메뉴 건너뛰기




Volumn 425, Issue 12, 2013, Pages 2164-2173

Structure of the Tubulin/FtsZ-like protein TubZ from pseudomonas bacteriophage ΦkZ

Author keywords

cytomotive; cytoskeletal; electron cryo microscopy; filamentous protein; X ray crystallography

Indexed keywords

BACTERIAL PROTEIN; TUBULIN; TUBZ PROTEIN; UNCLASSIFIED DRUG;

EID: 84878253286     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.03.019     Document Type: Article
Times cited : (28)

References (35)
  • 1
    • 0024475207 scopus 로고
    • High abundance of viruses found in aquatic environments
    • O. Bergh, K.Y. Børsheim, G. Bratbak, and M. Heldal High abundance of viruses found in aquatic environments Nature 340 1989 467 468
    • (1989) Nature , vol.340 , pp. 467-468
    • Bergh, O.1    Børsheim, K.Y.2    Bratbak, G.3    Heldal, M.4
  • 2
    • 56949093012 scopus 로고    scopus 로고
    • Evolution of cytomotive filaments: The cytoskeleton from prokaryotes to eukaryotes
    • J. Löwe, and L.A. Amos Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes Int. J. Biochem. Cell Biol. 41 2009 323 329
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 323-329
    • Löwe, J.1    Amos, L.A.2
  • 3
    • 80855156621 scopus 로고    scopus 로고
    • New insights into the mechanisms of cytomotive actin and tubulin filaments
    • C.H.S. Aylett, J. Löwe, and L.A. Amos New insights into the mechanisms of cytomotive actin and tubulin filaments Int. Rev. Cell Mol. Biol. 292 2011 1 71
    • (2011) Int. Rev. Cell Mol. Biol. , vol.292 , pp. 1-71
    • Aylett, C.H.S.1    Löwe, J.2    Amos, L.A.3
  • 4
    • 0021104934 scopus 로고
    • Partition of unit-copy miniplasmids to daughter cells. I. P1 and F miniplasmids contain discrete, interchangeable sequences sufficient to promote equipartition
    • S. Austin, and A. Abeles Partition of unit-copy miniplasmids to daughter cells. I. P1 and F miniplasmids contain discrete, interchangeable sequences sufficient to promote equipartition J. Mol. Biol. 169 1983 353 372
    • (1983) J. Mol. Biol. , vol.169 , pp. 353-372
    • Austin, S.1    Abeles, A.2
  • 6
    • 84862649347 scopus 로고    scopus 로고
    • A phage tubulin assembles dynamic filaments by an atypical mechanism to centre viral DNA within the host cell
    • J.A. Kraemer, M.L. Erb, C.A. Waddling, E.A. Montabana, E.A. Zehr, and H. Wang A phage tubulin assembles dynamic filaments by an atypical mechanism to centre viral DNA within the host cell Cell 149 2012 1488 1499
    • (2012) Cell , vol.149 , pp. 1488-1499
    • Kraemer, J.A.1    Erb, M.L.2    Waddling, C.A.3    Montabana, E.A.4    Zehr, E.A.5    Wang, H.6
  • 8
    • 33746358181 scopus 로고    scopus 로고
    • Dynamic filaments of the bacterial cytoskeleton
    • K.A. Michie, and J. Löwe Dynamic filaments of the bacterial cytoskeleton Annu. Rev. Biochem. 75 2006 467 492
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 467-492
    • Michie, K.A.1    Löwe, J.2
  • 9
    • 73349101910 scopus 로고    scopus 로고
    • Movement and equipositioning of plasmids by ParA filament disassembly
    • S. Ringgaard, J. van Zon, M. Howard, and K. Gerdes Movement and equipositioning of plasmids by ParA filament disassembly Proc. Natl Acad. Sci. USA 106 2009 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
  • 11
    • 34249897760 scopus 로고    scopus 로고
    • Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis
    • R.A. Larsen, C. Cusumano, A. Fujioka, G. Lim-Fong, P. Patterson, and J. Pogliano Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis J. Genes Dev. 21 2007 1340 1352
    • (2007) J. 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
  • 12
    • 43549088354 scopus 로고    scopus 로고
    • In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: Evidence for a capping mechanism
    • Y. Chen, and H.P. Erickson In vitro assembly studies of FtsZ/tubulin-like proteins (TubZ) from Bacillus plasmids: evidence for a capping mechanism J. Biol. Chem. 283 2008 8102 8109
    • (2008) J. Biol. Chem. , vol.283 , pp. 8102-8109
    • Chen, Y.1    Erickson, H.P.2
  • 13
    • 84866397940 scopus 로고    scopus 로고
    • Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid
    • S. Hoshino, and I. Hayashi Filament formation of the FtsZ/tubulin-like protein TubZ from the Bacillus cereus pXO1 plasmid J. Biol. Chem. 287 2012 32103 32112
    • (2012) J. Biol. Chem. , vol.287 , pp. 32103-32112
    • Hoshino, S.1    Hayashi, I.2
  • 15
    • 34848906889 scopus 로고    scopus 로고
    • "ΦKZ-like viruses", a proposed new genus of myovirus bacteriophages
    • V.N. Krylov, D.M. Dela Cruz, K. Hertveldt, and H.W. Ackermann "ΦKZ-like viruses", a proposed new genus of myovirus bacteriophages Arch. Virol. 152 2007 1955 1959
    • (2007) Arch. Virol. , vol.152 , pp. 1955-1959
    • Krylov, V.N.1    Dela Cruz, D.M.2    Hertveldt, K.3    Ackermann, H.W.4
  • 20
    • 84864494657 scopus 로고    scopus 로고
    • Mechanism of action of the cell-division inhibitor PC190723: Modulation of FtsZ assembly cooperativity
    • N.L. Elsen, J. Lu, G. Parthasarathy, J.C. Reid, S. Sharma, S.M. Soisson, and K.J. Lumb Mechanism of action of the cell-division inhibitor PC190723: modulation of FtsZ assembly cooperativity J. Am. Chem. Soc. 134 2012 12342 12345
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 12342-12345
    • Elsen, N.L.1    Lu, J.2    Parthasarathy, G.3    Reid, J.C.4    Sharma, S.5    Soisson, S.M.6    Lumb, K.J.7
  • 22
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha beta-tubulin at 3.5 Å resolution
    • J. Löwe, H. Li, K.H. Downing, and E. Nogales Refined structure of alpha beta-tubulin at 3.5 Å resolution J. Mol. Biol. 313 2001 1045 1057
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 23
    • 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
    • L. Ni, W. Xu, M. Kumaraswami, and M.A. Schumacher 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 2010 11763 11768
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11763-11768
    • Ni, L.1    Xu, W.2    Kumaraswami, M.3    Schumacher, M.A.4
  • 24
    • 84863341292 scopus 로고    scopus 로고
    • Restoring methicillin-resistant Staphylococcus aureus susceptibility to β-lactam antibiotics
    • C.M. Tan, A.G. Therien, J. Lu, S.H. Lee, A. Caron, and C.J. Gill Restoring methicillin-resistant Staphylococcus aureus susceptibility to β-lactam antibiotics Sci. Transl. Med. 4 2012 126ra35
    • (2012) Sci. Transl. Med. , vol.4
    • Tan, C.M.1    Therien, A.G.2    Lu, J.3    Lee, S.H.4    Caron, A.5    Gill, C.J.6
  • 26
    • 11844300427 scopus 로고    scopus 로고
    • Robotic nanolitre protein crystallisation at the MRC Laboratory of Molecular Biology
    • D. Stock, O. Perisic, and J. Löwe Robotic nanolitre protein crystallisation at the MRC Laboratory of Molecular Biology Prog. Biophys. Mol. Biol. 88 2004 311 327
    • (2004) Prog. Biophys. Mol. Biol. , vol.88 , pp. 311-327
    • Stock, D.1    Perisic, O.2    Löwe, J.3
  • 28
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • P. Evans Scaling and assessment of data quality Acta Crystallogr., Sect. D 62 2006 72 82
    • (2006) Acta Crystallogr., Sect. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr., Sect. D 50 1994 760 763
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 760-763
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr., Sect. D 53 1997 240 255
    • (1997) Acta Crystallogr., Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 34
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • L. Holm, and J. Park DaliLite workbench for protein structure comparison Bioinformatics 16 2000 566 567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 35
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.