메뉴 건너뛰기




Volumn 82, Issue 2, 2011, Pages 342-354

MamK, a bacterial actin, forms dynamic filaments in vivo that are regulated by the acidic proteins MamJ and LimJ

Author keywords

[No Author keywords available]

Indexed keywords

ACID PROTEIN; ACTIN; BACTERIAL PROTEIN; PROTEIN LIMJ; PROTEIN MAMJ; PROTEIN MAMK; UNCLASSIFIED DRUG;

EID: 80053944902     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07815.x     Document Type: Article
Times cited : (87)

References (48)
  • 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
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezú, F.O., Hale, C.A., Bernhardt, T.G., and de Boer, P.A. (2009) RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J 28: 193-204.
    • (2009) EMBO J , vol.28 , pp. 193-204
    • Bendezú, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    de Boer, P.A.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
  • 7
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-López, R., and Errington, J. (2003) The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell 4: 19-28.
    • (2003) Dev Cell , vol.4 , pp. 19-28
    • Carballido-López, R.1    Errington, J.2
  • 8
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-López, R., Formstone, A., Li, Y., Ehrlich, S.D., Noirot, P., and Errington, J. (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11: 399-409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-López, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 10
    • 33750713640 scopus 로고    scopus 로고
    • Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB
    • Defeu Soufo, H.J., and Graumann, P.L. (2006) Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol Microbiol 62: 1340-1356.
    • (2006) Mol Microbiol , vol.62 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 11
    • 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
  • 12
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni, A.V., Baida, C., White, C.L., and Gober, J.W. (2007) The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol 66: 174-188.
    • (2007) Mol Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 14
    • 77949567575 scopus 로고    scopus 로고
    • Bacterial actin MreB assembles in complex with cell shape protein RodZ
    • van den Ent, F., Johnson, C.M., Persons, L., de Boer, P., and Löwe, J. (2010) Bacterial actin MreB assembles in complex with cell shape protein RodZ. EMBO J 29: 1081-1090.
    • (2010) EMBO J , vol.29 , pp. 1081-1090
    • van den Ent, F.1    Johnson, C.M.2    Persons, L.3    de Boer, P.4    Löwe, J.5
  • 15
    • 67651210838 scopus 로고    scopus 로고
    • Magnetosomes and magneto-aerotaxis
    • Frankel, R.B., and Bazylinski, D.A. (2009) Magnetosomes and magneto-aerotaxis. Contrib Microbiol 16: 182-193.
    • (2009) Contrib Microbiol , vol.16 , pp. 182-193
    • Frankel, R.B.1    Bazylinski, D.A.2
  • 16
    • 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
  • 17
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B.subtilis
    • Garner, E.C., Bernard, R., Wang, W., Zhuang, X., Rudner, D.Z., and Mitchison, T. (2011) Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B.subtilis. Science 333: 222-225.
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 18
    • 80053999066 scopus 로고    scopus 로고
    • undated) Unrooted [WWW program]. URL
    • Gouy, M. (undated) Unrooted [WWW program]. URL.
    • Gouy, M.1
  • 19
    • 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
  • 20
    • 70349527943 scopus 로고    scopus 로고
    • Genomics, genetics, and cell biology of magnetosome formation
    • Jogler, C., and Schüler, D. (2009) Genomics, genetics, and cell biology of magnetosome formation. Annu Rev Microbiol 63: 501-521.
    • (2009) Annu Rev Microbiol , vol.63 , pp. 501-521
    • Jogler, C.1    Schüler, D.2
  • 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
    • 77954009237 scopus 로고    scopus 로고
    • Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense
    • Katzmann, E., Scheffel, A., Gruska, M., Plitzko, J.M., and Schüler, D. (2010) Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense. Mol Microbiol 77: 208-224.
    • (2010) Mol Microbiol , vol.77 , pp. 208-224
    • Katzmann, E.1    Scheffel, A.2    Gruska, M.3    Plitzko, J.M.4    Schüler, D.5
  • 24
    • 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
  • 25
    • 1642406025 scopus 로고    scopus 로고
    • Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation
    • Komeili, A., Vali, H., Beveridge, T.J., and Newman, D.K. (2004) Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation. Proc Natl Acad Sci USA 101: 3839-3844.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3839-3844
    • Komeili, A.1    Vali, H.2    Beveridge, T.J.3    Newman, D.K.4
  • 26
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili, A., Li, Z., Newman, D.K., and Jensen, G.J. (2006) Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311: 242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 27
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., Mastronarde, D.N., and McIntosh, J.R. (1996) Computer visualization of three-dimensional image data using IMOD. J Struct Biol 116: 71-76.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 28
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse, T., Bork-Jensen, J., and Gerdes, K. (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55: 78-89.
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 29
    • 17044371193 scopus 로고    scopus 로고
    • Peach: a simple Perl-based system for distributed computation and its application to cryo-EM data processing
    • Leong, P.A., Heymann, J.B., and Jensen, G.J. (2005) Peach: a simple Perl-based system for distributed computation and its application to cryo-EM data processing. Structure 13: 505-511.
    • (2005) Structure , vol.13 , pp. 505-511
    • Leong, P.A.1    Heymann, J.B.2    Jensen, G.J.3
  • 30
    • 77950442198 scopus 로고    scopus 로고
    • Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle
    • Murat, D., Quinlan, A., Vali, H., and Komeili, A. (2010) Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle. Proc Natl Acad Sci USA 107: 5593-5598.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5593-5598
    • Murat, D.1    Quinlan, A.2    Vali, H.3    Komeili, A.4
  • 31
    • 0037398732 scopus 로고    scopus 로고
    • Missing genes in metabolic pathways: a comparative genomics approach
    • Osterman, A., and Overbeek, R. (2003) Missing genes in metabolic pathways: a comparative genomics approach. Curr Opin Chem Biol 7: 238-251.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 238-251
    • Osterman, A.1    Overbeek, R.2
  • 32
    • 77954382802 scopus 로고    scopus 로고
    • An MCP-like protein interacts with the MamK cytoskeleton and is involved in magnetotaxis in Magnetospirillum magneticum AMB-1
    • Philippe, N., and Wu, L.F. (2010) An MCP-like protein interacts with the MamK cytoskeleton and is involved in magnetotaxis in Magnetospirillum magneticum AMB-1. J Mol Biol 400: 309-322.
    • (2010) J Mol Biol , vol.400 , pp. 309-322
    • Philippe, N.1    Wu, L.F.2
  • 33
    • 69849097861 scopus 로고    scopus 로고
    • The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation
    • Polka, J.K., 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, J.K.1    Kollman, J.M.2    Agard, D.A.3    Mullins, R.D.4
  • 34
    • 33751257193 scopus 로고    scopus 로고
    • Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles
    • Pradel, N., Santini, C.L., Bernadac, A., Fukumori, Y., and Wu, L.F. (2006) Biogenesis of actin-like bacterial cytoskeletal filaments destined for positioning prokaryotic magnetic organelles. Proc Natl Acad Sci USA 103: 17485-17489.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17485-17489
    • Pradel, N.1    Santini, C.L.2    Bernadac, A.3    Fukumori, Y.4    Wu, L.F.5
  • 35
    • 79955723752 scopus 로고    scopus 로고
    • The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization
    • Quinlan, A., Murat, D., Vali, H., and Komeili, A. (2011) The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization. Mol Microbiol 80: 1075-1087.
    • (2011) Mol Microbiol , vol.80 , pp. 1075-1087
    • Quinlan, A.1    Murat, D.2    Vali, H.3    Komeili, A.4
  • 37
    • 77949411276 scopus 로고    scopus 로고
    • A second actin-like MamK protein in Magnetospirillum magneticum AMB-1 encoded outside the genomic magnetosome island
    • Rioux, J.B., Philippe, N., Pereira, S., Pignol, D., Wu, L.F., and Ginet, N. (2010) A second actin-like MamK protein in Magnetospirillum magneticum AMB-1 encoded outside the genomic magnetosome island. PLoS ONE 5: e9151.
    • (2010) PLoS ONE , vol.5
    • Rioux, J.B.1    Philippe, N.2    Pereira, S.3    Pignol, D.4    Wu, L.F.5    Ginet, N.6
  • 38
    • 79954609556 scopus 로고    scopus 로고
    • Architecture and assembly of a divergent member of the ParM family of bacterial actin-like proteins
    • Rivera, C.R., Kollman, J.M., Polka, J.K., Agard, D.A., and Mullins, R.D. (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
  • 40
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage, D.F., Afonso, B., Chen, A.H., and Silver, P.A. (2010) Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 327: 1258-1261.
    • (2010) Science , vol.327 , pp. 1258-1261
    • Savage, D.F.1    Afonso, B.2    Chen, A.H.3    Silver, P.A.4
  • 41
    • 34548492254 scopus 로고    scopus 로고
    • The acidic repetitive domain of the Magnetospirillum gryphiswaldense MamJ protein displays hypervariability but is not required for magnetosome chain assembly
    • Scheffel, A., and Schüler, D. (2007) The acidic repetitive domain of the Magnetospirillum gryphiswaldense MamJ protein displays hypervariability but is not required for magnetosome chain assembly. J Bacteriol 189: 6437-6446.
    • (2007) J Bacteriol , vol.189 , pp. 6437-6446
    • Scheffel, A.1    Schüler, D.2
  • 42
    • 33644763960 scopus 로고    scopus 로고
    • An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria
    • Scheffel, A., Gruska, M., Faivre, D., Linaroudis, A., Plitzko, J.M., and Schüler, D. (2006) An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria. Nature 440: 110-114.
    • (2006) Nature , vol.440 , pp. 110-114
    • Scheffel, A.1    Gruska, M.2    Faivre, D.3    Linaroudis, A.4    Plitzko, J.M.5    Schüler, D.6
  • 43
    • 79952114513 scopus 로고    scopus 로고
    • The structure and function of bacterial actin homologs
    • Shaevitz, J.W., and Gitai, Z. (2010) The structure and function of bacterial actin homologs. Cold Spring Harb Perspect Biol 2: a000364.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Shaevitz, J.W.1    Gitai, Z.2
  • 45
    • 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
  • 46
    • 36749094503 scopus 로고    scopus 로고
    • Polymerization of the actin-like protein MamK, which is associated with magnetosomes
    • Taoka, A., Asada, R., Wu, L.F., and Fukumori, Y. (2007) Polymerization of the actin-like protein MamK, which is associated with magnetosomes. J Bacteriol 189: 8737-8740.
    • (2007) J Bacteriol , vol.189 , pp. 8737-8740
    • Taoka, A.1    Asada, R.2    Wu, L.F.3    Fukumori, Y.4
  • 48
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White, C.L., Kitich, A., and Gober, J.W. (2010) Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol Microbiol 76: 616-633.
    • (2010) Mol Microbiol , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.