메뉴 건너뛰기




Volumn 374, Issue 5, 2007, Pages 1158-1171

The Dynamic Mu Transpososome: MuB Activation Prevents Disintegration

Author keywords

integrase; phage Mu; target site; transposition; transposon

Indexed keywords

PROTEIN; PROTEIN MUA; PROTEIN MUB; TRANSPOSASE; UNCLASSIFIED DRUG;

EID: 36248967135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.09.079     Document Type: Article
Times cited : (7)

References (57)
  • 1
    • 0242636324 scopus 로고    scopus 로고
    • The outs and ins of transposition: from mu to kangaroo
    • Curcio M.J., and Derbyshire K.M. The outs and ins of transposition: from mu to kangaroo. Nature Rev. Mol. Cell Biol. 4 (2003) 865-877
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 865-877
    • Curcio, M.J.1    Derbyshire, K.M.2
  • 2
    • 27144556149 scopus 로고    scopus 로고
    • The transpososome: control of transposition at the level of catalysis
    • Gueguen E., Rousseau P., Duval-Valentin G., and Chandler M. The transpososome: control of transposition at the level of catalysis. Trends Microbiol. 13 (2005) 543-549
    • (2005) Trends Microbiol. , vol.13 , pp. 543-549
    • Gueguen, E.1    Rousseau, P.2    Duval-Valentin, G.3    Chandler, M.4
  • 4
    • 0035343895 scopus 로고    scopus 로고
    • Comparative architecture of transposase and integrase complexes
    • Rice P.A., and Baker T.A. Comparative architecture of transposase and integrase complexes. Nature Struct. Biol. 8 (2001) 302-307
    • (2001) Nature Struct. Biol. , vol.8 , pp. 302-307
    • Rice, P.A.1    Baker, T.A.2
  • 5
    • 85158061254 scopus 로고    scopus 로고
    • Chemical mechanisms for mobilizing DNA
    • Craig N.L., Craigie R., Gellert M., and Lambowitz A.M. (Eds), ASM Press, Washington, DC
    • Mizuuchi M.a.B., T.A. Chemical mechanisms for mobilizing DNA. In: Craig N.L., Craigie R., Gellert M., and Lambowitz A.M. (Eds). Mobile DNA II (2002), ASM Press, Washington, DC 12-23
    • (2002) Mobile DNA II , pp. 12-23
    • Mizuuchi M.a.B.,, T.A.1
  • 6
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker T.A., and Luo L. Identification of residues in the Mu transposase essential for catalysis. Proc. Natl Acad. Sci. USA 91 (1994) 6654-6658
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 7
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration
    • Rice P., and Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell 82 (1995) 209-220
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 8
    • 30044434257 scopus 로고    scopus 로고
    • Enhancer-independent Mu transposition from two topologically distinct synapses
    • Yin Z., and Harshey R.M. Enhancer-independent Mu transposition from two topologically distinct synapses. Proc. Natl Acad. Sci. USA 102 (2005) 18884-18889
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18884-18889
    • Yin, Z.1    Harshey, R.M.2
  • 9
  • 10
    • 0037123778 scopus 로고    scopus 로고
    • Path of DNA within the Mu transpososome. Transposase interactions bridging two Mu ends and the enhancer trap five DNA supercoils
    • Pathania S., Jayaram M., and Harshey R.M. Path of DNA within the Mu transpososome. Transposase interactions bridging two Mu ends and the enhancer trap five DNA supercoils. Cell 109 (2002) 425-436
    • (2002) Cell , vol.109 , pp. 425-436
    • Pathania, S.1    Jayaram, M.2    Harshey, R.M.3
  • 11
    • 0026708067 scopus 로고
    • Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition
    • Mizuuchi M., Baker T.A., and Mizuuchi K. Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition. Cell 70 (1992) 303-311
    • (1992) Cell , vol.70 , pp. 303-311
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 12
    • 0023646797 scopus 로고
    • Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu
    • Craigie R., and Mizuuchi K. Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu. Cell 51 (1987) 493-501
    • (1987) Cell , vol.51 , pp. 493-501
    • Craigie, R.1    Mizuuchi, K.2
  • 13
    • 0023663468 scopus 로고
    • Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA
    • Surette M.G., Buch S.J., and Chaconas G. Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell 49 (1987) 253-262
    • (1987) Cell , vol.49 , pp. 253-262
    • Surette, M.G.1    Buch, S.J.2    Chaconas, G.3
  • 14
    • 0025850374 scopus 로고
    • Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome
    • Lavoie B.D., Chan B.S., Allison R.G., and Chaconas G. Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome. EMBO J. 10 (1991) 3051-3059
    • (1991) EMBO J. , vol.10 , pp. 3051-3059
    • Lavoie, B.D.1    Chan, B.S.2    Allison, R.G.3    Chaconas, G.4
  • 15
    • 0023122585 scopus 로고
    • B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer
    • Maxwell A., Craigie R., and Mizuuchi K. B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer. Proc. Natl Acad. Sci. USA 84 (1987) 699-703
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 699-703
    • Maxwell, A.1    Craigie, R.2    Mizuuchi, K.3
  • 16
    • 0024294381 scopus 로고
    • Target immunity of Mu transposition reflects a differential distribution of Mu B protein
    • Adzuma K., and Mizuuchi K. Target immunity of Mu transposition reflects a differential distribution of Mu B protein. Cell 53 (1988) 257-266
    • (1988) Cell , vol.53 , pp. 257-266
    • Adzuma, K.1    Mizuuchi, K.2
  • 17
    • 0021684512 scopus 로고
    • Mechanism of transposition of bacteriophage Mu: polarity of the strand transfer reaction at the initiation of transposition
    • Mizuuchi K. Mechanism of transposition of bacteriophage Mu: polarity of the strand transfer reaction at the initiation of transposition. Cell 39 (1984) 395-404
    • (1984) Cell , vol.39 , pp. 395-404
    • Mizuuchi, K.1
  • 18
    • 0025899314 scopus 로고
    • Inversion of the phosphate chirality at the target site of Mu DNA strand transfer: evidence for a one-step transesterification mechanism
    • Mizuuchi K., and Adzuma K. Inversion of the phosphate chirality at the target site of Mu DNA strand transfer: evidence for a one-step transesterification mechanism. Cell 66 (1991) 129-140
    • (1991) Cell , vol.66 , pp. 129-140
    • Mizuuchi, K.1    Adzuma, K.2
  • 19
    • 0026093974 scopus 로고
    • DNase protection analysis of the stable synaptic complexes involved in Mu transposition
    • Mizuuchi M., Baker T.A., and Mizuuchi K. DNase protection analysis of the stable synaptic complexes involved in Mu transposition. Proc. Natl Acad. Sci. USA 88 (1991) 9031-9035
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9031-9035
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 20
    • 1242294509 scopus 로고    scopus 로고
    • Reorganization of the Mu transpososome active sites during a cooperative transition between DNA cleavage and joining
    • Williams T.L., and Baker T.A. Reorganization of the Mu transpososome active sites during a cooperative transition between DNA cleavage and joining. J. Biol. Chem. 279 (2004) 5135-5145
    • (2004) J. Biol. Chem. , vol.279 , pp. 5135-5145
    • Williams, T.L.1    Baker, T.A.2
  • 21
    • 17044421342 scopus 로고    scopus 로고
    • 3D reconstruction of the Mu transposase and the type 1 transpososome: a structural framework for Mu DNA transposition
    • Yuan J.F., Beniac D.R., Chaconas G., and Ottensmeyer F.P. 3D reconstruction of the Mu transposase and the type 1 transpososome: a structural framework for Mu DNA transposition. Genes Dev. 19 (2005) 840-852
    • (2005) Genes Dev. , vol.19 , pp. 840-852
    • Yuan, J.F.1    Beniac, D.R.2    Chaconas, G.3    Ottensmeyer, F.P.4
  • 22
    • 0031576325 scopus 로고    scopus 로고
    • Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase
    • Clubb R.T., Schumacher S., Mizuuchi K., Gronenborn A.M., and Clore G.M. Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase. J. Mol. Biol. 273 (1997) 19-25
    • (1997) J. Mol. Biol. , vol.273 , pp. 19-25
    • Clubb, R.T.1    Schumacher, S.2    Mizuuchi, K.3    Gronenborn, A.M.4    Clore, G.M.5
  • 23
    • 0025794342 scopus 로고
    • MuB protein allosterically activates strand transfer by the transposase of phage Mu
    • Baker T.A., Mizuuchi M., and Mizuuchi K. MuB protein allosterically activates strand transfer by the transposase of phage Mu. Cell 65 (1991) 1003-1013
    • (1991) Cell , vol.65 , pp. 1003-1013
    • Baker, T.A.1    Mizuuchi, M.2    Mizuuchi, K.3
  • 24
    • 1942533398 scopus 로고    scopus 로고
    • Visualizing the assembly and disassembly mechanisms of the MuB transposition targeting complex
    • Greene E.C., and Mizuuchi K. Visualizing the assembly and disassembly mechanisms of the MuB transposition targeting complex. J. Biol. Chem. 279 (2004) 16736-16743
    • (2004) J. Biol. Chem. , vol.279 , pp. 16736-16743
    • Greene, E.C.1    Mizuuchi, K.2
  • 25
    • 0036282822 scopus 로고    scopus 로고
    • Direct observation of single MuB polymers: evidence for a DNA-dependent conformational change for generating an active target complex
    • Greene E.C., and Mizuuchi K. Direct observation of single MuB polymers: evidence for a DNA-dependent conformational change for generating an active target complex. Mol. Cell 9 (2002) 1079-1089
    • (2002) Mol. Cell , vol.9 , pp. 1079-1089
    • Greene, E.C.1    Mizuuchi, K.2
  • 26
    • 0025953885 scopus 로고
    • Stimulation of the Mu DNA strand cleavage and intramolecular strand transfer reactions by the Mu B protein is independent of stable binding of the Mu B protein to DNA
    • Surette M.G., and Chaconas G. Stimulation of the Mu DNA strand cleavage and intramolecular strand transfer reactions by the Mu B protein is independent of stable binding of the Mu B protein to DNA. J. Biol. Chem. 266 (1991) 17306-17313
    • (1991) J. Biol. Chem. , vol.266 , pp. 17306-17313
    • Surette, M.G.1    Chaconas, G.2
  • 27
    • 0034486638 scopus 로고    scopus 로고
    • Domain III function of Mu transposase analysed by directed placement of subunits within the transpososome
    • Mariconda S., Namgoong S.Y., Yoon K.H., Jiang H., and Harshey R.M. Domain III function of Mu transposase analysed by directed placement of subunits within the transpososome. J. Biosci. 25 (2000) 347-360
    • (2000) J. Biosci. , vol.25 , pp. 347-360
    • Mariconda, S.1    Namgoong, S.Y.2    Yoon, K.H.3    Jiang, H.4    Harshey, R.M.5
  • 28
    • 0030908043 scopus 로고    scopus 로고
    • ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway
    • Levchenko I., Yamauchi M., and Baker T.A. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11 (1997) 1561-1572
    • (1997) Genes Dev. , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 29
    • 0041731693 scopus 로고    scopus 로고
    • Effect of mutations in the C-terminal domain of Mu B on DNA binding and interactions with Mu A transposase
    • Coros C.J., Sekino Y., Baker T.A., and Chaconas G. Effect of mutations in the C-terminal domain of Mu B on DNA binding and interactions with Mu A transposase. J. Biol. Chem. 278 (2003) 31210-31217
    • (2003) J. Biol. Chem. , vol.278 , pp. 31210-31217
    • Coros, C.J.1    Sekino, Y.2    Baker, T.A.3    Chaconas, G.4
  • 30
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko I., Luo L., and Baker T.A. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9 (1995) 2399-2408
    • (1995) Genes Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 31
    • 0029097732 scopus 로고
    • Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication
    • Nakai H., and Kruklitis R. Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication. J. Biol. Chem. 270 (1995) 19591-19598
    • (1995) J. Biol. Chem. , vol.270 , pp. 19591-19598
    • Nakai, H.1    Kruklitis, R.2
  • 32
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis R., Welty D.J., and Nakai H. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15 (1996) 935-944
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 33
    • 0028028002 scopus 로고
    • Complete transposition requires four active monomers in the mu transposase tetramer
    • Baker T.A., Kremenstova E., and Luo L. Complete transposition requires four active monomers in the mu transposase tetramer. Genes Dev. 8 (1994) 2416-2428
    • (1994) Genes Dev. , vol.8 , pp. 2416-2428
    • Baker, T.A.1    Kremenstova, E.2    Luo, L.3
  • 34
    • 0037040898 scopus 로고    scopus 로고
    • DNA recognition sites activate MuA transposase to perform transposition of non-Mu DNA
    • Goldhaber-Gordon I., Williams T.L., and Baker T.A. DNA recognition sites activate MuA transposase to perform transposition of non-Mu DNA. J. Biol. Chem. 277 (2002) 7694-7702
    • (2002) J. Biol. Chem. , vol.277 , pp. 7694-7702
    • Goldhaber-Gordon, I.1    Williams, T.L.2    Baker, T.A.3
  • 35
    • 0030828364 scopus 로고    scopus 로고
    • A new set of Mu DNA transposition intermediates: alternate pathways of target capture preceding strand transfer
    • Naigamwalla D.Z., and Chaconas G. A new set of Mu DNA transposition intermediates: alternate pathways of target capture preceding strand transfer. EMBO J. 16 (1997) 5227-5234
    • (1997) EMBO J. , vol.16 , pp. 5227-5234
    • Naigamwalla, D.Z.1    Chaconas, G.2
  • 36
    • 0346850576 scopus 로고    scopus 로고
    • MuA transposase separates DNA sequence recognition from catalysis
    • Goldhaber-Gordon I., Early M.H., and Baker T.A. MuA transposase separates DNA sequence recognition from catalysis. Biochemistry 42 (2003) 14633-14642
    • (2003) Biochemistry , vol.42 , pp. 14633-14642
    • Goldhaber-Gordon, I.1    Early, M.H.2    Baker, T.A.3
  • 37
    • 0032530649 scopus 로고    scopus 로고
    • An ATP-ADP switch in MuB controls progression of the Mu transposition pathway
    • Yamauchi M., and Baker T.A. An ATP-ADP switch in MuB controls progression of the Mu transposition pathway. EMBO J. 17 (1998) 5509-5518
    • (1998) EMBO J. , vol.17 , pp. 5509-5518
    • Yamauchi, M.1    Baker, T.A.2
  • 38
    • 0033569428 scopus 로고    scopus 로고
    • Organization and dynamics of the Mu transpososome: recombination by communication between two active sites
    • Williams T.L., Jackson E.L., Carritte A., and Baker T.A. Organization and dynamics of the Mu transpososome: recombination by communication between two active sites. Genes Dev. 13 (1999) 2725-2737
    • (1999) Genes Dev. , vol.13 , pp. 2725-2737
    • Williams, T.L.1    Jackson, E.L.2    Carritte, A.3    Baker, T.A.4
  • 39
    • 0029871975 scopus 로고    scopus 로고
    • The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis
    • Aldaz H., Schuster E., and Baker T.A. The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis. Cell 85 (1996) 257-269
    • (1996) Cell , vol.85 , pp. 257-269
    • Aldaz, H.1    Schuster, E.2    Baker, T.A.3
  • 40
    • 0029048507 scopus 로고
    • A domain sharing model for active site assembly within the Mu A tetramer during transposition: the enhancer may specify domain contributions
    • Yang J.Y., Kim K., Jayaram M., and Harshey R.M. A domain sharing model for active site assembly within the Mu A tetramer during transposition: the enhancer may specify domain contributions. EMBO J. 14 (1995) 2374-2384
    • (1995) EMBO J. , vol.14 , pp. 2374-2384
    • Yang, J.Y.1    Kim, K.2    Jayaram, M.3    Harshey, R.M.4
  • 41
    • 0028885831 scopus 로고
    • Assembly of phage Mu transpososomes: cooperative transitions assisted by protein and DNA scaffolds
    • Mizuuchi M., Baker T.A., and Mizuuchi K. Assembly of phage Mu transpososomes: cooperative transitions assisted by protein and DNA scaffolds. Cell 83 (1995) 375-385
    • (1995) Cell , vol.83 , pp. 375-385
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 42
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow S.A., Vincent K.A., Ellison V., and Brown P.O. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 255 (1992) 723-726
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 43
    • 0027404102 scopus 로고
    • Characterization of the forward and reverse integration reactions of the Moloney murine leukemia virus integrase protein purified from Escherichia coli
    • Jonsson C.B., Donzella G.A., and Roth M.J. Characterization of the forward and reverse integration reactions of the Moloney murine leukemia virus integrase protein purified from Escherichia coli. J. Biol. Chem. 268 (1993) 1462-1469
    • (1993) J. Biol. Chem. , vol.268 , pp. 1462-1469
    • Jonsson, C.B.1    Donzella, G.A.2    Roth, M.J.3
  • 44
    • 0033584864 scopus 로고    scopus 로고
    • Stereospecificity of reactions catalyzed by HIV-1 integrase
    • Gerton J.L., Herschlag D., and Brown P.O. Stereospecificity of reactions catalyzed by HIV-1 integrase. J. Biol. Chem. 274 (1999) 33480-33487
    • (1999) J. Biol. Chem. , vol.274 , pp. 33480-33487
    • Gerton, J.L.1    Herschlag, D.2    Brown, P.O.3
  • 45
    • 4444363151 scopus 로고    scopus 로고
    • True reversal of Mu integration
    • Au T.K., Pathania S., and Harshey R.M. True reversal of Mu integration. EMBO J. 23 (2004) 3408-3420
    • (2004) EMBO J. , vol.23 , pp. 3408-3420
    • Au, T.K.1    Pathania, S.2    Harshey, R.M.3
  • 46
    • 0037102133 scopus 로고    scopus 로고
    • IHF-independent assembly of the Tn10 strand transfer transpososome: implications for inhibition of disintegration
    • Stewart B.J., Wardle S.J., and Haniford D.B. IHF-independent assembly of the Tn10 strand transfer transpososome: implications for inhibition of disintegration. EMBO J. 21 (2002) 4380-4390
    • (2002) EMBO J. , vol.21 , pp. 4380-4390
    • Stewart, B.J.1    Wardle, S.J.2    Haniford, D.B.3
  • 47
    • 0032055477 scopus 로고    scopus 로고
    • Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro
    • Beall E.L., and Rio D.C. Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro. EMBO J. 17 (1998) 2122-2136
    • (1998) EMBO J. , vol.17 , pp. 2122-2136
    • Beall, E.L.1    Rio, D.C.2
  • 49
    • 0034625261 scopus 로고    scopus 로고
    • RAG1/2-mediated resolution of transposition intermediates: two pathways and possible consequences
    • Melek M., and Gellert M. RAG1/2-mediated resolution of transposition intermediates: two pathways and possible consequences. Cell 101 (2000) 625-633
    • (2000) Cell , vol.101 , pp. 625-633
    • Melek, M.1    Gellert, M.2
  • 50
    • 0028352363 scopus 로고
    • Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase
    • Mazumder A., Engelman A., Craigie R., Fesen M., and Pommier Y. Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase. Nucl. Acids Res. 22 (1994) 1037-1043
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1037-1043
    • Mazumder, A.1    Engelman, A.2    Craigie, R.3    Fesen, M.4    Pommier, Y.5
  • 51
    • 23644449096 scopus 로고    scopus 로고
    • Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase
    • Burton B.M., and Baker T.A. Remodeling protein complexes: insights from the AAA+ unfoldase ClpX and Mu transposase. Protein Sci. 14 (2005) 1945-1954
    • (2005) Protein Sci. , vol.14 , pp. 1945-1954
    • Burton, B.M.1    Baker, T.A.2
  • 52
    • 0030859543 scopus 로고    scopus 로고
    • Avoiding self: two Tn7-encoded proteins mediate target immunity in Tn7 transposition
    • Stellwagen A.E., and Craig N.L. Avoiding self: two Tn7-encoded proteins mediate target immunity in Tn7 transposition. EMBO J. 16 (1997) 6823-6834
    • (1997) EMBO J. , vol.16 , pp. 6823-6834
    • Stellwagen, A.E.1    Craig, N.L.2
  • 53
    • 0034816496 scopus 로고    scopus 로고
    • Targeting of the yeast Ty5 retrotransposon to silent chromatin is mediated by interactions between integrase and Sir4p
    • Xie W., Gai X., Zhu Y., Zappulla D.C., Sternglanz R., and Voytas D.F. Targeting of the yeast Ty5 retrotransposon to silent chromatin is mediated by interactions between integrase and Sir4p. Mol. Cell. Biol. 21 (2001) 6606-6614
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6606-6614
    • Xie, W.1    Gai, X.2    Zhu, Y.3    Zappulla, D.C.4    Sternglanz, R.5    Voytas, D.F.6
  • 54
    • 0028936732 scopus 로고
    • Requirement of RNA polymerase III transcription factors for in vitro position-specific integration of a retroviruslike element
    • Kirchner J., Connolly C.M., and Sandmeyer S.B. Requirement of RNA polymerase III transcription factors for in vitro position-specific integration of a retroviruslike element. Science 267 (1995) 1488-1491
    • (1995) Science , vol.267 , pp. 1488-1491
    • Kirchner, J.1    Connolly, C.M.2    Sandmeyer, S.B.3
  • 55
    • 0037688128 scopus 로고    scopus 로고
    • Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex
    • Burton B.M., and Baker T.A. Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex. Chem. Biol. 10 (2003) 463-472
    • (2003) Chem. Biol. , vol.10 , pp. 463-472
    • Burton, B.M.1    Baker, T.A.2
  • 56
    • 0025911364 scopus 로고
    • Steady-state kinetic analysis of ATP hydrolysis by the B protein of bacteriophage mu. Involvement of protein oligomerization in the ATPase cycle
    • Adzuma K., and Mizuuchi K. Steady-state kinetic analysis of ATP hydrolysis by the B protein of bacteriophage mu. Involvement of protein oligomerization in the ATPase cycle. J. Biol. Chem. 266 (1991) 6159-6167
    • (1991) J. Biol. Chem. , vol.266 , pp. 6159-6167
    • Adzuma, K.1    Mizuuchi, K.2
  • 57
    • 0037086543 scopus 로고    scopus 로고
    • Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex
    • Greene E.C., and Mizuuchi K. Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex. EMBO J. 21 (2002) 1477-1486
    • (2002) EMBO J. , vol.21 , pp. 1477-1486
    • Greene, E.C.1    Mizuuchi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.