RNase III. Cell 118 (2004) 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
  • 25
    • 0031470503 scopus 로고    scopus 로고
    • Regulation of ribonuclease III processing by double-helical sequence antideterminants
    • Zhang K., and Nicholson A.W. Regulation of ribonuclease III processing by double-helical sequence antideterminants. Proc. Natl. Acad. Sci. USA 94 (1997) 13437-13441
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13437-13441
    • Zhang, K.1    Nicholson, A.W.2
  • 26
    • 0031579473 scopus 로고    scopus 로고
    • A new expression vector for high level protein production, one step purification and direct isotopic labeling of calmodulin-binding peptide fusion proteins
    • Zheng C.-F., Simcox T., Xu L., and Vaillancourt P. A new expression vector for high level protein production, one step purification and direct isotopic labeling of calmodulin-binding peptide fusion proteins. Gene 186 (1997) 55-60
    • (1997) Gene , vol.186 , pp. 55-60
    • Zheng, C.-F.1    Simcox, T.2    Xu, L.3    Vaillancourt, P.4


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