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Volumn 2, Issue 6, 2014, Pages

Plasmid partition mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

CELL DIVISION; METABOLISM; PLASMID; TRANSPORT AT THE CELLULAR LEVEL;

EID: 84937779693     PISSN: None     EISSN: 21650497     Source Type: Journal    
DOI: 10.1128/microbiolspec.PLAS-0023-2014     Document Type: Article
Times cited : (122)

References (133)
  • 1
    • 14544272935 scopus 로고    scopus 로고
    • Partition systems of bacterial plasmids
    • In Funnell BE, Phillips GJ (ed), ASM Press, Washington, DC
    • Funnell BE, Slavcev RA. 2004. Partition systems of bacterial plasmids, p 81-103. In Funnell BE, Phillips GJ (ed), Plasmid Biology. ASM Press, Washington, DC.
    • (2004) Plasmid Biology , pp. 81-103
    • Funnell, B.E.1    Slavcev, R.A.2
  • 2
    • 0033861269 scopus 로고    scopus 로고
    • Plasmid and chromosome partitioning: surprises from phylogeny
    • Gerdes K, Moller-Jensen J, Jensen RB. 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    Jensen, R.B.3
  • 3
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin EV. 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
  • 4
    • 0035856287 scopus 로고    scopus 로고
    • The bacterial ParA-ParB partitioning proteins
    • Bignell C, Thomas CM. 2001. The bacterial ParA-ParB partitioning proteins. J Biotechnol 91:1-34.
    • (2001) J Biotechnol , vol.91 , pp. 1-34
    • Bignell, C.1    Thomas, C.M.2
  • 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, 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
    • 33646006683 scopus 로고    scopus 로고
    • A novel FtsZ-like protein is involved in replication of the anthrax toxin-encoding pXO1 plasmid in Bacillus anthracis
    • Tinsley E, Khan SA. 2006. A novel FtsZ-like protein is involved in replication of the anthrax toxin-encoding pXO1 plasmid in Bacillus anthracis. J Bacteriol 188:2829-2835.
    • (2006) J Bacteriol , vol.188 , pp. 2829-2835
    • Tinsley, E.1    Khan, S.A.2
  • 7
    • 33750979309 scopus 로고    scopus 로고
    • Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis
    • Tang M, Bideshi DK, Park H-W, Federici BA. 2006. Minireplicon from pBtoxis of Bacillus thuringiensis subsp. israelensis. Appl Environ Microbiol 72:6948-6954.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6948-6954
    • Tang, M.1    Bideshi, D.K.2    Park, H.-W.3    Federici, B.A.4
  • 8
    • 34249897760 scopus 로고    scopus 로고
    • Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis
    • Larsen RA, Cusumano C, Fujioka A, Lim-Fong G, Patterson P, Pogliano J. 2007. Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis. Genes Dev 21:1340-1352.
    • (2007) Genes Dev , vol.21 , pp. 1340-1352
    • Larsen, R.A.1    Cusumano, C.2    Fujioka, A.3    Lim-Fong, G.4    Patterson, P.5    Pogliano, J.6
  • 10
    • 84874192725 scopus 로고    scopus 로고
    • Organization and segregation of bacterial chromosomes
    • Wang XD, Llopis PM, Rudner DZ. 2013. Organization and segregation of bacterial chromosomes. Nat Rev Genet 14:191-203.
    • (2013) Nat Rev Genet , vol.14 , pp. 191-203
    • Wang, X.D.1    Llopis, P.M.2    Rudner, D.Z.3
  • 11
    • 0034687751 scopus 로고    scopus 로고
    • Active segregation by the Bacillus subtilis partitioning system in Escherichia coli
    • Yamaichi Y, Niki H. 2000. Active segregation by the Bacillus subtilis partitioning system in Escherichia coli. Proc Natl Acad Sci USA 97:14656-14661.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14656-14661
    • Yamaichi, Y.1    Niki, H.2
  • 12
    • 52949106530 scopus 로고    scopus 로고
    • Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA
    • Murray H, Errington J. 2008. Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA. Cell 135:74-84.
    • (2008) Cell , vol.135 , pp. 74-84
    • Murray, H.1    Errington, J.2
  • 13
    • 65549135760 scopus 로고    scopus 로고
    • Recruitment of condensin to replication origin regions by ParB/SpoOJ promotes chromosome segregation in B. subtilis
    • Gruber S, Errington J. 2009. Recruitment of condensin to replication origin regions by ParB/SpoOJ promotes chromosome segregation in B. subtilis. Cell 137:685-696.
    • (2009) Cell , vol.137 , pp. 685-696
    • Gruber, S.1    Errington, J.2
  • 14
    • 65549149524 scopus 로고    scopus 로고
    • Recruitment of SMC by ParB-parS organizes the origin region and promotes efficient chromosome segregation
    • Sullivan NL, Marquis KA, Rudner DZ. 2009. Recruitment of SMC by ParB-parS organizes the origin region and promotes efficient chromosome segregation. Cell 137:697-707.
    • (2009) Cell , vol.137 , pp. 697-707
    • Sullivan, N.L.1    Marquis, K.A.2    Rudner, D.Z.3
  • 15
    • 0035910030 scopus 로고    scopus 로고
    • The double par locus of virulence factor pB171: DNA segregation is correlated with oscillation of ParA
    • Ebersbach G, 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
  • 17
    • 77749270506 scopus 로고    scopus 로고
    • Functional analysis of the stability determinant AlfB of pBET131, a miniplasmid derivative of Bacillus subtilis (natto) plasmid pLS32
    • Tanaka T. 2010. Functional analysis of the stability determinant AlfB of pBET131, a miniplasmid derivative of Bacillus subtilis (natto) plasmid pLS32. J Bacteriol 192:1221-1230.
    • (2010) J Bacteriol , vol.192 , pp. 1221-1230
    • Tanaka, T.1
  • 19
    • 0034765465 scopus 로고    scopus 로고
    • Determinants of segregational stability of the linear plasmid-prophage N15 of Escherichia coli
    • Grigoriev PS, Lobocka MB. 2001. Determinants of segregational stability of the linear plasmid-prophage N15 of Escherichia coli. Mol Microbiol 42:355-368.
    • (2001) Mol Microbiol , vol.42 , pp. 355-368
    • Grigoriev, P.S.1    Lobocka, M.B.2
  • 20
    • 77953540848 scopus 로고    scopus 로고
    • On the role of centromere dispersion in stability of linear bacterial plasmids
    • Dorokhov B, Ravin N, Lane D. 2010. On the role of centromere dispersion in stability of linear bacterial plasmids. Plasmid 64:51-59.
    • (2010) Plasmid , vol.64 , pp. 51-59
    • Dorokhov, B.1    Ravin, N.2    Lane, D.3
  • 21
  • 22
    • 0032555159 scopus 로고    scopus 로고
    • Mechanism of DNA segregation in prokaryotes: replicon pairing by parC of plasmid R1
    • Jensen RB, Lurz R, 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
  • 23
    • 71049168305 scopus 로고    scopus 로고
    • Single-molecule analysis of protein-DNA complexes formed during partition of newly replicated plasmid molecules in Streptococcus pyogenes
    • Pratto F, Suzuki Y, Takeyasu K, Alonso JC. 2009. Single-molecule analysis of protein-DNA complexes formed during partition of newly replicated plasmid molecules in Streptococcus pyogenes. J Biol Chem 284:30298-30306.
    • (2009) J Biol Chem , vol.284 , pp. 30298-30306
    • Pratto, F.1    Suzuki, Y.2    Takeyasu, K.3    Alonso, J.C.4
  • 24
    • 0032862454 scopus 로고    scopus 로고
    • P1 ParB domain structure includes two independent multimerization domains
    • Surtees JA, Funnell BE. 1999. P1 ParB domain structure includes two independent multimerization domains. J Bacteriol 181:5898-5908.
    • (1999) J Bacteriol , vol.181 , pp. 5898-5908
    • Surtees, J.A.1    Funnell, B.E.2
  • 25
    • 0035853857 scopus 로고    scopus 로고
    • The DNA binding domains of P1 ParB and the architecture of the P1 plasmid partition complex
    • Surtees JA, Funnell BE. 2001. The DNA binding domains of P1 ParB and the architecture of the P1 plasmid partition complex. J Biol Chem 276:12385-12394.
    • (2001) J Biol Chem , vol.276 , pp. 12385-12394
    • Surtees, J.A.1    Funnell, B.E.2
  • 26
    • 0038545473 scopus 로고    scopus 로고
    • Mapping of functional domains in F plasmid partition proteins reveals a bipartite SopB-recognition domain in SopA
    • Ravin NV, Rech J, Lane D. 2003. Mapping of functional domains in F plasmid partition proteins reveals a bipartite SopB-recognition domain in SopA. J Mol Biol 329:875-889.
    • (2003) J Mol Biol , vol.329 , pp. 875-889
    • Ravin, N.V.1    Rech, J.2    Lane, D.3
  • 27
    • 0032531743 scopus 로고    scopus 로고
    • Probing the structure of complex macromolecular interactions by homolog specificity scanning: the P1 and P7 plasmid partition systems
    • Radnedge L, Youngren B, Davis M, Austin S. 1998. Probing the structure of complex macromolecular interactions by homolog specificity scanning: the P1 and P7 plasmid partition systems. EMBOJ 17:6076-6085.
    • (1998) EMBOJ , vol.17 , pp. 6076-6085
    • Radnedge, L.1    Youngren, B.2    Davis, M.3    Austin, S.4
  • 29
    • 0037040226 scopus 로고    scopus 로고
    • An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4
    • Delbruck H, Ziegelin G, Lanka E, Heinemann U. 2002. An Src homology 3-like domain is responsible for dimerization of the repressor protein KorB encoded by the promiscuous IncP plasmid RP4. J Biol Chem 277:4191-4198.
    • (2002) J Biol Chem , vol.277 , pp. 4191-4198
    • Delbruck, H.1    Ziegelin, G.2    Lanka, E.3    Heinemann, U.4
  • 30
    • 3042642002 scopus 로고    scopus 로고
    • Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB
    • Khare D, Ziegelin G, Lanka E, Heinemann U. 2004. Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. Nat Struct Mol Biol 11:656-663.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 656-663
    • Khare, D.1    Ziegelin, G.2    Lanka, E.3    Heinemann, U.4
  • 31
    • 28544449434 scopus 로고    scopus 로고
    • ParB-DNA structures reveal DNA binding mechanism of partition complex formation
    • Schumacher MA, Funnell BE. 2005. ParB-DNA structures reveal DNA binding mechanism of partition complex formation. Nature 438:516-519.
    • (2005) Nature , vol.438 , pp. 516-519
    • Schumacher, M.A.1    Funnell, B.E.2
  • 32
    • 34249858192 scopus 로고    scopus 로고
    • Structure of a fourway bridged ParB-DNA complex provides insight into P1 segrosome assembly
    • Schumacher MA, Mansoor A, Funnell BE. 2007. Structure of a fourway bridged ParB-DNA complex provides insight into P1 segrosome assembly. J Biol Chem 282:10456-10464.
    • (2007) J Biol Chem , vol.282 , pp. 10456-10464
    • Schumacher, M.A.1    Mansoor, A.2    Funnell, B.E.3
  • 33
    • 77955243507 scopus 로고    scopus 로고
    • Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes
    • Schumacher MA, Piro KM, Xu WJ. 2010. Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. Nucleic Acids Res 38:4514-4526.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4514-4526
    • Schumacher, M.A.1    Piro, K.M.2    Xu, W.J.3
  • 34
    • 0030015553 scopus 로고    scopus 로고
    • Molecular dissection of a protein SopB essential for Escherichia coli F plasmid partition
    • Hanai R, Liu RP, Benedetti P, Caron PR, Lynch AS, Wang JC. 1996. Molecular dissection of a protein SopB essential for Escherichia coli F plasmid partition. J Biol Chem 271:17469-17475.
    • (1996) J Biol Chem , vol.271 , pp. 17469-17475
    • Hanai, R.1    Liu, R.P.2    Benedetti, P.3    Caron, P.R.4    Lynch, A.S.5    Wang, J.C.6
  • 37
    • 80053192327 scopus 로고    scopus 로고
    • Centromere binding specificity in assembly of the F plasmid partition complex
    • Pillet F, Sanchez A, Lane D, Leberre VA, Bouet JY. 2011. Centromere binding specificity in assembly of the F plasmid partition complex. Nucleic Acids Res 39:7477-7486.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7477-7486
    • Pillet, F.1    Sanchez, A.2    Lane, D.3    Leberre, V.A.4    Bouet, J.Y.5
  • 38
    • 84876388319 scopus 로고    scopus 로고
    • Insight into centromere-binding properties of ParB proteins: a secondary binding motif is essential for bacterial genome maintenance
    • Sanchez A, Rech J, Gasc C, Bouet JY. 2013. Insight into centromere-binding properties of ParB proteins: a secondary binding motif is essential for bacterial genome maintenance. Nucleic Acids Res 41:3094-3103.
    • (2013) Nucleic Acids Res , vol.41 , pp. 3094-3103
    • Sanchez, A.1    Rech, J.2    Gasc, C.3    Bouet, J.Y.4
  • 39
    • 34249705227 scopus 로고    scopus 로고
    • P1 partition complex assembly involves several modes of protein-DNA recognition
    • Vecchiarelli AG, Schumacher MA, Funnell BE. 2007. P1 partition complex assembly involves several modes of protein-DNA recognition. J Biol Chem 282:10944-10952.
    • (2007) J Biol Chem , vol.282 , pp. 10944-10952
    • Vecchiarelli, A.G.1    Schumacher, M.A.2    Funnell, B.E.3
  • 40
    • 71049141221 scopus 로고    scopus 로고
    • Dual role of DNA in regulating ATP hydrolysis by the SopA partition protein
    • Ah-Seng Y, Lopez F, Pasta F, Lane D, Bouet J-Y. 2009. Dual role of DNA in regulating ATP hydrolysis by the SopA partition protein. J Biol Chem 284:30067-30075.
    • (2009) J Biol Chem , vol.284 , pp. 30067-30075
    • Ah-Seng, Y.1    Lopez, F.2    Pasta, F.3    Lane, D.4    Bouet, J.-Y.5
  • 41
    • 3242882269 scopus 로고    scopus 로고
    • Structural analysis of the chromosome segregation protein Spo0J from Thermus thermophilus
    • Leonard TA, Butler PJG, Lowe J. 2004. Structural analysis of the chromosome segregation protein Spo0J from Thermus thermophilus. Mol Microbiol 53:419-432.
    • (2004) Mol Microbiol , vol.53 , pp. 419-432
    • Leonard, T.A.1    Butler, P.J.G.2    Lowe, J.3
  • 42
    • 33747067108 scopus 로고    scopus 로고
    • The bacterial chromosome segregation protein Spo0J spreads along DNA from parS nucleation sites
    • Murray H, Ferreira H, Errington J. 2006. The bacterial chromosome segregation protein Spo0J spreads along DNA from parS nucleation sites. Mol Microbiol 61:1352-1361.
    • (2006) Mol Microbiol , vol.61 , pp. 1352-1361
    • Murray, H.1    Ferreira, H.2    Errington, J.3
  • 43
    • 0033592870 scopus 로고    scopus 로고
    • Intracellular localization of P1 ParB protein depends on ParA and parS
    • Erdmann N, PetroffT, Funnell BE. 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
  • 44
    • 31344431592 scopus 로고    scopus 로고
    • Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB
    • Adachi S, Hori K, 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
  • 45
    • 77749246076 scopus 로고    scopus 로고
    • P1 plasmid segregation: accurate re-distribution by dynamic plasmid pairing and separation
    • Sengupta M, Nielsen HJ, Youngren B, Austin S. 2010. P1 plasmid segregation: accurate re-distribution by dynamic plasmid pairing and separation. J Bacteriol 192:1175-1183.
    • (2010) J Bacteriol , vol.192 , pp. 1175-1183
    • Sengupta, M.1    Nielsen, H.J.2    Youngren, B.3    Austin, S.4
  • 46
    • 34249810957 scopus 로고    scopus 로고
    • Oscillating focus of SopA associated with filamentous structure guides partitioning of F plasmid
    • Hatano T, Yamaichi Y, Niki H. 2007. Oscillating focus of SopA associated with filamentous structure guides partitioning of F plasmid. Mol Microbiol 64:1198-1213.
    • (2007) Mol Microbiol , vol.64 , pp. 1198-1213
    • Hatano, T.1    Yamaichi, Y.2    Niki, H.3
  • 47
    • 78649614755 scopus 로고    scopus 로고
    • Partitioning of P1 plasmids by gradual distribution of the ATPase ParA
    • Hatano T, Niki H. 2010. Partitioning of P1 plasmids by gradual distribution of the ATPase ParA. Mol Microbiol 78:1182-1198.
    • (2010) Mol Microbiol , vol.78 , pp. 1182-1198
    • Hatano, T.1    Niki, H.2
  • 48
    • 0033587717 scopus 로고    scopus 로고
    • Gene silencing via protein-mediated subcellular localization of DNA
    • Kim S-K, Wang JC. 1999. Gene silencing via protein-mediated subcellular localization of DNA. Proc Natl Acad Sci USA 96:8557-8561.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8557-8561
    • Kim, S.-K.1    Wang, J.C.2
  • 49
    • 0033593587 scopus 로고    scopus 로고
    • Silencing of genes flanking the P1 plasmid centromere
    • Rodionov O, Lobocka M, 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
  • 50
    • 3142740459 scopus 로고    scopus 로고
    • Plasmid partitioning and the spreading of P1 partition protein ParB
    • Rodionov O, 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
  • 51
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: variations on a theme
    • Schreiter ER, Drennan CL. 2007. Ribbon-helix-helix transcription factors: variations on a theme. Nat Rev Microbiol 5:710-720.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 710-720
    • Schreiter, E.R.1    Drennan, C.L.2
  • 52
    • 0035824885 scopus 로고    scopus 로고
    • Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5Åresolution
    • Murayama K, Orth P, de la Hoz AB, Alonso JC, Saenger W. 2001. Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5Åresolution. J Mol Biol 314:789-796.
    • (2001) J Mol Biol , vol.314 , pp. 789-796
    • Murayama, K.1    Orth, P.2    de la Hoz, A.B.3    Alonso, J.C.4    Saenger, W.5
  • 53
    • 0344826584 scopus 로고    scopus 로고
    • ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure
    • Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian L-Y. 2003. ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. Mol Microbiol 50:1141-1153.
    • (2003) Mol Microbiol , vol.50 , pp. 1141-1153
    • Golovanov, A.P.1    Barillà, D.2    Golovanova, M.3    Hayes, F.4    Lian, L.-Y.5
  • 54
    • 33645528243 scopus 로고    scopus 로고
    • Structures of ω repressors bound to direct and inverted DNA repeats explain modulation of transcription
    • Weihofen WA, Cicek A, Pratto F, Alonso JC, Saenger W. 2006. Structures of ω repressors bound to direct and inverted DNA repeats explain modulation of transcription. Nucleic Acids Res 34:1450-1458.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1450-1458
    • Weihofen, W.A.1    Cicek, A.2    Pratto, F.3    Alonso, J.C.4    Saenger, W.5
  • 55
    • 79954585164 scopus 로고    scopus 로고
    • Crystal structure and centromere binding of the plasmid segregation protein ParB from pCXC100
    • Huang L, Yin P, Zhu X, Zhang Y, Ye KQ. 2011. Crystal structure and centromere binding of the plasmid segregation protein ParB from pCXC100. Nucleic Acids Res 39:2954-2968.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2954-2968
    • Huang, L.1    Yin, P.2    Zhu, X.3    Zhang, Y.4    Ye, K.Q.5
  • 56
    • 33846919050 scopus 로고    scopus 로고
    • The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif
    • Barillà D, Carmelo E, Hayes F. 2007. The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif. Proc Natl Acad Sci USA 104:1811-1816.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1811-1816
    • Barillà, D.1    Carmelo, E.2    Hayes, F.3
  • 58
    • 46349097796 scopus 로고    scopus 로고
    • Streptococcus pyogenes pSM19035 requires dynamic assembly of ATP-bound ParA and ParB on parS DNA during plasmid segregation
    • Pratto F, Cicek A, Weihofen WA, Lurz R, Saenger W, Alonso JC. 2008. Streptococcus pyogenes pSM19035 requires dynamic assembly of ATP-bound ParA and ParB on parS DNA during plasmid segregation. Nucleic Acids Res 36:3676-3689.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3676-3689
    • Pratto, F.1    Cicek, A.2    Weihofen, W.A.3    Lurz, R.4    Saenger, W.5    Alonso, J.C.6
  • 62
    • 77957107804 scopus 로고    scopus 로고
    • The ParMRC system: molecular mechanisms of plasmid segregation by actin-like filaments
    • Salje J, Gayathri P, Lowe J. 2010. The ParMRC system: molecular mechanisms of plasmid segregation by actin-like filaments. Nat RevMicrobiol 8:683-692.
    • (2010) Nat RevMicrobiol , vol.8 , pp. 683-692
    • Salje, J.1    Gayathri, P.2    Lowe, J.3
  • 63
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den Ent F, Moller-Jensen J, Amos LA, Gerdes K, Lowe J. 2002. F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J 21:6935-6943.
    • (2002) EMBO J , vol.21 , pp. 6935-6943
    • van den Ent, F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 64
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent F, Amos LA, Lowe J. 2001. Prokaryotic origin of the actin cytoskeleton. Nature 413:39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • van den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 65
    • 70350141267 scopus 로고    scopus 로고
    • Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A
    • Derman AI, Becker EC, Truong BD, Fujioka A, Tucey TM, Erb ML, Patterson PC, Pogliano J. 2009. Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A. Mol Microbiol 73:534-552.
    • (2009) Mol Microbiol , vol.73 , pp. 534-552
    • Derman, A.I.1    Becker, E.C.2    Truong, B.D.3    Fujioka, A.4    Tucey, T.M.5    Erb, M.L.6    Patterson, P.C.7    Pogliano, J.8
  • 66
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner EC, Campbell CS, Mullins RD. 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
  • 67
    • 33847675333 scopus 로고    scopus 로고
    • Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homolog
    • Garner EC, Campbell CS, Weibel DB, Mullins RD. 2007. Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homolog. Science 315:1270-1274.
    • (2007) Science , vol.315 , pp. 1270-1274
    • Garner, E.C.1    Campbell, C.S.2    Weibel, D.B.3    Mullins, R.D.4
  • 68
    • 79954609556 scopus 로고    scopus 로고
    • Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins
    • Rivera CR, Kollman JM, Polka JK, Agard DA, Mullins RD. 2011. Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins. J Biol Chem 286:14282-14290.
    • (2011) J Biol Chem , vol.286 , pp. 14282-14290
    • Rivera, C.R.1    Kollman, J.M.2    Polka, J.K.3    Agard, D.A.4    Mullins, R.D.5
  • 70
    • 69849107000 scopus 로고    scopus 로고
    • Structural polymorphism of the ParM filament and dynamic instability
    • Galkin VE, Orlova A, Rivera C, Mullins RD, Egelman EH. 2009. Structural polymorphism of the ParM filament and dynamic instability. Structure 17:1253-1264.
    • (2009) Structure , vol.17 , pp. 1253-1264
    • Galkin, V.E.1    Orlova, A.2    Rivera, C.3    Mullins, R.D.4    Egelman, E.H.5
  • 71
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism
    • Moller-Jensen J, Borch J, Dam M, Jensen RB, RoepstorffP, Gerdes K. 2003. Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol Cell 12:1477-1487.
    • (2003) Mol Cell , vol.12 , pp. 1477-1487
    • Moller-Jensen, J.1    Borch, J.2    Dam, M.3    Jensen, R.B.4    Roepstorff, P.5    Gerdes, K.6
  • 72
    • 36849033421 scopus 로고    scopus 로고
    • In vivo visualization of type II plasmid segregation: bacterial actin filaments pushing plasmids
    • Campbell CS, Mullins RD. 2007. In vivo visualization of type II plasmid segregation: bacterial actin filaments pushing plasmids. J Cell Biol 179:1059-1066.
    • (2007) J Cell Biol , vol.179 , pp. 1059-1066
    • Campbell, C.S.1    Mullins, R.D.2
  • 73
    • 58849121358 scopus 로고    scopus 로고
    • Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation
    • Salje J, Zuber B, Lowe J. 2009. Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation. Science 323:509-512.
    • (2009) Science , vol.323 , pp. 509-512
    • Salje, J.1    Zuber, B.2    Lowe, J.3
  • 74
    • 84870708478 scopus 로고    scopus 로고
    • A bipolar spindle of antiparallel ParM filaments drives bacterial plasmid segregation
    • Gayathri P, Fujii T, Moller-Jensen J, van den Ent F, Namba K, Lowe J. 2012. A bipolar spindle of antiparallel ParM filaments drives bacterial plasmid segregation. Science 338:1334-1337.
    • (2012) Science , vol.338 , pp. 1334-1337
    • Gayathri, P.1    Fujii, T.2    Moller-Jensen, J.3    van den Ent, F.4    Namba, K.5    Lowe, J.6
  • 78
    • 69849097861 scopus 로고    scopus 로고
    • The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation
    • Polka JK, Kollman JM, Agard DA, Mullins RD. 2009. The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation. J Bacteriol 191:6219-6230.
    • (2009) J Bacteriol , vol.191 , pp. 6219-6230
    • Polka, J.K.1    Kollman, J.M.2    Agard, D.A.3    Mullins, R.D.4
  • 79
    • 0025149275 scopus 로고
    • A family of ATPases involved in active partitioning of diverse bacterial plasmids
    • Motallebi-Veshareh M, Rouch DA, Thomas CM. 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
  • 80
    • 84865794654 scopus 로고    scopus 로고
    • The ParA/MinD family puts things in their place
    • Lutkenhaus J. 2012. The ParA/MinD family puts things in their place. Trends Microbiol 20:411-418.
    • (2012) Trends Microbiol , vol.20 , pp. 411-418
    • Lutkenhaus, J.1
  • 81
    • 84868026951 scopus 로고    scopus 로고
    • Surfing biological surfaces: exploiting the nucleoid for partition and transport in bacteria
    • Vecchiarelli AG, Mizuuchi K, Funnell BE. 2012. Surfing biological surfaces: exploiting the nucleoid for partition and transport in bacteria. Mol Microbiol 86:513-523.
    • (2012) Mol Microbiol , vol.86 , pp. 513-523
    • Vecchiarelli, A.G.1    Mizuuchi, K.2    Funnell, B.E.3
  • 82
    • 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 AL, 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
  • 83
    • 29144454213 scopus 로고    scopus 로고
    • Bacterial DNA segregation by dynamic SopA polymers
    • Lim GE, Derman AI, 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
  • 84
    • 1942468854 scopus 로고    scopus 로고
    • Bacterial mitosis: partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at midcell
    • Ebersbach G, Gerdes K. 2004. Bacterial mitosis: partitioning protein ParA oscillates in spiral-shaped structures and positions plasmids at midcell. Mol Microbiol 52:385-398.
    • (2004) Mol Microbiol , vol.52 , pp. 385-398
    • Ebersbach, G.1    Gerdes, K.2
  • 85
    • 73349101910 scopus 로고    scopus 로고
    • Movement and equipositioning of plasmids by ParA filament disassembly
    • Ringgaard S, van Zon J, Howard M, Gerdes K. 2009. Movement and equipositioning of plasmids by ParA filament disassembly. Proc Natl Acad Sci USA 106:19369-19374.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 19369-19374
    • Ringgaard, S.1    van Zon, J.2    Howard, M.3    Gerdes, K.4
  • 86
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin DM, de Boer PAJ. 1999. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc Natl Acad Sci USA 96:4971-4976.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.J.2
  • 88
    • 84855867420 scopus 로고    scopus 로고
    • ATP-regulated interactions between P1 ParA, ParB and non-specific DNA that are stabilized by the plasmid partition site, parS
    • Havey JC, Vecchiarelli AG, Funnell BE. 2012. ATP-regulated interactions between P1 ParA, ParB and non-specific DNA that are stabilized by the plasmid partition site, parS. Nucleic Acids Res 40:801-812.
    • (2012) Nucleic Acids Res , vol.40 , pp. 801-812
    • Havey, J.C.1    Vecchiarelli, A.G.2    Funnell, B.E.3
  • 89
    • 84879045680 scopus 로고    scopus 로고
    • Dissection of the ATPase active site of P1 ParA reveals multiple active forms essential for plasmid partition
    • Vecchiarelli AG, Havey JC, Ing LL, Wong EOY, Waples WG, Funnell BE. 2013. Dissection of the ATPase active site of P1 ParA reveals multiple active forms essential for plasmid partition. J Biol Chem 288:17823-17831.
    • (2013) J Biol Chem , vol.288 , pp. 17823-17831
    • Vecchiarelli, A.G.1    Havey, J.C.2    Ing, L.L.3    Wong, E.O.Y.4    Waples, W.G.5    Funnell, B.E.6
  • 90
    • 84876063388 scopus 로고    scopus 로고
    • Cell-free study of F plasmid partition provides evidence for cargo transport by a diffusionratchet mechanism
    • Vecchiarelli AG, Hwang LC, Mizuuchi K. 2013. Cell-free study of F plasmid partition provides evidence for cargo transport by a diffusionratchet mechanism. Proc Natl Acad Sci USA 110:E1390-E1397.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. E1390-E1397
    • Vecchiarelli, A.G.1    Hwang, L.C.2    Mizuuchi, K.3
  • 92
    • 54249093366 scopus 로고    scopus 로고
    • F plasmid partition depends on interaction of SopA with non-specific DNA
    • Castaing J-P, Bouet J-Y, Lane D. 2008. F plasmid partition depends on interaction of SopA with non-specific DNA. Mol Microbiol 70:1000-1011.
    • (2008) Mol Microbiol , vol.70 , pp. 1000-1011
    • Castaing, J.-P.1    Bouet, J.-Y.2    Lane, D.3
  • 93
    • 33846081941 scopus 로고    scopus 로고
    • Polymerization of SopA partition ATPase: regulation by DNA binding and SopB
    • Bouet J-Y, Ah-Seng Y, Benmeradi N, Lane D. 2007. Polymerization of SopA partition ATPase: regulation by DNA binding and SopB. Mol Microbiol 63:468-481.
    • (2007) Mol Microbiol , vol.63 , pp. 468-481
    • Bouet, J.-Y.1    Ah-Seng, Y.2    Benmeradi, N.3    Lane, D.4
  • 94
    • 35349020414 scopus 로고    scopus 로고
    • Promiscuous stimulation of ParF protein polymerization by heterogeneous centromere binding factors
    • Machon C, Fothergill TJG, Barillà D, Hayes F. 2007. Promiscuous stimulation of ParF protein polymerization by heterogeneous centromere binding factors. J Mol Biol 374:1-8.
    • (2007) J Mol Biol , vol.374 , pp. 1-8
    • Machon, C.1    Fothergill, T.J.G.2    Barillà, D.3    Hayes, F.4
  • 95
    • 17844403033 scopus 로고    scopus 로고
    • Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
    • Barillà D, Rosenberg MF, Nobbmann U, 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
    • Barillà, D.1    Rosenberg, M.F.2    Nobbmann, U.3    Hayes, F.4
  • 96
    • 79954599462 scopus 로고    scopus 로고
    • Molecular anatomy of the Streptococcus pyogenes pSM19035 partition and segrosome complexes
    • Soberón NE, Lioy VS, Pratto F, Volante A, Alonso JC. 2011. Molecular anatomy of the Streptococcus pyogenes pSM19035 partition and segrosome complexes. Nucleic Acids Res 39:2624-2637.
    • (2011) Nucleic Acids Res , vol.39 , pp. 2624-2637
    • Soberón, N.E.1    Lioy, V.S.2    Pratto, F.3    Volante, A.4    Alonso, J.C.5
  • 97
    • 67649562300 scopus 로고    scopus 로고
    • Structural basis for ADP-mediated transcriptional regulation by P1 and P7 ParA
    • Dunham TD, Xu W, Funnell BE, Schumacher MA. 2009. Structural basis for ADP-mediated transcriptional regulation by P1 and P7 ParA. EMBO J 28:1792-1802.
    • (2009) EMBO J , vol.28 , pp. 1792-1802
    • Dunham, T.D.1    Xu, W.2    Funnell, B.E.3    Schumacher, M.A.4
  • 98
    • 84864394575 scopus 로고    scopus 로고
    • Structural mechanism of ATP-induced polymerization of the partition factor ParF
    • Schumacher MA, Ye QZ, Barge MT, Zampini M, Barilla D, Hayes F. 2012. Structural mechanism of ATP-induced polymerization of the partition factor ParF. J Biol Chem 287:26146-26154.
    • (2012) J Biol Chem , vol.287 , pp. 26146-26154
    • Schumacher, M.A.1    Ye, Q.Z.2    Barge, M.T.3    Zampini, M.4    Barilla, D.5    Hayes, F.6
  • 99
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: application to microtubules and the ribosome
    • Baker N, Sept D, Joseph S, Holst M, McCammon J. 2001. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98:10037-10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.1    Sept, D.2    Joseph, S.3    Holst, M.4    McCammon, J.5
  • 100
    • 0026585678 scopus 로고
    • Biochemical activities of the ParA partition protein of the P1 plasmid
    • Davis MA, Martin KA, Austin SJ. 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
  • 101
    • 0026758465 scopus 로고
    • ATPase activity of SopA, a protein essential for active partitioning of F-plasmid
    • Watanabe E, Wachi M, Yamasaki M, 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
  • 102
    • 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 DJ, 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
  • 103
    • 79961135028 scopus 로고    scopus 로고
    • The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis
    • Park K-T, Wu W, Battaile Kevin P, Lovell S, Holyoak T, Lutkenhaus J. 2011. The Min oscillator uses MinD-dependent conformational changes in MinE to spatially regulate cytokinesis. Cell 146:396-407.
    • (2011) Cell , vol.146 , pp. 396-407
    • Park, K.-T.1    Wu, W.2    Battaile Kevin, P.3    Lovell, S.4    Holyoak, T.5    Lutkenhaus, J.6
  • 104
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: structure and DNA binding of the Soj dimer: a conserved biological switch
    • Leonard TA, Butler PJ, 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
  • 105
    • 79952450528 scopus 로고    scopus 로고
    • Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC
    • Wu W, Park K-T, Holyoak T, Lutkenhaus J. 2011. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol Microbiol 79:1515-1528.
    • (2011) Mol Microbiol , vol.79 , pp. 1515-1528
    • Wu, W.1    Park, K.-T.2    Holyoak, T.3    Lutkenhaus, J.4
  • 106
    • 0030919148 scopus 로고    scopus 로고
    • Modulation of the P1 plasmid partition protein ParA by ATP, ADP and P1 ParB
    • Davey MJ, Funnell BE. 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
  • 107
    • 38049165679 scopus 로고    scopus 로고
    • Soj (ParA) DNA binding is mediated by conserved arginines and is essential for plasmid segregation
    • Hester CM, Lutkenhaus J. 2007. Soj (ParA) DNA binding is mediated by conserved arginines and is essential for plasmid segregation. Proc Natl Acad Sci USA 104:20326-20331.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20326-20331
    • Hester, C.M.1    Lutkenhaus, J.2
  • 108
    • 58549109035 scopus 로고    scopus 로고
    • Bacterial genome partitioning: N-terminal domain of IncC protein encoded by broad-host-range plasmid RK2 modulates oligomerisation and DNA binding
    • Batt SM, Bingle LEH, Dafforn TR, Thomas CM. 2009. Bacterial genome partitioning: N-terminal domain of IncC protein encoded by broad-host-range plasmid RK2 modulates oligomerisation and DNA binding. J Mol Biol 385:1361-1374.
    • (2009) J Mol Biol , vol.385 , pp. 1361-1374
    • Batt, S.M.1    Bingle, L.E.H.2    Dafforn, T.R.3    Thomas, C.M.4
  • 109
    • 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, Funnell BE. 1999. P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities. EMBOJ 18:1415-1424.
    • (1999) EMBOJ , vol.18 , pp. 1415-1424
    • Bouet, J.-Y.1    Funnell, B.E.2
  • 110
    • 0034808020 scopus 로고    scopus 로고
    • The three-dimensional structure of septumsite-determining proteinMinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP
    • Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I. 2001. The three-dimensional structure of septumsite-determining proteinMinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP. Structure 9:817-826.
    • (2001) Structure , vol.9 , pp. 817-826
    • Sakai, N.1    Yao, M.2    Itou, H.3    Watanabe, N.4    Yumoto, F.5    Tanokura, M.6    Tanaka, I.7
  • 111
    • 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, 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
  • 113
    • 0027944755 scopus 로고
    • The P1 plasmid partition protein ParA. A role for ATP in site-specific DNA binding
    • Davey MJ, Funnell BE. 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
  • 114
    • 0035801498 scopus 로고    scopus 로고
    • Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis
    • Fung E, Bouet J-Y, Funnell BE. 2001. Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis. EMBO J 20:4901-4911.
    • (2001) EMBO J , vol.20 , pp. 4901-4911
    • Fung, E.1    Bouet, J.-Y.2    Funnell, B.E.3
  • 115
    • 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, 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
  • 116
    • 0035976748 scopus 로고    scopus 로고
    • Role of the ATP-binding site of SopA protein in partition of the F plasmid
    • Libante V, Thion L, 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
  • 118
    • 0242268448 scopus 로고    scopus 로고
    • Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones
    • Huang KC, Meir Y, Wingreen NS. 2003. Dynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zones. Proc Natl Acad Sci USA 100:12724-12728.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12724-12728
    • Huang, K.C.1    Meir, Y.2    Wingreen, N.S.3
  • 119
    • 82555165967 scopus 로고    scopus 로고
    • ParA ATPases canmove and position DNA and subcellular structures
    • Szardenings F, Guymer D, Gerdes K. 2011. ParA ATPases canmove and position DNA and subcellular structures. Curr Opin Microbiol 14:712-718.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 712-718
    • Szardenings, F.1    Guymer, D.2    Gerdes, K.3
  • 120
    • 84877594627 scopus 로고    scopus 로고
    • Plasmid partition: sisters drifting apart
    • Sherratt D. 2013. Plasmid partition: sisters drifting apart. EMBO J 32:1208-1210.
    • (2013) EMBO J , vol.32 , pp. 1208-1210
    • Sherratt, D.1
  • 121
    • 79960401024 scopus 로고    scopus 로고
    • A family of ParA-like ATPases promotes cell pole maturation by facilitating polar localization of chemotaxis proteins
    • Ringgaard S, Schirner K, Davis BM, Waldor MK. 2011. A family of ParA-like ATPases promotes cell pole maturation by facilitating polar localization of chemotaxis proteins. Genes Dev 25:1544-1555.
    • (2011) Genes Dev , vol.25 , pp. 1544-1555
    • Ringgaard, S.1    Schirner, K.2    Davis, B.M.3    Waldor, M.K.4
  • 123
    • 65249182459 scopus 로고    scopus 로고
    • The tubulin-like RepX protein encoded by the pXO1 plasmid forms polymers in vivo in Bacillus anthracis
    • Akhtar P, Anand SP, Watkins SC, Khan SA. 2009. The tubulin-like RepX protein encoded by the pXO1 plasmid forms polymers in vivo in Bacillus anthracis. J Bacteriol 191:2493-2500.
    • (2009) J Bacteriol , vol.191 , pp. 2493-2500
    • Akhtar, P.1    Anand, S.P.2    Watkins, S.C.3    Khan, S.A.4
  • 124
    • 36549026935 scopus 로고    scopus 로고
    • Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis
    • Tang M, Bideshi DK, Park H-W, Federici BA. 2007. Iteron-binding ORF157 and FtsZ-like ORF156 proteins encoded by pBtoxis play a role in its replication in Bacillus thuringiensis subsp. israelensis. J Bacteriol 189:8053-8058.
    • (2007) J Bacteriol , vol.189 , pp. 8053-8058
    • Tang, M.1    Bideshi, D.K.2    Park, H.-W.3    Federici, B.A.4
  • 125
    • 77955395804 scopus 로고    scopus 로고
    • Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition
    • Ni LS, Xu WJ, Kumaraswami M, Schumacher MA. 2010. Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition. Proc Natl Acad Sci USA 107:11763-11768.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11763-11768
    • Ni, L.S.1    Xu, W.J.2    Kumaraswami, M.3    Schumacher, M.A.4
  • 126
    • 43549088354 scopus 로고    scopus 로고
    • In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism
    • Chen YD, Erickson HP. 2008. In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism. J Biol Chem 283:8102-8109.
    • (2008) J Biol Chem , vol.283 , pp. 8102-8109
    • Chen, Y.D.1    Erickson, H.P.2
  • 128
    • 84866397940 scopus 로고    scopus 로고
    • Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid
    • Hoshino S, Hayashi I. 2012. Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid. J Biol Chem 287:32103-32112.
    • (2012) J Biol Chem , vol.287 , pp. 32103-32112
    • Hoshino, S.1    Hayashi, I.2
  • 129
    • 84867365232 scopus 로고    scopus 로고
    • Superstructure of the centromeric complex of TubZRC plasmid partitioning systems
    • Aylett CHS, Lowe J. 2012. Superstructure of the centromeric complex of TubZRC plasmid partitioning systems. Proc Natl Acad Sci USA 109:16522-16527.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 16522-16527
    • Aylett, C.H.S.1    Lowe, J.2
  • 130
    • 84892725835 scopus 로고    scopus 로고
    • Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids
    • Ah-Seng Y, Rech J, Lane D, Bouet JY. 2013. Defining the role of ATP hydrolysis in mitotic segregation of bacterial plasmids. PLoS Genet 9:e1003956. doi:10.1371/journal.pgen.1003956.
    • (2013) PLoS Genet , vol.9
    • Ah-Seng, Y.1    Rech, J.2    Lane, D.3    Bouet, J.Y.4
  • 131
  • 132
    • 84871006430 scopus 로고    scopus 로고
    • Variation of the folding and dynamics of the Escherichia coli chromosome with growth conditions
    • Hadizadeh Yazdi N, Guet CC, Johnson RC, Marko JF. 2012. Variation of the folding and dynamics of the Escherichia coli chromosome with growth conditions. Mol Microbiol 86:1318-1333.
    • (2012) Mol Microbiol , vol.86 , pp. 1318-1333
    • Hadizadeh Yazdi, N.1    Guet, C.C.2    Johnson, R.C.3    Marko, J.F.4
  • 133
    • 84877694848 scopus 로고    scopus 로고
    • Four-dimensional imaging of E. coli nucleoid organization and dynamics in living cells
    • Fisher JK, Bourniquel A, Witz G, Weiner B, Prentiss M, Kleckner N. 2013. Four-dimensional imaging of E. coli nucleoid organization and dynamics in living cells. Cell 153:882-895.
    • (2013) Cell , vol.153 , pp. 882-895
    • Fisher, J.K.1    Bourniquel, A.2    Witz, G.3    Weiner, B.4    Prentiss, M.5    Kleckner, N.6


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