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Volumn 63, Issue 2, 2007, Pages 468-481

Polymerization of SopA partition ATPase: Regulation by DNA binding and SopB

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BINDING PROTEIN; BINDING PROTEIN SOPA; BINDING PROTEIN SOPB; POLYMER; UNCLASSIFIED DRUG;

EID: 33846081941     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05537.x     Document Type: Article
Times cited : (97)

References (49)
  • 1
    • 31344431592 scopus 로고    scopus 로고
    • Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB
    • Adachi, S., Hori, K., and Hiraga, S. (2006) Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB. J Mol Biol 356: 850-863.
    • (2006) J Mol Biol , vol.356 , pp. 850-863
    • Adachi, S.1    Hori, K.2    Hiraga, S.3
  • 2
    • 17844403033 scopus 로고    scopus 로고
    • Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
    • Barilla, D., Rosenberg, M.F., Nobbmann, U., and Hayes, F. (2005) Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF. EMBO J 24: 1453-1464.
    • (2005) EMBO J , vol.24 , pp. 1453-1464
    • Barilla, D.1    Rosenberg, M.F.2    Nobbmann, U.3    Hayes, F.4
  • 3
    • 0028912206 scopus 로고
    • Partition functions of mini-F affect plasmid DNA topology in Escherichia coli
    • Biek, D.P., and Strings, J. (1995) Partition functions of mini-F affect plasmid DNA topology in Escherichia coli. J Mol Biol 246: 388-400.
    • (1995) J Mol Biol , vol.246 , pp. 388-400
    • Biek, D.P.1    Strings, J.2
  • 4
    • 0032823461 scopus 로고    scopus 로고
    • Effect of growth rate and incC mutation on symmetric plasmid distribution by the IncP-1 partitioning apparatus
    • Bignell, C.R., Haines, A.S., Khare, D., and Thomas, C.M. (1999) Effect of growth rate and incC mutation on symmetric plasmid distribution by the IncP-1 partitioning apparatus. Mol Microbiol 34: 205-216.
    • (1999) Mol Microbiol , vol.34 , pp. 205-216
    • Bignell, C.R.1    Haines, A.S.2    Khare, D.3    Thomas, C.M.4
  • 5
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89: 7290-7294.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 6
    • 0033106245 scopus 로고    scopus 로고
    • P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities
    • Bouet, J.Y., and Funnell, B.E. (1999) P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities. EMBO J 18: 1415-1424.
    • (1999) EMBO J , vol.18 , pp. 1415-1424
    • Bouet, J.Y.1    Funnell, B.E.2
  • 7
    • 13144251156 scopus 로고    scopus 로고
    • Probing plasmid partition with centromere-based incompatibility
    • Bouet, J.Y., Rech, J., Egloff, S., Biek, D.P., and Lane, D. (2005) Probing plasmid partition with centromere-based incompatibility. Mol Microbiol 55: 511-525.
    • (2005) Mol Microbiol , vol.55 , pp. 511-525
    • Bouet, J.Y.1    Rech, J.2    Egloff, S.3    Biek, D.P.4    Lane, D.5
  • 8
    • 0024971458 scopus 로고
    • Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes
    • Cann, J.R. (1989) Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes. J Biol Chem 264: 17032-17040.
    • (1989) J Biol Chem , vol.264 , pp. 17032-17040
    • Cann, J.R.1
  • 9
    • 0027944755 scopus 로고
    • The P1 plasmid partition protein ParA. A role for ATP in site-specific DNA binding
    • Davey, M.J., and Funnell, B.E. (1994) The P1 plasmid partition protein ParA. A role for ATP in site-specific DNA binding. J Biol Chem 269: 29908-29913.
    • (1994) J Biol Chem , vol.269 , pp. 29908-29913
    • Davey, M.J.1    Funnell, B.E.2
  • 10
    • 0030919148 scopus 로고    scopus 로고
    • Modulation of the P1 plasmid partition protein ParA by ATP, ADP, and P1 ParB
    • Davey, M.J., and Funnell, B.E. (1997) Modulation of the P1 plasmid partition protein ParA by ATP, ADP, and P1 ParB. J Biol Chem 272: 15286-15292.
    • (1997) J Biol Chem , vol.272 , pp. 15286-15292
    • Davey, M.J.1    Funnell, B.E.2
  • 11
    • 0026585678 scopus 로고
    • Biochemical activities of the ParA partition protein of the P1 plasmid
    • Davis, M.A., Martin, K.A., and Austin, S.J. (1992) Biochemical activities of the ParA partition protein of the P1 plasmid. Mol Microbiol 6: 1141-1147.
    • (1992) Mol Microbiol , vol.6 , pp. 1141-1147
    • Davis, M.A.1    Martin, K.A.2    Austin, S.J.3
  • 12
    • 0029798284 scopus 로고    scopus 로고
    • The P1 ParA protein and its ATPase activity play a direct role in the segregation of plasmid copies to daughter cells
    • Davis, M.A., Radnedge, L., Martin, K.A., Hayes, F., Youngren, B., and Austin, S.J. (1996) The P1 ParA protein and its ATPase activity play a direct role in the segregation of plasmid copies to daughter cells. Mol Microbiol 21: 1029-1036.
    • (1996) Mol Microbiol , vol.21 , pp. 1029-1036
    • Davis, M.A.1    Radnedge, L.2    Martin, K.A.3    Hayes, F.4    Youngren, B.5    Austin, S.J.6
  • 13
    • 0036670336 scopus 로고    scopus 로고
    • ParB-stimulated nucleotide exchange regulates a switch in functionally distinct ParA activities
    • Easter, J., Jr, and Gober, J.W. (2002) ParB-stimulated nucleotide exchange regulates a switch in functionally distinct ParA activities. Mol Cell 10: 427-434.
    • (2002) Mol Cell , vol.10 , pp. 427-434
    • Easter Jr, J.1    Gober, J.W.2
  • 14
    • 0035910030 scopus 로고    scopus 로고
    • The double par locus of virulence factor pB171: DNA segregation is correlated with oscillation of ParA
    • Ebersbach, G., and Gerdes, K. (2001) The double par locus of virulence factor pB171: DNA segregation is correlated with oscillation of ParA. Proc Natl Acad Sci USA 98: 15078-15083.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15078-15083
    • Ebersbach, G.1    Gerdes, K.2
  • 15
    • 1942468854 scopus 로고    scopus 로고
    • Bacterial mitosis: Partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell
    • Ebersbach, G., and Gerdes, K. (2004) Bacterial mitosis: partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at mid-cell. Mol Microbiol 52: 385-398.
    • (2004) Mol Microbiol , vol.52 , pp. 385-398
    • Ebersbach, G.1    Gerdes, K.2
  • 16
    • 29444437147 scopus 로고    scopus 로고
    • Plasmid segregation mechanisms
    • Ebersbach, G., and Gerdes, K. (2005) Plasmid segregation mechanisms. Annu Rev Genet 39: 453-479.
    • (2005) Annu Rev Genet , vol.39 , pp. 453-479
    • Ebersbach, G.1    Gerdes, K.2
  • 17
    • 33748512415 scopus 로고    scopus 로고
    • Regular cellular distribution of plasmids by oscillating and filament-forming ParA ATPase of plasmid pB171
    • Ebersbach, G., Ringgaard, S., Moller-Jensen, J., Wang, Q., Sherratt, D.J., and Gerdes, K. (2006) Regular cellular distribution of plasmids by oscillating and filament-forming ParA ATPase of plasmid pB171. Mol Microbiol 61: 1428-1442.
    • (2006) Mol Microbiol , vol.61 , pp. 1428-1442
    • Ebersbach, G.1    Ringgaard, S.2    Moller-Jensen, J.3    Wang, Q.4    Sherratt, D.J.5    Gerdes, K.6
  • 18
    • 0035724353 scopus 로고    scopus 로고
    • Pairing of P1 plasmid partition sites by ParB
    • Edgar, R., Chattoraj, D.K., and Yarmolinsky, M. (2001) Pairing of P1 plasmid partition sites by ParB. Mol Microbiol 42: 1363-1370.
    • (2001) Mol Microbiol , vol.42 , pp. 1363-1370
    • Edgar, R.1    Chattoraj, D.K.2    Yarmolinsky, M.3
  • 19
    • 33645095732 scopus 로고    scopus 로고
    • P1 plasmid partition: In vivo evidence for the ParA- and ParB-mediated formation of an anchored parS complex in the absence of a partner parS
    • Edgar, R., Biek, D., and Yarmolinsky, M. (2006) P1 plasmid partition: in vivo evidence for the ParA- and ParB-mediated formation of an anchored parS complex in the absence of a partner parS. Mol Microbiol 59: 276-287.
    • (2006) Mol Microbiol , vol.59 , pp. 276-287
    • Edgar, R.1    Biek, D.2    Yarmolinsky, M.3
  • 20
    • 0033592870 scopus 로고    scopus 로고
    • Intracellular localization of P1 ParB protein depends on ParA and parS
    • Erdmann, N., Petroff, T., and Funnell, B.E. (1999) Intracellular localization of P1 ParB protein depends on ParA and parS. Proc Natl Acad Sci USA 96: 14905-14910.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14905-14910
    • Erdmann, N.1    Petroff, T.2    Funnell, B.E.3
  • 21
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner, E.C., Campbell, C.S., and Mullins, R.D. (2004) Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306: 1021-1025.
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1    Campbell, C.S.2    Mullins, R.D.3
  • 22
    • 0033861269 scopus 로고    scopus 로고
    • Plasmid and chromosome partitioning: Surprises from phylogeny
    • Gerdes, K., Moller-Jensen, J., and Bugge Jensen, R. (2000) Plasmid and chromosome partitioning: surprises from phylogeny. Mol Microbiol 37: 455-466.
    • (2000) Mol Microbiol , vol.37 , pp. 455-466
    • Gerdes, K.1    Moller-Jensen, J.2    Bugge Jensen, R.3
  • 23
    • 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. (2002) Dynamics of a protein polymer: the assembly and disassembly pathways of the MuB transposition target complex. EMBO J 21: 1477-1486.
    • (2002) EMBO J , vol.21 , pp. 1477-1486
    • Greene, E.C.1    Mizuuchi, K.2
  • 24
    • 0035901493 scopus 로고    scopus 로고
    • Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
    • Hayashi, I., Oyama, T., and Morikawa, K. (2001) Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J 20: 1819-1828.
    • (2001) EMBO J , vol.20 , pp. 1819-1828
    • Hayashi, I.1    Oyama, T.2    Morikawa, K.3
  • 25
    • 0031888009 scopus 로고    scopus 로고
    • Autoregulation of the partition genes of the mini-F plasmid and the intracellular localization of their products in Escherichia coli
    • Hirano, M., Mori, H., Onogi, T., Yamazoe, M., Niki, H., Ogura, T., and Hiraga, S. (1998) Autoregulation of the partition genes of the mini-F plasmid and the intracellular localization of their products in Escherichia coli. Mol Gen Genet 257: 392-403.
    • (1998) Mol Gen Genet , vol.257 , pp. 392-403
    • Hirano, M.1    Mori, H.2    Onogi, T.3    Yamazoe, M.4    Niki, H.5    Ogura, T.6    Hiraga, S.7
  • 26
    • 0037076380 scopus 로고    scopus 로고
    • Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
    • Hu, Z., Gogol, E.P., and Lutkenhaus, J. (2002) Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc Natl Acad Sci USA 99: 6761-6766.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6761-6766
    • Hu, Z.1    Gogol, E.P.2    Lutkenhaus, J.3
  • 27
    • 0037539991 scopus 로고    scopus 로고
    • A mechanism for ParB-dependent waves of ParA, a protein related to DNA segregation during cell division in prokaryotes
    • Hunding, A., Ebersbach, G., and Gerdes, K. (2003) A mechanism for ParB-dependent waves of ParA, a protein related to DNA segregation during cell division in prokaryotes. J Mol Biol 329: 35-43.
    • (2003) J Mol Biol , vol.329 , pp. 35-43
    • Hunding, A.1    Ebersbach, G.2    Gerdes, K.3
  • 28
    • 0031580213 scopus 로고    scopus 로고
    • Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex
    • Jensen, R.B., and Gerdes, K. (1997) Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex. J Mol Biol 269: 505-513.
    • (1997) J Mol Biol , vol.269 , pp. 505-513
    • Jensen, R.B.1    Gerdes, K.2
  • 29
    • 0032555159 scopus 로고    scopus 로고
    • Mechanism of DNA segregation in prokaryotes: Replicon pairing by parC of plasmid R1
    • Jensen, R.B., Lurz, R., and Gerdes, K. (1998) Mechanism of DNA segregation in prokaryotes: replicon pairing by parC of plasmid R1. Proc Natl Acad Sci USA 95: 8550-8555.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8550-8555
    • Jensen, R.B.1    Lurz, R.2    Gerdes, K.3
  • 30
    • 0031002795 scopus 로고    scopus 로고
    • Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex
    • Klemm, R.D., Austin, R.J., and Bell, S.P. (1997) Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex. Cell 88: 493-502.
    • (1997) Cell , vol.88 , pp. 493-502
    • Klemm, R.D.1    Austin, R.J.2    Bell, S.P.3
  • 31
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin, E.V. (1993) A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J Mol Biol 229: 1165-1174.
    • (1993) J Mol Biol , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 32
    • 0033678964 scopus 로고    scopus 로고
    • Disruption of the F plasmid partition complex in vivo by partition protein SopA
    • Lemonnier, M., Bouet, J.Y., Libante, V., and Lane, D. (2000) Disruption of the F plasmid partition complex in vivo by partition protein SopA. Mol Microbiol 38: 493-505.
    • (2000) Mol Microbiol , vol.38 , pp. 493-505
    • Lemonnier, M.1    Bouet, J.Y.2    Libante, V.3    Lane, D.4
  • 33
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: Structure and DNA binding of the Soj dimer - a conserved biological switch
    • Leonard, T.A., Butler, P.J., and Lowe, J. (2005) Bacterial chromosome segregation: structure and DNA binding of the Soj dimer - a conserved biological switch. EMBO J 24: 270-282.
    • (2005) EMBO J , vol.24 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 34
    • 0035976748 scopus 로고    scopus 로고
    • Role of the ATP-binding site of SopA protein in partition of the F plasmid
    • Libante, V., Thion, L., and Lane, D. (2001) Role of the ATP-binding site of SopA protein in partition of the F plasmid. J Mol Biol 314: 387-399.
    • (2001) J Mol Biol , vol.314 , pp. 387-399
    • Libante, V.1    Thion, L.2    Lane, D.3
  • 35
    • 29144454213 scopus 로고    scopus 로고
    • Bacterial DNA segregation by dynamic SopA polymers
    • Lim, G.E., Derman, A.I., and Pogliano, J. (2005) Bacterial DNA segregation by dynamic SopA polymers. Proc Natl Acad Sci USA 102: 17658-17663.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17658-17663
    • Lim, G.E.1    Derman, A.I.2    Pogliano, J.3
  • 36
    • 0028960197 scopus 로고
    • SopB protein-meditated silencing of genes linked to the sopC locus of Escherichia coli F plasmid
    • Lynch, A.S., and Wang, J.C. (1995) SopB protein-meditated silencing of genes linked to the sopC locus of Escherichia coli F plasmid. Proc Natl Acad Sci USA 92: 1896-1900.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1896-1900
    • Lynch, A.S.1    Wang, J.C.2
  • 37
    • 0033231585 scopus 로고    scopus 로고
    • Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation
    • Marston, A.L., and Errington, J. (1999) Dynamic movement of the ParA-like Soj protein of B. subtilis and its dual role in nucleoid organization and developmental regulation. Mol Cell 4: 673-682.
    • (1999) Mol Cell , vol.4 , pp. 673-682
    • Marston, A.L.1    Errington, J.2
  • 38
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Moller-Jensen, J., Jensen, R.B., Lowe, J., and Gerdes, K. (2002) Prokaryotic DNA segregation by an actin-like filament. EMBO J 21: 3119-3127.
    • (2002) EMBO J , vol.21 , pp. 3119-3127
    • Moller-Jensen, J.1    Jensen, R.B.2    Lowe, J.3    Gerdes, K.4
  • 39
    • 0024971390 scopus 로고
    • Purification and characterization of SopA and SopB proteins essential for F plasmid partitioning
    • Mori, H., Mori, Y., Ichinose, C., Niki, H., Ogura, T., Kato, A., and Hiraga, S. (1989) Purification and characterization of SopA and SopB proteins essential for F plasmid partitioning. J Biol Chem 264: 15535-15541.
    • (1989) J Biol Chem , vol.264 , pp. 15535-15541
    • Mori, H.1    Mori, Y.2    Ichinose, C.3    Niki, H.4    Ogura, T.5    Kato, A.6    Hiraga, S.7
  • 40
    • 0025149275 scopus 로고
    • A family of ATPases involved in active partitioning of diverse bacterial plasmids
    • Motallebi-Veshareh, M., Rouch, D.A., and Thomas, C.M. (1990) A family of ATPases involved in active partitioning of diverse bacterial plasmids. Mol Microbiol 4: 1455-1463.
    • (1990) Mol Microbiol , vol.4 , pp. 1455-1463
    • Motallebi-Veshareh, M.1    Rouch, D.A.2    Thomas, C.M.3
  • 41
    • 0033231557 scopus 로고    scopus 로고
    • Control of development by altered localization of a transcription factor in B. subtilis
    • Quisel, J.D., Lin, D.C., and Grossman, A.D. (1999) Control of development by altered localization of a transcription factor in B. subtilis. Mol Cell 4: 665-672.
    • (1999) Mol Cell , vol.4 , pp. 665-672
    • Quisel, J.D.1    Lin, D.C.2    Grossman, A.D.3
  • 42
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
    • Raskin, D.M., and de Boer, P.A. (1999) MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J Bacteriol 181: 6419-6424.
    • (1999) J Bacteriol , vol.181 , pp. 6419-6424
    • Raskin, D.M.1    de Boer, P.A.2
  • 43
    • 3142740459 scopus 로고    scopus 로고
    • Plasmid partitioning and the spreading of P1 partition protein ParB
    • Rodionov, O., and Yarmolinsky, M. (2004) Plasmid partitioning and the spreading of P1 partition protein ParB. Mol Microbiol 52: 1215-1223.
    • (2004) Mol Microbiol , vol.52 , pp. 1215-1223
    • Rodionov, O.1    Yarmolinsky, M.2
  • 44
    • 0033593587 scopus 로고    scopus 로고
    • Silencing of genes flanking the P1 plasmid centromere
    • Rodionov, O., Lobocka, M., and Yarmolinsky, M. (1999) Silencing of genes flanking the P1 plasmid centromere. Science 283: 546-549.
    • (1999) Science , vol.283 , pp. 546-549
    • Rodionov, O.1    Lobocka, M.2    Yarmolinsky, M.3
  • 45
    • 0037168644 scopus 로고    scopus 로고
    • Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE
    • Suefuji, K., Valluzzi, R., and RayChaudhuri, D. (2002) Dynamic assembly of MinD into filament bundles modulated by ATP, phospholipids, and MinE. Proc Natl Acad Sci USA 99: 16776-16781.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16776-16781
    • Suefuji, K.1    Valluzzi, R.2    RayChaudhuri, D.3
  • 46
    • 0026758465 scopus 로고
    • ATPase activity of SopA, a protein essential for active partitioning of F-plasmid
    • Watanabe, E., Wachi, M., Yamasaki, M., and Nagai, K. (1992) ATPase activity of SopA, a protein essential for active partitioning of F-plasmid. Mol Gen Genet 234: 346-352.
    • (1992) Mol Gen Genet , vol.234 , pp. 346-352
    • Watanabe, E.1    Wachi, M.2    Yamasaki, M.3    Nagai, K.4
  • 47
    • 0026528758 scopus 로고
    • Active partitioning of bacterial plasmids
    • Williams, D.R., and Thomas, C.M. (1992) Active partitioning of bacterial plasmids. J Gen Microbiol 138: 1-16.
    • (1992) J Gen Microbiol , vol.138 , pp. 1-16
    • Williams, D.R.1    Thomas, C.M.2
  • 48
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong, I., and Lohman, T.M. (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.M.2
  • 49
    • 0038605538 scopus 로고    scopus 로고
    • Intra- and internucleosomal protein-DNA interactions of the core histone tail domains in a model system
    • Zheng, C., and Hayes, J.J. (2003) Intra- and internucleosomal protein-DNA interactions of the core histone tail domains in a model system. J Biol Chem 278: 24217-24224.
    • (2003) J Biol Chem , vol.278 , pp. 24217-24224
    • Zheng, C.1    Hayes, J.J.2


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