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Volumn 397, Issue 4, 2010, Pages 1031-1041

Polymeric structures and dynamic properties of the bacterial actin AlfA

Author keywords

Actin homolog; AlfA; Electron microscopy; Helical symmetry; Treadmilling

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; F ACTIN; GUANOSINE TRIPHOSPHATE; MREB PROTEIN; PROTEIN ALFA; PROTEIN PARM; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 77950020896     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.010     Document Type: Article
Times cited : (29)

References (29)
  • 1
    • 0021798253 scopus 로고
    • Buffer capacity of bacilli that grow at different pH ranges
    • Krulwich T.A., Agus R., Schneier M., Guffanti A.A. Buffer capacity of bacilli that grow at different pH ranges. J. Bacteriol. 1985, 162:768-772.
    • (1985) J. Bacteriol. , vol.162 , pp. 768-772
    • Krulwich, T.A.1    Agus, R.2    Schneier, M.3    Guffanti, A.A.4
  • 2
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo
    • Cayley S., Lewis B.A., Guttman H.J., Record M.T. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo. J. Mol. Biol. 1991, 222:281-300.
    • (1991) J. Mol. Biol. , vol.222 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record, M.T.4
  • 4
    • 0028224273 scopus 로고
    • The internal pH of the forespore compartment of Bacillus magaterium decreases by about 1 pH unit during sporulation
    • MacGill N.G., Cowan A.E., Koppel D.E., Setlow P. The internal pH of the forespore compartment of Bacillus magaterium decreases by about 1 pH unit during sporulation. J. Bacteriol. 1994, 176:2252-2258.
    • (1994) J. Bacteriol. , vol.176 , pp. 2252-2258
    • MacGill, N.G.1    Cowan, A.E.2    Koppel, D.E.3    Setlow, P.4
  • 5
    • 33845772164 scopus 로고    scopus 로고
    • DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development
    • Becker E., Herrera N.C., Gunderson F.Q., Derman A.I., Dance A.L., Sims J., et al. DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development. EMBO J. 2006, 25:5919-5931.
    • (2006) EMBO J. , vol.25 , pp. 5919-5931
    • Becker, E.1    Herrera, N.C.2    Gunderson, F.Q.3    Derman, A.I.4    Dance, A.L.5    Sims, J.6
  • 7
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones L.J., Carballido-López R., Errington J. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 2001, 104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-López, R.2    Errington, J.3
  • 8
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Møller-Jensen J., Jensen R.B., Löwe J., Gerdes K. Prokaryotic DNA segregation by an actin-like filament. EMBO J. 2002, 21:6935-6943.
    • (2002) EMBO J. , vol.21 , pp. 6935-6943
    • Møller-Jensen, J.1    Jensen, R.B.2    Löwe, J.3    Gerdes, K.4
  • 9
    • 38849114991 scopus 로고    scopus 로고
    • Polymerization properties of the Thermatoga maritima actin MreB: roles of temperature, nucleotides and ions
    • Bean G.J., Amann K.J. Polymerization properties of the Thermatoga maritima actin MreB: roles of temperature, nucleotides and ions. Biochemistry 2008, 47:826-835.
    • (2008) Biochemistry , vol.47 , pp. 826-835
    • Bean, G.J.1    Amann, K.J.2
  • 10
    • 11244348910 scopus 로고    scopus 로고
    • A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus
    • Chen Y., Bjornson K., Redick S.D., Erickson H.P. A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus. Biophys. J. 2005, 88:505-514.
    • (2005) Biophys. J. , vol.88 , pp. 505-514
    • Chen, Y.1    Bjornson, K.2    Redick, S.D.3    Erickson, H.P.4
  • 11
    • 38949129203 scopus 로고    scopus 로고
    • Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability
    • Popp D., Narita A., Oda T., Fujisawa T., Matsuo H., Nitanai Y., et al. Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability. EMBO J. 2008, 27:570-579.
    • (2008) EMBO J. , vol.27 , pp. 570-579
    • Popp, D.1    Narita, A.2    Oda, T.3    Fujisawa, T.4    Matsuo, H.5    Nitanai, Y.6
  • 12
    • 0025970527 scopus 로고
    • Actin: protein structure and filament dynamics
    • Carlier M.F. Actin: protein structure and filament dynamics. J. Biol. Chem. 1991, 266:1-4.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1-4
    • Carlier, M.F.1
  • 13
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb M.R. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl Acad. Sci. 1992, 89:4884-4887.
    • (1992) Proc. Natl Acad. Sci. , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 14
    • 51049096605 scopus 로고    scopus 로고
    • Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle α-actin mutants
    • Iwasa M., Maeda K., Narita A., Maeda Y., Oda T. Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle α-actin mutants. J. Biol. Chem. 2008, 238:21045-21053.
    • (2008) J. Biol. Chem. , vol.238 , pp. 21045-21053
    • Iwasa, M.1    Maeda, K.2    Narita, A.3    Maeda, Y.4    Oda, T.5
  • 15
    • 0036713779 scopus 로고    scopus 로고
    • Microscopic analysis of polymerization dynamics with individual actin filaments
    • Fujiwara I., Takahashi S., Tadakuma H., Funatsu T., Ishiwata S. Microscopic analysis of polymerization dynamics with individual actin filaments. Nat. Cell Biol. 2002, 4:666-673.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 666-673
    • Fujiwara, I.1    Takahashi, S.2    Tadakuma, H.3    Funatsu, T.4    Ishiwata, S.5
  • 16
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomotive cells
    • Theriot J.A., Mitchison T.J. Actin microfilament dynamics in locomotive cells. Nature 1991, 352:126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 19
    • 0020625408 scopus 로고
    • Kinetic evidence for a monomer activation step in actin polymerization
    • Cooper J.A., Buhle E.L., Walker S.B., Tsong T.Y., Pollard T.D. Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry 1983, 22:2193-2202.
    • (1983) Biochemistry , vol.22 , pp. 2193-2202
    • Cooper, J.A.1    Buhle, E.L.2    Walker, S.B.3    Tsong, T.Y.4    Pollard, T.D.5
  • 20
    • 69849097861 scopus 로고    scopus 로고
    • The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation
    • Polka L., Kollman J.M., Agard D.A., Mullins R.D. The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation. J. Bacteriol. 2009, 191:6219-6230.
    • (2009) J. Bacteriol. , vol.191 , pp. 6219-6230
    • Polka, L.1    Kollman, J.M.2    Agard, D.A.3    Mullins, R.D.4
  • 22
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • Van den Ent F., Amos L.A., Löwe J. Prokaryotic origin of the actin cytoskeleton. Nature 2001, 413:39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van den Ent, F.1    Amos, L.A.2    Löwe, J.3
  • 23
    • 77950022048 scopus 로고    scopus 로고
    • Polymorphic perversity in protein polymers
    • Egelman E.H. Polymorphic perversity in protein polymers. FASEB J. 2008, 22:537.3.
    • (2008) FASEB J. , vol.22
    • Egelman, E.H.1
  • 24
    • 49649092897 scopus 로고    scopus 로고
    • Effect of short-range forces on the length distribution of cytoskeletal proteins
    • Popp D., Gov N.S., Iwasa M., Maeda Y. Effect of short-range forces on the length distribution of cytoskeletal proteins. Biopolymers 2008, 89:711-721.
    • (2008) Biopolymers , vol.89 , pp. 711-721
    • Popp, D.1    Gov, N.S.2    Iwasa, M.3    Maeda, Y.4
  • 25
    • 0016233229 scopus 로고
    • The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphate reaction
    • Bagshaw C., Trentham D. The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphate reaction. Biochem. J. 1973, 141:331-349.
    • (1973) Biochem. J. , vol.141 , pp. 331-349
    • Bagshaw, C.1    Trentham, D.2
  • 26
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: applications to the HIV proteinase
    • Kuzmic P. Program DYNAFIT for the analysis of enzyme kinetic data: applications to the HIV proteinase. Ann. Biochem. 1996, 237:260-273.
    • (1996) Ann. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 27
    • 0029881549 scopus 로고    scopus 로고
    • Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules
    • Yasunaga T., Wakabayashi T. Extensible and object-oriented system Eos supplies a new environment for image analysis of electron micrographs of macromolecules. J. Struct. Biol. 1996, 116:155-160.
    • (1996) J. Struct. Biol. , vol.116 , pp. 155-160
    • Yasunaga, T.1    Wakabayashi, T.2
  • 28
    • 19144368653 scopus 로고    scopus 로고
    • Improvement of a high pressure cell with diamond windows for solution X-ray scattering of proteins
    • Nishikawa Y., Fujisawa T., Inoko Y., Moritoki M. Improvement of a high pressure cell with diamond windows for solution X-ray scattering of proteins. Nucl. Instrum. Methods Phys. Res. Sect. A 2001, 467:1384-1387.
    • (2001) Nucl. Instrum. Methods Phys. Res. Sect. A , vol.467 , pp. 1384-1387
    • Nishikawa, Y.1    Fujisawa, T.2    Inoko, Y.3    Moritoki, M.4
  • 29
    • 38949144961 scopus 로고    scopus 로고
    • Structural studies on protein solutions by using solution X-ray scattering technique at RIKEN structural biology beamline I (BL45XU)
    • Fujisawa T. Structural studies on protein solutions by using solution X-ray scattering technique at RIKEN structural biology beamline I (BL45XU). J. Crystallogr. Soc. Jpn. 2000, 42:97-105.
    • (2000) J. Crystallogr. Soc. Jpn. , vol.42 , pp. 97-105
    • Fujisawa, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.