메뉴 건너뛰기




Volumn 80, Issue 2, 2011, Pages 300-308

Many ways to build an actin filament

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALPHA ACTIN; F ACTIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; MREB PROTEIN;

EID: 79954414615     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07599.x     Document Type: Review
Times cited : (20)

References (54)
  • 1
    • 38449116591 scopus 로고    scopus 로고
    • GTP-dependent polymerization of the tubulin-like RepX replication protein encoded by the pXO1 plasmid of Bacillus anthracis
    • Anand, S.P., Akhtar, P., Tinsley, E., Watkins, S.C., and Khan, S.A. (2008) GTP-dependent polymerization of the tubulin-like RepX replication protein encoded by the pXO1 plasmid of Bacillus anthracis. Mol Microbiol 67: 881-890.
    • (2008) Mol Microbiol , vol.67 , pp. 881-890
    • Anand, S.P.1    Akhtar, P.2    Tinsley, E.3    Watkins, S.C.4    Khan, S.A.5
  • 2
    • 38849114991 scopus 로고    scopus 로고
    • Polymerization properties of the Thermatoga maritime actin MreB: roles of temperature, nucleotides and ions
    • Bean, G.J., and Amann, K. (2008) Polymerization properties of the Thermatoga maritime actin MreB: roles of temperature, nucleotides and ions. Biochemistry 47: 826-835.
    • (2008) Biochemistry , vol.47 , pp. 826-835
    • Bean, G.J.1    Amann, K.2
  • 3
    • 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., etal. (2006) DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development. EMBO J 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
  • 4
    • 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
  • 5
    • 0033565651 scopus 로고    scopus 로고
    • Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 colocalizes with its replicon during the cell cycle
    • Bugge-Jensen, R., and Gerdes, K. (1999) Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 colocalizes with its replicon during the cell cycle. EMBO J 18: 4076-4084.
    • (1999) EMBO J , vol.18 , pp. 4076-4084
    • Bugge-Jensen, R.1    Gerdes, K.2
  • 6
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF
    • Burtnick, L.D., Urosev, D., Irobi, E., Narayan, K., and Robinson, R.C. (2004) Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF. EMBO J 23: 2713-2722.
    • (2004) EMBO J , vol.23 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 8
    • 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., and Record, M.T. (1991) 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 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
  • 9
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel, R.A., and Errington, J. (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113: 767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 10
    • 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, A.I., Becker, E.C., Truong, B.D., Fujioka, A., Tucey, T.M., Erb, M.L., etal. (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
  • 11
    • 77950022048 scopus 로고    scopus 로고
    • Polymorphic perversity in protein polymers
    • Egelman, E.H. (2008) Polymorphic perversity in protein polymers. FASEB J 22: 537.3.
    • (2008) FASEB J , vol.22 , pp. 5373
    • Egelman, E.H.1
  • 12
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman, E.H., Francis, N., and DeRosier, D.J. (1982) F-actin is a helix with a random variable twist. Nature 298: 131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 13
    • 31344480941 scopus 로고    scopus 로고
    • GTPase activity, structure and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB
    • Esue, O., Wirtz, D., and Tseng, Y. (2006) GTPase activity, structure and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB. J Bacteriol 188: 968-976.
    • (2006) J Bacteriol , vol.188 , pp. 968-976
    • Esue, O.1    Wirtz, D.2    Tseng, Y.3
  • 14
    • 69849107000 scopus 로고    scopus 로고
    • Structural polymorphism of the ParM filament and dynamic instability
    • Galkin, V.E., Orlova, A., Rivera, C., Mullins, R.D., and Egelman E.H. (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
  • 15
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner, E.C., Cambell, 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    Cambell, C.S.2    Mullins, R.D.3
  • 16
    • 33847675333 scopus 로고    scopus 로고
    • Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homolog
    • Garner, E.C., Cambell, C.S., Weibel, D.B., and Mullins, R.D. (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    Cambell, C.S.2    Weibel, D.B.3    Mullins, R.D.4
  • 17
    • 77953724552 scopus 로고    scopus 로고
    • Pushing and pulling in DNA segregation
    • Gerdes, K., Howard, M., and Szardenings, F. (2010) Pushing and pulling in DNA segregation. Cell 141: 927-942.
    • (2010) Cell , vol.141 , pp. 927-942
    • Gerdes, K.1    Howard, M.2    Szardenings, F.3
  • 18
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes, K.C., Popp, D., Gebhard, W., and Kabsch, W. (1990) Atomic model of the actin filament. Nature 347: 44-49.
    • (1990) Nature , vol.347 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 19
    • 63449131009 scopus 로고    scopus 로고
    • Continued protein synthesis at low [ATP] and [GTP] enables cell adaptation during energy limitation
    • Jewett, M.C., Miller, M.L., Chen, Y., and Swartz, J.R. (2009) Continued protein synthesis at low [ATP] and [GTP] enables cell adaptation during energy limitation. J Bacteriol 191: 1083-1091.
    • (2009) J Bacteriol , vol.191 , pp. 1083-1091
    • Jewett, M.C.1    Miller, M.L.2    Chen, Y.3    Swartz, J.R.4
  • 20
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones, L.J., Carballido-Lopez, R., and Errington, J. (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104: 913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 21
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch, W., and Holmes, K.C. (1995) The actin fold. FASEB J 9: 167-174.
    • (1995) FASEB J , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 23
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • Kim, S.Y., Gitai, Z., Kinkhabwala, A., Shapiro, L., and Moerner, W.E. (2006) Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc Natl Acad Sci USA 103: 10929-10934.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10929-10934
    • Kim, S.Y.1    Gitai, Z.2    Kinkhabwala, A.3    Shapiro, L.4    Moerner, W.E.5
  • 24
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • Kueh, H.Y., and Mitchison, T.J. (2009) Structural plasticity in actin and tubulin polymer dynamics. Science 325: 960-963.
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 25
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li, Z., Trimble, M.J., Brun, Y.V., and Jensen, G.J. (2007) The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26: 4694-4708.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 26
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe, J., and Amos, L.A. (1998) Crystal structure of the bacterial cell-division protein FtsZ. Nature 391: 203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 28
    • 0031787749 scopus 로고    scopus 로고
    • Counterion condensation revisted
    • Manning, G.S., and Ray, J. (1998) Counterion condensation revisted. J Biomol Struct Dyn 16: 461-476.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 461-476
    • Manning, G.S.1    Ray, J.2
  • 29
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton, A.P. (2000) Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 10: 34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 30
    • 25444487734 scopus 로고    scopus 로고
    • Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations
    • Minton, A.P. (2005) Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations. J Pharm Sci 94: 1668-1675.
    • (2005) J Pharm Sci , vol.94 , pp. 1668-1675
    • Minton, A.P.1
  • 31
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison, T., and Kirschner, M. (1984) Dynamic instability of microtubule growth. Nature 312: 237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 32
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Møller-Jensen, J., Jensen, R.B., Löwe, 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
    • Møller-Jensen, J.1    Jensen, R.B.2    Löwe, J.3    Gerdes, K.4
  • 35
    • 0031795574 scopus 로고    scopus 로고
    • Effect of length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by X-ray fiber diffraction
    • Oda, T., Makino, K., Yamashita, I., Namba, K., and Maeda, Y. (1998) Effect of length and effective diameter of F-actin on the filament orientation in liquid crystalline sols measured by X-ray fiber diffraction. Biophys J 75: 2672-2681.
    • (1998) Biophys J , vol.75 , pp. 2672-2681
    • Oda, T.1    Makino, K.2    Yamashita, I.3    Namba, K.4    Maeda, Y.5
  • 36
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular-to fibrous-actin transition. -
    • Oda, T., Iwasa, M., Aihara, T., Maeda, Y., and Narita, A. (2009) The nature of the globular-to fibrous-actin transition. 457: 441-445.
    • (2009) , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maeda, Y.4    Narita, A.5
  • 38
    • 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., and Mullins, R.D. (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, L.1    Kollman, J.M.2    Agard, D.A.3    Mullins, R.D.4
  • 40
    • 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., Matsui, H., Nitanai, Y., etal. (2008a) Molecular Structure of the ParM Polymer and the Mechanism Leading to its Nucleotide Driven Dynamic Instability. EMBO J 27: 570-579.
    • (2008) EMBO J , vol.27 , pp. 570-579
    • Popp, D.1    Narita, A.2    Oda, T.3    Fujisawa, T.4    Matsui, H.5    Nitanai, Y.6
  • 41
    • 49649092897 scopus 로고    scopus 로고
    • Effect of short-range forces on the length distribution of fibrous cytoskeletal proteins
    • Popp, D., Gov, N.S., Iwasa, M., and Maeda, Y. (2008b) Effect of short-range forces on the length distribution of fibrous cytoskeletal proteins. Biopolymers 89: 711-721.
    • (2008) Biopolymers , vol.89 , pp. 711-721
    • Popp, D.1    Gov, N.S.2    Iwasa, M.3    Maeda, Y.4
  • 43
    • 77950020896 scopus 로고    scopus 로고
    • Polymeric structures and dynamic properties of the bacterial actin AlfA
    • Popp, D., Narita, A., Ghoshdastider, U., Maeda, K., Maéda, Y., Oda, T., etal. (2010a) Polymeric structures and dynamic properties of the bacterial actin AlfA. J Mol Biol 397: 1031-1041.
    • (2010) J Mol Biol , vol.397 , pp. 1031-1041
    • Popp, D.1    Narita, A.2    Ghoshdastider, U.3    Maeda, K.4    Maéda, Y.5    Oda, T.6
  • 44
    • 77951220899 scopus 로고    scopus 로고
    • Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation
    • Popp, D., Xu, W., Narita, A., Brzoska, A.J., Skurray, R.A., Firth, N., etal. (2010b) Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation. J Biol Chem 285: 10130-10140.
    • (2010) J Biol Chem , vol.285 , pp. 10130-10140
    • Popp, D.1    Xu, W.2    Narita, A.3    Brzoska, A.J.4    Skurray, R.A.5    Firth, N.6
  • 47
    • 58849121358 scopus 로고    scopus 로고
    • Electron microscopy of E. coli reveals filament bundles involved in plasmid DNA segregation
    • Salje, J., Zuber, B., and Löwe, J. (2009) Electron microscopy 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    Löwe, J.3
  • 48
    • 0017102423 scopus 로고
    • 1,4-Diaminobutane (putrescine), spermidine, and spermine
    • Tabor, C.W., and Tabor, H. (1976) 1, 4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem 45: 285-306.
    • (1976) Annu Rev Biochem , vol.45 , pp. 285-306
    • Tabor, C.W.1    Tabor, H.2
  • 49
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor, C.W., and Tabor, H. (1985) Polyamines in microorganisms. Microbiol Rev 49: 81-89.
    • (1985) Microbiol Rev , vol.49 , pp. 81-89
    • Tabor, C.W.1    Tabor, H.2
  • 50
    • 0030845631 scopus 로고    scopus 로고
    • Opposite effects of electrostatic and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes
    • Tang, J.X., Tao, T., Traub, P., and Janmey, P.A. (1997) Opposite effects of electrostatic and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes. Biochemistry 36: 12600-126007.
    • (1997) Biochemistry , vol.36 , pp. 12600-126007
    • Tang, J.X.1    Tao, T.2    Traub, P.3    Janmey, P.A.4
  • 51
    • 0018961098 scopus 로고
    • In vivo energetics and control of nitrogen fixation: changes in the adenylate energy charge and adensosine 5'-diphosphate/adenosine 5'-triphosphate ratios of cells during growth on dinitrogen versus growth on ammonia
    • Upchurch, R.G., and Mortenson, D.E. (1980) In vivo energetics and control of nitrogen fixation: changes in the adenylate energy charge and adensosine 5'-diphosphate/adenosine 5'-triphosphate ratios of cells during growth on dinitrogen versus growth on ammonia. J Bacteriol 143: 274-284.
    • (1980) J Bacteriol , vol.143 , pp. 274-284
    • Upchurch, R.G.1    Mortenson, D.E.2
  • 52
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • Van den Ent, F., Amos, L.A., and Löwe, 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    Löwe, J.3
  • 54
    • 77951687980 scopus 로고    scopus 로고
    • Electrostatics of strongly charged biological polymers: ion-mediated interactions and self-organization in nucleic acids and proteins
    • Wong, C.L., and Pollack, L. (2010) Electrostatics of strongly charged biological polymers: ion-mediated interactions and self-organization in nucleic acids and proteins. Annu Rev Phys Chem 61: 171-189.
    • (2010) Annu Rev Phys Chem , vol.61 , pp. 171-189
    • Wong, C.L.1    Pollack, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.