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Volumn 5, Issue JAN, 2014, Pages

Structure prediction of magnetosome-associated proteins

Author keywords

Magnetosome; Magnetotactic bacteria; Membrane invagination; Protein structure function; Structure prediction

Indexed keywords

BACTERIAL PROTEIN; DIACYLGLYCEROL; DIACYLGLYCEROL KINASE; MAGNETOSOME ASSOCIATED PROTEIN; MAMA PROTEIN; MAMB PROTEIN; MAMC PROTEIN; MAMD PROTEIN; MAME PROTEIN; MAMF PROTEIN; MAMG PROTEIN; MAMH PROTEIN; MAMI PROTEIN; MAMJ PROTEIN; MAMK PROTEIN; MAML PROTEIN; MAMM PROTEIN; MAMN PROTEIN; MAMO PROTEIN; MAMP PROTEIN; MAMQ PROTEIN; MAMR PROTEIN; MAMS PROTEIN; MAMT PROTEIN; MAMU PROTEIN; MAMX PROTEIN; MAMY PROTEIN; MAMZ PROTEIN; MMS6 PROTEIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84893704714     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00009     Document Type: Article
Times cited : (73)

References (106)
  • 1
    • 80052968079 scopus 로고    scopus 로고
    • Common ancestry of iron oxide- and iron-sulfide-based biomineralization in magnetotactic bacteria
    • doi: 10.1038/ismej.2011.35
    • Abreu, F., Cantão, M. E., Nicolás, M. F., Barcellos, F. G., Morillo, V., Almeida, L. G., et al. (2011). Common ancestry of iron oxide- and iron-sulfide-based biomineralization in magnetotactic bacteria. ISME J. 5, 1634-1640. doi: 10.1038/ismej.2011.35
    • (2011) ISME J , vol.5 , pp. 1634-1640
    • Abreu, F.1    Cantão, M.E.2    Nicolás, M.F.3    Barcellos, F.G.4    Morillo, V.5    Almeida, L.G.6
  • 2
    • 84873144799 scopus 로고    scopus 로고
    • Cryo-electron tomography of the magnetotactic vibrio Magnetovibrio blakemorei: insights into the biomineralization of prismatic magnetosomes
    • doi: 10.1016/j.jsb.2012.12.002
    • Abreu, F., Sousa, A. A, Aronova, M. A, Kim, Y., Cox, D., Leapman, R. D., et al. (2013). Cryo-electron tomography of the magnetotactic vibrio Magnetovibrio blakemorei: insights into the biomineralization of prismatic magnetosomes. J. Struct. Biol. 181, 162-168. doi: 10.1016/j.jsb.2012.12.002
    • (2013) J. Struct. Biol. , vol.181 , pp. 162-168
    • Abreu, F.1    Sousa, A.A.2    Aronova, M.A.3    Kim, Y.4    Cox, D.5    Leapman, R.D.6
  • 4
    • 47649122779 scopus 로고    scopus 로고
    • Formation of magnetite by bacteria and its application
    • doi: 10.1098/rsif.2008.0170
    • Arakaki, A., Nakazawa, H., Nemoto, M., Mori, T., and Matsunaga, T. (2008). Formation of magnetite by bacteria and its application. J. R. Soc. Interface 5, 977-999. doi: 10.1098/rsif.2008.0170
    • (2008) J. R. Soc. Interface , vol.5 , pp. 977-999
    • Arakaki, A.1    Nakazawa, H.2    Nemoto, M.3    Mori, T.4    Matsunaga, T.5
  • 5
    • 0037424274 scopus 로고    scopus 로고
    • A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1
    • doi: 10.1074/jbc. M211729200
    • Arakaki, A., Webb, J., and Matsunaga, T. (2003). A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. J. Biol. Chem. 278, 8745-8750. doi: 10.1074/jbc. M211729200
    • (2003) J. Biol. Chem. , vol.278 , pp. 8745-8750
    • Arakaki, A.1    Webb, J.2    Matsunaga, T.3
  • 6
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • doi: 10.1093/bioinformatics/bti770
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006). The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. doi: 10.1093/bioinformatics/bti770
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 7
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • doi: 10.1073/pnas.181342398
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J., and McCammon, J. A. (2001). Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc. Natl. Acad. Sci. U.S.A. 98, 10037-10041. doi: 10.1073/pnas.181342398
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 8
    • 0018880142 scopus 로고
    • Ultrastructure of a magnetotactic spirillum
    • Balkwill, D. L., Maratea, D., and Blakemore, R. P. (1980). Ultrastructure of a magnetotactic spirillum. J. Bacteriol. 141, 1399-408.
    • (1980) J. Bacteriol. , vol.141 , pp. 1399-1408
    • Balkwill, D.L.1    Maratea, D.2    Blakemore, R.P.3
  • 9
    • 84883745459 scopus 로고    scopus 로고
    • Magnetotactic bacteria form magnetite from a phosphate-rich ferric hydroxide via nanometric ferric (oxyhydr)oxide intermediates
    • doi: 10.1073/pnas.1307119110
    • Baumgartner, J., Morin, G., Menguy, N., Perez Gonzalez, T., Widdrat, M., Cosmidis, J., et al. (2013). Magnetotactic bacteria form magnetite from a phosphate-rich ferric hydroxide via nanometric ferric (oxyhydr)oxide intermediates. Proc. Natl. Acad. Sci. U.S.A. 110, 14883-14888. doi: 10.1073/pnas.1307119110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 14883-14888
    • Baumgartner, J.1    Morin, G.2    Menguy, N.3    Perez Gonzalez, T.4    Widdrat, M.5    Cosmidis, J.6
  • 10
    • 8644265890 scopus 로고    scopus 로고
    • Chemolithoautotrophy in the marine, magnetotactic bacterial strains MV-1 and MV-2
    • doi: 10.1007/s00203-004-0716-y
    • Bazylinski, D. A., Dean, A. J., Williams, T. J., Long, L. K., Middleton, S. L., and Dubbels, B. L. (2004). Chemolithoautotrophy in the marine, magnetotactic bacterial strains MV-1 and MV-2. Arch. Microbiol. 182, 373-387. doi: 10.1007/s00203-004-0716-y
    • (2004) Arch. Microbiol. , vol.182 , pp. 373-387
    • Bazylinski, D.A.1    Dean, A.J.2    Williams, T.J.3    Long, L.K.4    Middleton, S.L.5    Dubbels, B.L.6
  • 11
    • 4844225111 scopus 로고    scopus 로고
    • Magnetosome formation in prokaryotes
    • doi: 10.1038/nrmicro842
    • Bazylinski, D. A, and Frankel, R. B. (2004). Magnetosome formation in prokaryotes. Nat. Rev. Microbiol. 2, 217-230. doi: 10.1038/nrmicro842
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 217-230
    • Bazylinski, D.A.1    Frankel, R.B.2
  • 12
    • 0000362638 scopus 로고
    • Biogeochemical conditions favoring magnetite formation during anaerobic iron reduction biogeochemical conditions favoring magnetite formation during anaerobic iron reduction
    • Bell, P. E., Mills, A. L., and Herman, J. S. (1987). Biogeochemical conditions favoring magnetite formation during anaerobic iron reduction biogeochemical conditions favoring magnetite formation during anaerobic iron reduction. Appl. Environ. Microbiol. 53, 2610-2616.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2610-2616
    • Bell, P.E.1    Mills, A.L.2    Herman, J.S.3
  • 13
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
    • Blatch, G. L., and Lässle, M. (1999). The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. BioEssays news Rev. Mol. Cell. Dev. Biol. 21, 932-939.
    • (1999) BioEssays news Rev. Mol. Cell. Dev. Biol. , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 14
    • 58949093219 scopus 로고    scopus 로고
    • The chemistry and biochemistry of heme c: functional bases for covalent attachment
    • doi: 10.1039/b717196j
    • Bowman, S. E. J., and Bren, K. L. (2008). The chemistry and biochemistry of heme c: functional bases for covalent attachment. Nat. Prod. Rep. 25, 1118-1130. doi: 10.1039/b717196j
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 1118-1130
    • Bowman, S.E.J.1    Bren, K.L.2
  • 15
    • 13444305296 scopus 로고    scopus 로고
    • The ProDom database of protein domain families: more emphasis on 3D
    • doi: 10.1093/nar/gki034
    • Bru, C., Courcelle, E., Carrère, S., Beausse, Y., Dalmar, S., and Kahn, D. (2005). The ProDom database of protein domain families: more emphasis on 3D. Nucleic Acids Res. 33, D212-D215. doi: 10.1093/nar/gki034
    • (2005) Nucleic Acids Res , vol.33
    • Bru, C.1    Courcelle, E.2    Carrère, S.3    Beausse, Y.4    Dalmar, S.5    Kahn, D.6
  • 16
    • 33845619142 scopus 로고    scopus 로고
    • The bacterial actin-like cytoskeleton
    • doi: 10.1128/MMBR.00014-06
    • Carballido-López, R. (2006). The bacterial actin-like cytoskeleton. Microbiol. Mol. Biol. Rev. 70, 888-909. doi: 10.1128/MMBR.00014-06
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 888-909
    • Carballido-López, R.1
  • 17
    • 84891370087 scopus 로고    scopus 로고
    • Interaction of proteins associated with the magnetosome assembly in magnetotactic bacteria as revealed by two-hybrid two-photon excitation fluorescence lifetime imaging microscopy förster resonance energy transfer
    • doi: 10.1021/jp4086987
    • Carillo, M. A., Bennet, M., and Faivre, D. (2013). Interaction of proteins associated with the magnetosome assembly in magnetotactic bacteria as revealed by two-hybrid two-photon excitation fluorescence lifetime imaging microscopy förster resonance energy transfer. J. Phys. Chem. B, 117, 14642-14648. doi: 10.1021/jp4086987
    • (2013) J. Phys. Chem. B , vol.117 , pp. 14642-14648
    • Carillo, M.A.1    Bennet, M.2    Faivre, D.3
  • 18
    • 23144465987 scopus 로고    scopus 로고
    • SCRATCH: a protein structure and structural feature prediction server
    • doi: 10.1093/nar/gki396
    • Cheng, J., Randall, A. Z., Sweredoski, M. J., and Baldi, P. (2005). SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res. 33, W72-W76. doi: 10.1093/nar/gki396
    • (2005) Nucleic Acids Res , vol.33
    • Cheng, J.1    Randall, A.Z.2    Sweredoski, M.J.3    Baldi, P.4
  • 19
    • 67749099836 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation
    • doi: 10.1074/jbc. M109.019653
    • Cohen-Gonsaud, M., Barthe, P., Canova, M. J., Stagier-Simon, C., Kremer, L., Roumestand, C., et al. (2009). The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation. J. Biol. Chem. 284, 19290-19300. doi: 10.1074/jbc. M109.019653
    • (2009) J. Biol. Chem. , vol.284 , pp. 19290-19300
    • Cohen-Gonsaud, M.1    Barthe, P.2    Canova, M.J.3    Stagier-Simon, C.4    Kremer, L.5    Roumestand, C.6
  • 20
    • 0037151036 scopus 로고    scopus 로고
    • A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane
    • doi: 10.1074/jbc. M200577200
    • Cragg, R. A, Christie, G. R., Phillips, S. R., Russi, R. M., Küry, S., Mathers, J. C., et al. (2002). A novel zinc-regulated human zinc transporter, hZTL1, is localized to the enterocyte apical membrane. J. Biol. Chem. 277, 22789-22797. doi: 10.1074/jbc. M200577200
    • (2002) J. Biol. Chem. , vol.277 , pp. 22789-22797
    • Cragg, R.A.1    Christie, G.R.2    Phillips, S.R.3    Russi, R.M.4    Küry, S.5    Mathers, J.C.6
  • 21
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5 implications for TPR-mediated protein-protein interactions
    • doi: 10.1093/emboj/17.5.1192
    • Das, A. K., Cohen, P. W., and Barford, D. (1998). The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17, 1192-1199. doi: 10.1093/emboj/17.5.1192
    • (1998) EMBO J , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 22
    • 0346945148 scopus 로고    scopus 로고
    • Pymol: an open-source molecular graphics tool. Ccp4 Newsl
    • DeLano, W. L. (2002). Pymol: an open-source molecular graphics tool. Ccp4 Newsl. Protein Crystallogr. 40, 11.
    • (2002) Protein Crystallogr , vol.40 , pp. 11
    • DeLano, W.L.1
  • 23
    • 0031780597 scopus 로고    scopus 로고
    • Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA
    • doi: 10.1046/j.1365-2958.1998.00752.x
    • Din, N., Quardokus, E. M., Sackett, M. J., and Brun, Y. V (1998). Dominant C-terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA. Mol. Microbiol. 27, 1051-1063. doi: 10.1046/j.1365-2958.1998.00752.x
    • (1998) Mol. Microbiol. , vol.27 , pp. 1051-1063
    • Din, N.1    Quardokus, E.M.2    Sackett, M.J.3    Brun, Y.V.4
  • 24
    • 75749102218 scopus 로고    scopus 로고
    • Deletion of the ftsZ-like gene results in the production of superparamagnetic magnetite magnetosomes in Magnetospirillum gryphiswaldense
    • doi: 10.1128/JB.01292-09
    • Ding, Y., Li, J., Liu, J., Yang, J., Jiang, W., Tian, J., et al. (2010). Deletion of the ftsZ-like gene results in the production of superparamagnetic magnetite magnetosomes in Magnetospirillum gryphiswaldense. J. Bacteriol. 192, 1097-1105. doi: 10.1128/JB.01292-09
    • (2010) J. Bacteriol. , vol.192 , pp. 1097-1105
    • Ding, Y.1    Li, J.2    Liu, J.3    Yang, J.4    Jiang, W.5    Tian, J.6
  • 25
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • doi: 10.1093/bioinformatics/bti541
    • Dosztányi, Z., Csizmok, V., Tompa, P., and Simon, I. (2005). IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21, 3433-3434. doi: 10.1093/bioinformatics/bti541
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 26
    • 80053944902 scopus 로고    scopus 로고
    • MamK, a bacterial actin, forms dynamic filaments in vivo that are regulated by the acidic proteins MamJ and LimJ
    • doi: 10.1111/j.1365-2958.2011.07815.x
    • Draper, O., Byrne, M. E., Li, Z., Keyhani, S., Barrozo, J. C., Jensen, G., et al. (2011). MamK, a bacterial actin, forms dynamic filaments in vivo that are regulated by the acidic proteins MamJ and LimJ. Mol. Microbiol. 82, 342-354. doi: 10.1111/j.1365-2958.2011.07815.x
    • (2011) Mol. Microbiol. , vol.82 , pp. 342-354
    • Draper, O.1    Byrne, M.E.2    Li, Z.3    Keyhani, S.4    Barrozo, J.C.5    Jensen, G.6
  • 27
    • 57349106491 scopus 로고    scopus 로고
    • Magnetotactic bacteria and magnetosomes
    • doi: 10.1021/cr078258w
    • Faivre, D., and Schüler, D. (2008). Magnetotactic bacteria and magnetosomes. Chem. Rev. 108, 4875-4898. doi: 10.1021/cr078258w
    • (2008) Chem. Rev. , vol.108 , pp. 4875-4898
    • Faivre, D.1    Schüler, D.2
  • 28
    • 84876585742 scopus 로고    scopus 로고
    • Magnetite biomineralization in Magnetospirillum gryphiswaldense?: time-resolved magnetic and structural studies
    • doi: 10.1021/nn3059983
    • Fdez-Gubieda, M. L., Alicia Muela, Javier Alonso, Ana Garc?a-Prieto, L. O., and Rodrigo Fernandez-Pacheco, and J. M. B. (2013). Magnetite biomineralization in Magnetospirillum gryphiswaldense?: time-resolved magnetic and structural studies. ACS Nano 7, 3297-3305. doi: 10.1021/nn3059983
    • (2013) ACS Nano , vol.7 , pp. 3297-3305
    • Fdez-Gubieda, M.L.1    Muela, A.2    Alonso, J.3    Ana García-Prieto, L.O.4    Fernandez-Pacheco, R.5    Barandiarán, J.M.6
  • 29
    • 84880104658 scopus 로고    scopus 로고
    • Integrated self-assembly of the mms6 magnetosome protein to form an iron-responsive structure
    • doi: 10.3390/ijms140714594
    • Feng, S., Wang, L., Palo, P., Liu, X., Mallapragada, S. K., and Nilsen-Hamilton, M. (2013). Integrated self-assembly of the mms6 magnetosome protein to form an iron-responsive structure. Int. J. Mol. Sci. 14, 14594-14606. doi: 10.3390/ijms140714594
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 14594-14606
    • Feng, S.1    Wang, L.2    Palo, P.3    Liu, X.4    Mallapragada, S.K.5    Nilsen-Hamilton, M.6
  • 30
    • 67651210838 scopus 로고    scopus 로고
    • Magnetosomes and magneto-aerotaxis
    • doi: 10.1159/000219380
    • Frankel, R. B., and Bazylinski, D. A. (2009). Magnetosomes and magneto-aerotaxis. Contrib. Microbiol. 16, 182-193. doi: 10.1159/000219380
    • (2009) Contrib. Microbiol. , vol.16 , pp. 182-193
    • Frankel, R.B.1    Bazylinski, D.A.2
  • 31
    • 0018346438 scopus 로고
    • Magnetite in freshwater magnetotactic bacteria
    • doi: 10.1126/science.203.4387.1355
    • Frankel, R. B., Blakemore, R. P., and Wolfe, R. S. (1979). Magnetite in freshwater magnetotactic bacteria. Science 203, 1355-1356. doi: 10.1126/science.203.4387.1355
    • (1979) Science , vol.203 , pp. 1355-1356
    • Frankel, R.B.1    Blakemore, R.P.2    Wolfe, R.S.3
  • 32
    • 31444443960 scopus 로고    scopus 로고
    • Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed
    • doi: 10.1016/j.febslet.2006.01.003
    • Fukuda, Y., Okamura, Y., Takeyama, H., and Matsunaga, T. (2006). Dynamic analysis of a genomic island in Magnetospirillum sp. strain AMB-1 reveals how magnetosome synthesis developed. FEBS Lett. 580, 801-812. doi: 10.1016/j.febslet.2006.01.003
    • (2006) FEBS Lett , vol.580 , pp. 801-812
    • Fukuda, Y.1    Okamura, Y.2    Takeyama, H.3    Matsunaga, T.4
  • 33
    • 0023954501 scopus 로고
    • Characterization of the bacterial magnetosome membrane
    • Gorby, Y. A, Beveridge, T. J., and Blakemore, R. P. (1988). Characterization of the bacterial magnetosome membrane. J. Bacteriol. 170, 834-841.
    • (1988) J. Bacteriol. , vol.170 , pp. 834-841
    • Gorby, Y.A.1    Beveridge, T.J.2    Blakemore, R.P.3
  • 34
    • 84865308519 scopus 로고    scopus 로고
    • Biogenesis and subcellular organization of the magnetosome organelles of magnetotactic bacteria
    • doi: 10.1016/j.ceb.2012.05.008
    • Greene, S. E., and Komeili, A. (2012). Biogenesis and subcellular organization of the magnetosome organelles of magnetotactic bacteria. Curr. Opin. Cell Biol. 24, 490-495. doi: 10.1016/j.ceb.2012.05.008
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 490-495
    • Greene, S.E.1    Komeili, A.2
  • 35
    • 1842592740 scopus 로고    scopus 로고
    • Biochemical and proteomic analysis of the magnetosome membrane in Magnetospirillum gryphiswaldense
    • doi: 10.1128/AEM.70.2.1040-1050.2004
    • Gru, K., Mu, E., Otto, A., Reszka, R., Linder, D., Kube, M., et al. (2004). Biochemical and proteomic analysis of the magnetosome membrane in Magnetospirillum gryphiswaldense. 70, 1040-1050. doi: 10.1128/AEM.70.2.1040-1050.2004
    • (2004) , vol.70 , pp. 1040-1050
    • Gru, K.1    Mu, E.2    Otto, A.3    Reszka, R.4    Linder, D.5    Kube, M.6
  • 36
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • doi: 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723. doi: 10.1002/elps.1150181505
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 37
    • 20944450788 scopus 로고    scopus 로고
    • New developments in the understanding of the cation diffusion facilitator family
    • doi: 10.1007/s10295-005-0224-3
    • Haney, C. J., Grass, G., Franke, S., and Rensing, C. (2005). New developments in the understanding of the cation diffusion facilitator family. J. Ind. Microbiol. Biotechnol. 32, 215-226. doi: 10.1007/s10295-005-0224-3
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 215-226
    • Haney, C.J.1    Grass, G.2    Franke, S.3    Rensing, C.4
  • 38
    • 0025599473 scopus 로고
    • Ton B protein of Salmonella typhimurium A model for signal tranduction between membranes
    • doi: 10.1016/S0022-2836(99)80009-6
    • Hannavy, K., Barr, G. C., Dorman, C. J., Adamson, J., Mazengera, L. R., Gallagher, M. P., et al. (1990). Ton B protein of Salmonella typhimurium A model for signal tranduction between membranes. J. Mol. Biol. 216, 897-910. doi: 10.1016/S0022-2836(99)80009-6
    • (1990) J. Mol. Biol. , vol.216 , pp. 897-910
    • Hannavy, K.1    Barr, G.C.2    Dorman, C.J.3    Adamson, J.4    Mazengera, L.R.5    Gallagher, M.P.6
  • 39
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • doi: 10.1126/science.1087619
    • Huang, Y., Lemieux, M. J., Song, J., Auer, M., and Wang, D.-N. (2003). Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301, 616-620. doi: 10.1126/science.1087619
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.-N.5
  • 40
    • 34247854965 scopus 로고    scopus 로고
    • Role of the PDZ domains in Escherichia coli DegP protein
    • doi: 10.1128/JB.01788-06
    • Iwanczyk, J., Damjanovic, D., Kooistra, J., Leong, V., Jomaa, A., Ghirlando, R., et al. (2007). Role of the PDZ domains in Escherichia coli DegP protein. J. Bacteriol. 189, 3176-3186. doi: 10.1128/JB.01788-06
    • (2007) J. Bacteriol. , vol.189 , pp. 3176-3186
    • Iwanczyk, J.1    Damjanovic, D.2    Kooistra, J.3    Leong, V.4    Jomaa, A.5    Ghirlando, R.6
  • 41
    • 83355177967 scopus 로고    scopus 로고
    • Magnetosome chains are recruited to cellular division sites and split by asymmetric septation
    • doi: 10.1111/j.1365-2958.2011.07874.x
    • Katzmann, E., Müller, F. D., Lang, C., Messerer, M., Winklhofer, M., Plitzko, J. M., et al. (2011). Magnetosome chains are recruited to cellular division sites and split by asymmetric septation. Mol. Microbiol. 82, 1316-1329. doi: 10.1111/j.1365-2958.2011.07874.x
    • (2011) Mol. Microbiol. , vol.82 , pp. 1316-1329
    • Katzmann, E.1    Müller, F.D.2    Lang, C.3    Messerer, M.4    Winklhofer, M.5    Plitzko, J.M.6
  • 42
    • 77954009237 scopus 로고    scopus 로고
    • Loss of the actin-like protein MamK has pleiotropic effects on magnetosome formation and chain assembly in Magnetospirillum gryphiswaldense
    • doi: 10.1111/j.1365-2958.2010.07202.x
    • 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. doi: 10.1111/j.1365-2958.2010.07202.x
    • (2010) Mol. Microbiol. , vol.77 , pp. 208-224
    • Katzmann, E.1    Scheffel, A.2    Gruska, M.3    Plitzko, J.M.4    Schüler, D.5
  • 43
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • doi: 10.1038/nprot.2009.2
    • Kelley, L. A., and Sternberg, M. J. E. (2009). Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371. doi: 10.1038/nprot.2009.2
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 44
    • 0027073933 scopus 로고
    • Magnetic domain state and coercivity predictions for biogenic greigite (Fe3S4): a comparison of theory with magnetosome observations
    • doi: 10.1029/92JB01290
    • Kirschvink, J. C. D. R. J. L. (1992). Magnetic domain state and coercivity predictions for biogenic greigite (Fe3S4): a comparison of theory with magnetosome observations. J. Geophys. Res. 97 17309-17315. doi: 10.1029/92JB01290
    • (1992) J. Geophys. Res. , vol.97 , pp. 17309-17315
    • Kirschvink, J.C.D.R.J.L.1
  • 45
    • 83355174257 scopus 로고    scopus 로고
    • Molecular mechanisms of compartmentalization and biomineralization in magnetotactic bacteria
    • doi: 10.1111/j.1574-6976.2011.00315.x
    • Komeili, A. (2012). Molecular mechanisms of compartmentalization and biomineralization in magnetotactic bacteria. FEMS Microbiol. Rev. 36, 232-255. doi: 10.1111/j.1574-6976.2011.00315.x
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 232-255
    • Komeili, A.1
  • 46
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • doi: 10.1126/science.1123231
    • 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. doi: 10.1126/science.1123231
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 47
    • 1642406025 scopus 로고    scopus 로고
    • Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation
    • doi: 10.1073/pnas.0400391101
    • 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. U.S.A. 101, 3839-3844. doi: 10.1073/pnas.0400391101
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3839-3844
    • Komeili, A.1    Vali, H.2    Beveridge, T.J.3    Newman, D.K.4
  • 48
    • 49449106164 scopus 로고    scopus 로고
    • Expression of green fluorescent protein fused to magnetosome proteins in microaerophilic magnetotactic bacteria
    • doi: 10.1128/AEM.00231-08
    • Lang, C., and Schüler, D. (2008). Expression of green fluorescent protein fused to magnetosome proteins in microaerophilic magnetotactic bacteria. Appl. Environ. Microbiol. 74, 4944-4953. doi: 10.1128/AEM.00231-08
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 4944-4953
    • Lang, C.1    Schüler, D.2
  • 49
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: structure, specificity, and modification
    • doi: 10.1186/1478-811X-8-8
    • Lee, H.-J., and Zheng, J. J. (2010). PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun. Signal. 8, 8. doi: 10.1186/1478-811X-8-8
    • (2010) Cell Commun. Signal. , vol.8 , pp. 8
    • Lee, H.-J.1    Zheng, J.J.2
  • 50
    • 0030200603 scopus 로고    scopus 로고
    • Identification of an H2-M3-restricted Listeria epitope: implications for antigen presentation by M3
    • doi: 10.1016/S1074-7613(00)80310-6
    • Lenz, L. L., Dere, B., and Bevan, M. J. (1996). Identification of an H2-M3-restricted Listeria epitope: implications for antigen presentation by M3. Immunity 5, 63-72. doi: 10.1016/S1074-7613(00)80310-6
    • (1996) Immunity , vol.5 , pp. 63-72
    • Lenz, L.L.1    Dere, B.2    Bevan, M.J.3
  • 51
    • 0041386069 scopus 로고    scopus 로고
    • ClustalW-MPI: ClustalW analysis using distributed and parallel computing
    • doi: 10.1093/bioinformatics/btg192
    • Li, K.-B. (2003). ClustalW-MPI: ClustalW analysis using distributed and parallel computing. Bioinformatics 19, 1585-1586. doi: 10.1093/bioinformatics/btg192
    • (2003) Bioinformatics , vol.19 , pp. 1585-1586
    • Li, K.-B.1
  • 52
    • 84857884618 scopus 로고    scopus 로고
    • Functional analysis of the magnetosome island in Magnetospirillum gryphiswaldense: the mamAB operon is sufficient for magnetite biomineralization
    • doi: 10.1371/journal.pone.0025561
    • Lohsse, A., Ullrich, S., Katzmann, E., Borg, S., Wanner, G., Richter, M., et al. (2011). Functional analysis of the magnetosome island in Magnetospirillum gryphiswaldense: the mamAB operon is sufficient for magnetite biomineralization. PLoS ONE 6:e25561. doi: 10.1371/journal.pone.0025561
    • (2011) PLoS ONE , vol.6
    • Lohsse, A.1    Ullrich, S.2    Katzmann, E.3    Borg, S.4    Wanner, G.5    Richter, M.6
  • 53
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • doi: 10.1038/34472
    • Löwe, J., and Amos, L. A. (1998). Crystal structure of the bacterial cell-division protein FtsZ. Nature 391, 203-206. doi: 10.1038/34472
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 54
    • 84876811958 scopus 로고    scopus 로고
    • The bacterial magnetosome: a unique prokaryotic organelle
    • doi: 10.1159/000346543
    • Lower, B. H., and Bazylinski, D. A. (2013). The bacterial magnetosome: a unique prokaryotic organelle. J. Mol. Microbiol. Biotechnol. 23, 63-80. doi: 10.1159/000346543
    • (2013) J. Mol. Microbiol. Biotechnol. , vol.23 , pp. 63-80
    • Lower, B.H.1    Bazylinski, D.A.2
  • 55
    • 70349789244 scopus 로고    scopus 로고
    • Structural basis for autoregulation of the zinc transporter YiiP
    • doi: 10.1038/nsmb.1662
    • Lu, M., Chai, J., and Fu, D. (2009). Structural basis for autoregulation of the zinc transporter YiiP. Nat. Struct. Mol. Biol. 16, 1063-1067. doi: 10.1038/nsmb.1662
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1063-1067
    • Lu, M.1    Chai, J.2    Fu, D.3
  • 56
    • 84869884515 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter
    • doi: 10.1038/nature11542
    • Mancusso, R., Gregorio, G. G., Liu, Q., and Wang, D.-N. (2012). Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter. Nature 491, 622-626. doi: 10.1038/nature11542
    • (2012) Nature , vol.491 , pp. 622-626
    • Mancusso, R.1    Gregorio, G.G.2    Liu, Q.3    Wang, D.-N.4
  • 57
    • 0025197444 scopus 로고
    • Biomineralization of ferrimagnetic greigite (Fe3S4) and iron pyrite (FeS2) in a magnetotactic bacterium
    • doi: 10.1038/343258a0
    • Mann, S., Sparks, N. H. C., Frankel, R. B., Bazylinski, D. A., and Jannasch, H. W. (1990). Biomineralization of ferrimagnetic greigite (Fe3S4) and iron pyrite (FeS2) in a magnetotactic bacterium. Nature 343, 258-261. doi: 10.1038/343258a0
    • (1990) Nature , vol.343 , pp. 258-261
    • Mann, S.1    Sparks, N.H.C.2    Frankel, R.B.3    Bazylinski, D.A.4    Jannasch, H.W.5
  • 59
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • doi: 10.1093/bioinformatics/16.4.404
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000). The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405. doi: 10.1093/bioinformatics/16.4.404
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 60
    • 38149018650 scopus 로고    scopus 로고
    • Diacylglycerol kinases: at the hub of cell signalling
    • doi: 10.1042/BJ20071040
    • Mérida, I., Avila-Flores, A., and Merino, E. (2008). Diacylglycerol kinases: at the hub of cell signalling. Biochem. J. 409, 1-18. doi: 10.1042/BJ20071040
    • (2008) Biochem. J. , vol.409 , pp. 1-18
    • Mérida, I.1    Avila-Flores, A.2    Merino, E.3
  • 61
    • 0032518656 scopus 로고    scopus 로고
    • Dynamic assembly of FtsZ regulated by GTP hydrolysis
    • doi: 10.1093/emboj/17.2.462
    • Mukherjee, A, and Lutkenhaus, J. (1998). Dynamic assembly of FtsZ regulated by GTP hydrolysis. EMBO J. 17, 462-469. doi: 10.1093/emboj/17.2.462
    • (1998) EMBO J , vol.17 , pp. 462-469
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 62
    • 84864820253 scopus 로고    scopus 로고
    • The magnetosome membrane protein, MmsF, is a major regulator of magnetite biomineralization in Magnetospirillum magneticum AMB-1
    • doi: 10.1111/j.1365-2958.2012.08132.x
    • Murat, D., Falahati, V., Bertinetti, L., Csencsits, R., Körnig, A., Downing, K., et al. (2012). The magnetosome membrane protein, MmsF, is a major regulator of magnetite biomineralization in Magnetospirillum magneticum AMB-1. Mol. Microbiol. 85, 684-699. doi: 10.1111/j.1365-2958.2012.08132.x
    • (2012) Mol. Microbiol. , vol.85 , pp. 684-699
    • Murat, D.1    Falahati, V.2    Bertinetti, L.3    Csencsits, R.4    Körnig, A.5    Downing, K.6
  • 63
    • 77950442198 scopus 로고    scopus 로고
    • Comprehensive genetic dissection of the magnetosome gene island reveals the step-wise assembly of a prokaryotic organelle
    • doi: 10.1073/pnas.0914439107
    • 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. U.S.A. 107, 5593-5598. doi: 10.1073/pnas.0914439107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5593-5598
    • Murat, D.1    Quinlan, A.2    Vali, H.3    Komeili, A.4
  • 64
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold:common structural and functional solution for non-homologous sequences
    • Murzin, A. G. (1993). OB(oligonucleotide/oligosaccharide binding)-fold:common structural and functional solution for non-homologous sequences. EMBO J. 12, 861-867.
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 65
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • doi: 10.1111/j.1432-1033.1994.00951.x
    • Niggli, V., Kaufmann, S., Goldmann, W. H., Weber, T., and Isenberg, G. (1994). Identification of functional domains in the cytoskeletal protein talin. Eur. J. Biochem. 224, 951-957. doi: 10.1111/j.1432-1033.1994.00951.x
    • (1994) Eur. J. Biochem. , vol.224 , pp. 951-957
    • Niggli, V.1    Kaufmann, S.2    Goldmann, W.H.3    Weber, T.4    Isenberg, G.5
  • 66
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • doi: 10.1074/jbc. R000006200
    • O'Halloran, T. V, and Culotta, V. C. (2000). Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275, 25057-25060. doi: 10.1074/jbc. R000006200
    • (2000) J. Biol. Chem. , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 67
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi, K., Ohto, Y., Aizawa, S., Macnab, R. M., and Iino, T. (1994). FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176, 2272-2281.
    • (1994) J. Bacteriol. , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.3    Macnab, R.M.4    Iino, T.5
  • 68
    • 0029994744 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene encoding a new member of the tetratricopeptide protein family from magnetosomes of Magnetospirillum magnetotacticum
    • doi: 10.1016/0378-1119(95)00008-9
    • Okuda, Y., Denda, K., and Fukumori, Y. (1996). Cloning and sequencing of a gene encoding a new member of the tetratricopeptide protein family from magnetosomes of Magnetospirillum magnetotacticum. Gene 171, 99-102. doi: 10.1016/0378-1119(95)00008-9
    • (1996) Gene , vol.171 , pp. 99-102
    • Okuda, Y.1    Denda, K.2    Fukumori, Y.3
  • 69
    • 84864021815 scopus 로고    scopus 로고
    • Identification of functionally important TonB-ExbD periplasmic domain interactions in vivo
    • doi: 10.1128/JB.00018-12
    • Ollis, A. A, and Postle, K. (2012). Identification of functionally important TonB-ExbD periplasmic domain interactions in vivo. J. Bacteriol. 194, 3078-3087. doi: 10.1128/JB.00018-12
    • (2012) J. Bacteriol. , vol.194 , pp. 3078-3087
    • Ollis, A.A.1    Postle, K.2
  • 70
    • 84873636376 scopus 로고    scopus 로고
    • The bacterial actin MamK: in vitro assembly behavior and filament architecture
    • doi: 10.1074/jbc. M112.417030
    • Ozyamak, E., Kollman, J., Agard, D. A, and Komeili, A. (2013). The bacterial actin MamK: in vitro assembly behavior and filament architecture. J. Biol. Chem. 288, 4265-4277. doi: 10.1074/jbc. M112.417030
    • (2013) J. Biol. Chem. , vol.288 , pp. 4265-4277
    • Ozyamak, E.1    Kollman, J.2    Agard, D.A.3    Komeili, A.4
  • 71
    • 0030812638 scopus 로고    scopus 로고
    • MicroReview The HtrA family of serine proteases
    • doi: 10.1046/j.1365-2958.1997.5601928.x
    • Pallen, M. J., and Wren, B. W. (1997). MicroReview The HtrA family of serine proteases. Mol. Microbiol. 26, 209-221. doi: 10.1046/j.1365-2958.1997.5601928.x
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 73
    • 4143083987 scopus 로고    scopus 로고
    • Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
    • doi: 10.1038/sj.emboj.7600285
    • Papagrigoriou, E., Gingras, A. R., Barsukov, I. L., Bate, N., Fillingham, I. J., Patel, B., et al. (2004). Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. EMBO J. 23, 2942-2951. doi: 10.1038/sj.emboj.7600285
    • (2004) EMBO J , vol.23 , pp. 2942-2951
    • Papagrigoriou, E.1    Gingras, A.R.2    Barsukov, I.L.3    Bate, N.4    Fillingham, I.J.5    Patel, B.6
  • 75
    • 0030953624 scopus 로고    scopus 로고
    • A novel family of ubiquitous heavy metal ion transport proteins
    • doi: 10.1007/s002329900192
    • Paulsen, I. T., and Saier, M. H. (1997). A novel family of ubiquitous heavy metal ion transport proteins. J. Membr. Biol. 156, 99-103. doi: 10.1007/s002329900192
    • (1997) J. Membr. Biol. , vol.156 , pp. 99-103
    • Paulsen, I.T.1    Saier, M.H.2
  • 76
    • 84876797248 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic phosphate transporter
    • doi: 10.1038/nature12042
    • Pedersen, B. P., Kumar, H., Waight, A. B., Risenmay, A. J., Roe-Zurz, Z., Chau, B. H., et al. (2013). Crystal structure of a eukaryotic phosphate transporter. Nature 496, 533-536. doi: 10.1038/nature12042
    • (2013) Nature , vol.496 , pp. 533-536
    • Pedersen, B.P.1    Kumar, H.2    Waight, A.B.3    Risenmay, A.J.4    Roe-Zurz, Z.5    Chau, B.H.6
  • 77
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
    • doi: 10.1126/science.1092586
    • Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., et al. (2004). BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303, 495-499. doi: 10.1126/science.1092586
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6
  • 78
    • 79955723752 scopus 로고    scopus 로고
    • The HtrA/DegP family protease MamE is a bifunctional protein with roles in magnetosome protein localization and magnetite biomineralization
    • doi: 10.1111/j.1365-2958.2011.07631.x
    • 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. doi: 10.1111/j.1365-2958.2011.07631.x
    • (2011) Mol. Microbiol. , vol.80 , pp. 1075-1087
    • Quinlan, A.1    Murat, D.2    Vali, H.3    Komeili, A.4
  • 79
    • 84883162839 scopus 로고    scopus 로고
    • The magnetosome proteins MamX, MamZ, and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense
    • doi: 10.1111/mmi.12317
    • Raschdorf, O., Müller, F. D., Pósfai, M., Plitzko, J. M., and Schüler, D. (2013). The magnetosome proteins MamX, MamZ, and MamH are involved in redox control of magnetite biomineralization in Magnetospirillum gryphiswaldense. Mol. Microbiol. 86, 872-886. doi: 10.1111/mmi.12317
    • (2013) Mol. Microbiol. , vol.86 , pp. 872-886
    • Raschdorf, O.1    Müller, F.D.2    Pósfai, M.3    Plitzko, J.M.4    Schüler, D.5
  • 80
    • 34347392111 scopus 로고    scopus 로고
    • Comparative genome analysis of four magnetotactic bacteria reveals a complex set of group-specific genes implicated in magnetosome biomineralization and function
    • doi: 10.1128/JB.00119-07
    • Richter, M., Kube, M., Bazylinski, D. A, Lombardot, T., Glöckner, F. O., Reinhardt, R., et al. (2007). Comparative genome analysis of four magnetotactic bacteria reveals a complex set of group-specific genes implicated in magnetosome biomineralization and function. J. Bacteriol. 189, 4899-4910. doi: 10.1128/JB.00119-07
    • (2007) J. Bacteriol. , vol.189 , pp. 4899-4910
    • Richter, M.1    Kube, M.2    Bazylinski, D.A.3    Lombardot, T.4    Glöckner, F.O.5    Reinhardt, R.6
  • 81
    • 0036928819 scopus 로고    scopus 로고
    • Regulation of directionality in bacteriophage ? site-specific recombination: structure of the Xis protein
    • doi: 10.1016/S0022-2836(02)01150-6
    • Sam, M. D., Papagiannis, C. V., Connolly, K. M., Corselli, L., Iwahara, J., Lee, J., et al. (2002). Regulation of directionality in bacteriophage ? site-specific recombination: structure of the Xis protein. J. Mol. Biol. 324, 791-805. doi: 10.1016/S0022-2836(02)01150-6
    • (2002) J. Mol. Biol. , vol.324 , pp. 791-805
    • Sam, M.D.1    Papagiannis, C.V.2    Connolly, K.M.3    Corselli, L.4    Iwahara, J.5    Lee, J.6
  • 82
    • 37549010991 scopus 로고    scopus 로고
    • The major magnetosome proteins MamGFDC are not essential for magnetite biomineralization in Magnetospirillum gryphiswaldense but regulate the size of magnetosome crystals
    • doi: 10.1128/JB.01371-07
    • Scheffel, A., Gärdes, A., Grünberg, K., Wanner, G., and Schüler, D. (2008). The major magnetosome proteins MamGFDC are not essential for magnetite biomineralization in Magnetospirillum gryphiswaldense but regulate the size of magnetosome crystals. J. Bacteriol. 190, 377-386. doi: 10.1128/JB.01371-07
    • (2008) J. Bacteriol. , vol.190 , pp. 377-386
    • Scheffel, A.1    Gärdes, A.2    Grünberg, K.3    Wanner, G.4    Schüler, D.5
  • 83
    • 33644763960 scopus 로고    scopus 로고
    • An acidic protein aligns magnetosomes along a filamentous structure in magnetotactic bacteria
    • doi: 10.1038/nature04382
    • 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. doi: 10.1038/nature04382
    • (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
  • 84
    • 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
    • doi: 10.1128/JB.00421-07
    • 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. doi: 10.1128/JB.00421-07
    • (2007) J. Bacteriol. , vol.189 , pp. 6437-6446
    • Scheffel, A.1    Schüler, D.2
  • 85
    • 0035964940 scopus 로고    scopus 로고
    • The polymerization mechanism of the bacterial cell division protein FtsZ
    • doi: 10.1016/S0014-5793(01)02855-1
    • Scheffers, D., and Driessen, A J. (2001). The polymerization mechanism of the bacterial cell division protein FtsZ. FEBS Lett. 506, 6-10. doi: 10.1016/S0014-5793(01)02855-1
    • (2001) FEBS Lett , vol.506 , pp. 6-10
    • Scheffers, D.1    Driessen, A.J.2
  • 86
    • 0025994679 scopus 로고
    • The genus Magnetospirillum gen. nov. description of Magnetospirillum gryphiswaldense sp. nov. and transfer of Aquaspirillum magnetotacticum to Magnetospirillum magnetotacticum comb. nov
    • doi: 10.1016/S0723-2020(11)80313-9
    • Schleifer, K.-H., Schüler, D., Spring, S., Weizenegger, M., Amann, R., Ludwig, W., et al. (1991). The genus Magnetospirillum gen. nov. description of Magnetospirillum gryphiswaldense sp. nov. and transfer of Aquaspirillum magnetotacticum to Magnetospirillum magnetotacticum comb. nov. Syst. Appl. Microbiol. 14, 379-385. doi: 10.1016/S0723-2020(11)80313-9
    • (1991) Syst. Appl. Microbiol. , vol.14 , pp. 379-385
    • Schleifer, K.-H.1    Schüler, D.2    Spring, S.3    Weizenegger, M.4    Amann, R.5    Ludwig, W.6
  • 87
    • 17344383176 scopus 로고    scopus 로고
    • Characterization of a spontaneous nonmagnetic mutant of Magnetospirillum gryphiswaldense reveals a large deletion comprising a putative magnetosome island
    • doi: 10.1128/JB.185.19.5779-5790.2003
    • Schübbe, S., Kube, M., and Scheffel, A. (2003). Characterization of a spontaneous nonmagnetic mutant of Magnetospirillum gryphiswaldense reveals a large deletion comprising a putative magnetosome island. J. Bacteriol. 185, 5779-5790. doi: 10.1128/JB.185.19.5779-5790.2003
    • (2003) J. Bacteriol. , vol.185 , pp. 5779-5790
    • Schübbe, S.1    Kube, M.2    Scheffel, A.3
  • 88
    • 33748791714 scopus 로고    scopus 로고
    • Transcriptional organization and regulation of magnetosome operons in Magnetospirillum gryphiswaldense
    • doi: 10.1128/AEM.00201-06
    • Schübbe, S., Würdemann, C., Peplies, J., Heyen, U., Wawer, C., Glöckner, F. O., et al. (2006). Transcriptional organization and regulation of magnetosome operons in Magnetospirillum gryphiswaldense. Appl. Environ. Microbiol. 72, 5757-5765. doi: 10.1128/AEM.00201-06
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5757-5765
    • Schübbe, S.1    Würdemann, C.2    Peplies, J.3    Heyen, U.4    Wawer, C.5    Glöckner, F.O.6
  • 89
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • doi: 10.1146/annurev.neuro.24.1.1
    • Sheng, M., and Sala, C. (2001). PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29. doi: 10.1146/annurev.neuro.24.1.1
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 90
    • 84870230056 scopus 로고    scopus 로고
    • Magnetochrome: a c-type cytochrome domain specific to magnetotatic bacteria
    • doi: 10.1042/BST20120104
    • Siponen, M. I., Adryanczyk, G., Ginet, N., Arnoux, P., and Pignol, D. (2012). Magnetochrome: a c-type cytochrome domain specific to magnetotatic bacteria. Biochem. Soc. Trans. 40, 1319-1323. doi: 10.1042/BST20120104
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1319-1323
    • Siponen, M.I.1    Adryanczyk, G.2    Ginet, N.3    Arnoux, P.4    Pignol, D.5
  • 91
    • 84886946156 scopus 로고    scopus 로고
    • Structural insight into magnetochrome-mediated magnetite biomineralization
    • doi: 10.1038/nature12573
    • Siponen, M. I., Legrand, P., Widdrat, M., Jones, S. R., Zhang, W.-J., Chang, M. C. Y., et al. (2013). Structural insight into magnetochrome-mediated magnetite biomineralization. Nature 502, 681-684. doi: 10.1038/nature12573
    • (2013) Nature , vol.502 , pp. 681-684
    • Siponen, M.I.1    Legrand, P.2    Widdrat, M.3    Jones, S.R.4    Zhang, W.-J.5    Chang, M.C.Y.6
  • 92
    • 36949006066 scopus 로고    scopus 로고
    • XtalPred: a web server for prediction of protein crystallizability
    • doi: 10.1093/bioinformatics/btm477
    • Slabinski, L., Jaroszewski, L., Rychlewski, L., Wilson, I. A, Lesley, S. A, and Godzik, A. (2007). XtalPred: a web server for prediction of protein crystallizability. Bioinformatics 23, 3403-3405. doi: 10.1093/bioinformatics/btm477
    • (2007) Bioinformatics , vol.23 , pp. 3403-3405
    • Slabinski, L.1    Jaroszewski, L.2    Rychlewski, L.3    Wilson, I.4    Lesley, A.S.5    Godzik, A.A.6
  • 93
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • doi: 10.1093/bioinformatics/bti125
    • Söding, J. (2005). Protein homology detection by HMM-HMM comparison. Bioinformatics 21, 951-960. doi: 10.1093/bioinformatics/bti125
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 94
    • 47749126543 scopus 로고    scopus 로고
    • Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer
    • doi: 10.1074/jbc. M710126200
    • Solmaz, S. R. N., and Hunte, C. (2008). Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J. Biol. Chem. 283, 17542-17549. doi: 10.1074/jbc. M710126200
    • (2008) J. Biol. Chem. , vol.283 , pp. 17542-17549
    • Solmaz, S.R.N.1    Hunte, C.2
  • 95
    • 84860617794 scopus 로고    scopus 로고
    • Insight into the assembly properties and functional organisation of the magnetotactic bacterial actin-like homolog MamK
    • doi: 10.1371/journal.pone.0034189
    • Sonkaria, S., Fuentes, G., Verma, C., Narang, R., Khare, V., Fischer, A., et al. (2012). Insight into the assembly properties and functional organisation of the magnetotactic bacterial actin-like homolog, MamK. PLoS ONE 7:e34189. doi: 10.1371/journal.pone.0034189
    • (2012) PLoS ONE , vol.7
    • Sonkaria, S.1    Fuentes, G.2    Verma, C.3    Narang, R.4    Khare, V.5    Fischer, A.6
  • 96
    • 77951185382 scopus 로고    scopus 로고
    • Identification and functional characterization of liposome tubulation protein from magnetotactic bacteria
    • doi: 10.1111/j.1365-2958.2010.07117.x
    • Tanaka, M., Arakaki, A., and Matsunaga, T. (2010). Identification and functional characterization of liposome tubulation protein from magnetotactic bacteria. Mol. Microbiol. 76, 480-488. doi: 10.1111/j.1365-2958.2010.07117.x
    • (2010) Mol. Microbiol. , vol.76 , pp. 480-488
    • Tanaka, M.1    Arakaki, A.2    Matsunaga, T.3
  • 97
    • 79953175285 scopus 로고    scopus 로고
    • MMS6 protein regulates crystal morphology during nano-sized magnetite biomineralization in vivo
    • doi: 10.1074/jbc. M110.183434
    • Tanaka, M., Mazuyama, E., Arakaki, A., and Matsunaga, T. (2011). MMS6 protein regulates crystal morphology during nano-sized magnetite biomineralization in vivo. J. Biol. Chem. 286, 6386-6392. doi: 10.1074/jbc. M110.183434
    • (2011) J. Biol. Chem. , vol.286 , pp. 6386-6392
    • Tanaka, M.1    Mazuyama, E.2    Arakaki, A.3    Matsunaga, T.4
  • 98
    • 80855144209 scopus 로고    scopus 로고
    • The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly
    • doi: 10.1111/j.1365-2958.2011.07863.x
    • Uebe, R., Junge, K., Henn, V., Poxleitner, G., Katzmann, E., Plitzko, J. M., et al. (2011). The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol. Microbiol. 82, 818-835. doi: 10.1111/j.1365-2958.2011.07863.x
    • (2011) Mol. Microbiol. , vol.82 , pp. 818-835
    • Uebe, R.1    Junge, K.2    Henn, V.3    Poxleitner, G.4    Katzmann, E.5    Plitzko, J.M.6
  • 99
    • 0033749209 scopus 로고    scopus 로고
    • Properties and functions of diacylglycerol kinases
    • doi: 10.1016/S0898-6568(00)00113-3
    • Van Blitterswijk, W. J., and Houssa, B. (2000). Properties and functions of diacylglycerol kinases. Cell. Signal. 12, 595-605. doi: 10.1016/S0898-6568(00)00113-3
    • (2000) Cell. Signal. , vol.12 , pp. 595-605
    • Van Blitterswijk, W.J.1    Houssa, B.2
  • 100
    • 79953153131 scopus 로고    scopus 로고
    • Extensions of PDZ domains as important structural and functional elements
    • doi: 10.1007/s13238-010-0099-6
    • Wang, C. K., Pan, L., Chen, J., and Zhang, M. (2010). Extensions of PDZ domains as important structural and functional elements. Protein Cell 1, 737-751. doi: 10.1007/s13238-010-0099-6
    • (2010) Protein Cell , vol.1 , pp. 737-751
    • Wang, C.K.1    Pan, L.2    Chen, J.3    Zhang, M.4
  • 101
    • 0035486722 scopus 로고    scopus 로고
    • A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria
    • doi: 10.1128/AEM.67.10.4573-4582.2001
    • Wawer, C., Tebo, B. M., Gru, K., and Schu, D. (2001). A large gene cluster encoding several magnetosome proteins is conserved in different species of magnetotactic bacteria. Appl. Environ. Microbiol. 67, 4573-4582. doi: 10.1128/AEM.67.10.4573-4582.2001
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4573-4582
    • Wawer, C.1    Tebo, B.M.2    Gru, K.3    Schu, D.4
  • 102
    • 77952712556 scopus 로고    scopus 로고
    • Visualization and structural analysis of the bacterial magnetic organelle magnetosome using atomic force microscopy
    • doi: 10.1073/pnas.1001870107
    • Yamamoto, D., Taoka, A., Uchihashi, T., Sasaki, H., Watanabe, H., Ando, T., et al. (2010). Visualization and structural analysis of the bacterial magnetic organelle magnetosome using atomic force microscopy. Proc. Natl. Acad. Sci. U.S.A. 107, 9382-9387. doi: 10.1073/pnas.1001870107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9382-9387
    • Yamamoto, D.1    Taoka, A.2    Uchihashi, T.3    Sasaki, H.4    Watanabe, H.5    Ando, T.6
  • 103
    • 77957259375 scopus 로고    scopus 로고
    • mamO and mamE genes are essential for magnetosome crystal biomineralization in Magnetospirillum gryphiswaldense MSR-1
    • doi: 10.1016/j.resmic.2010.07.002
    • Yang, W., Li, R., Peng, T., Zhang, Y., Jiang, W., Li, Y., et al. (2010). mamO and mamE genes are essential for magnetosome crystal biomineralization in Magnetospirillum gryphiswaldense MSR-1. Res. Microbiol. 161, 701-705. doi: 10.1016/j.resmic.2010.07.002
    • (2010) Res. Microbiol. , vol.161 , pp. 701-705
    • Yang, W.1    Li, R.2    Peng, T.3    Zhang, Y.4    Jiang, W.5    Li, Y.6
  • 104
    • 84868508259 scopus 로고    scopus 로고
    • Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein
    • doi: 10.1016/j.jsb.2012.08.001
    • Zeytuni, N., Baran, D., Davidov, G., and Zarivach, R. (2012). Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA. J. Struct. Biol. 180, 479-487. doi: 10.1016/j.jsb.2012.08.001
    • (2012) MamA. J. Struct. Biol. , vol.180 , pp. 479-487
    • Zeytuni, N.1    Baran, D.2    Davidov, G.3    Zarivach, R.4
  • 105
    • 80052011286 scopus 로고    scopus 로고
    • Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly
    • doi: 10.1073/pnas.1103367108
    • Zeytuni, N., Ozyamak, E., Ben-Harush, K., Davidov, G., Levin, M., Gat, Y., and Moyal, T. (2011). Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly. Proc. Natl. Acad. Sci. U.S.A. 108, E480-E487. doi: 10.1073/pnas.1103367108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Zeytuni, N.1    Ozyamak, E.2    Ben-Harush, K.3    Davidov, G.4    Levin, M.5    Gat, Y.6    Moyal, T.7
  • 106
    • 34547559252 scopus 로고    scopus 로고
    • Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain
    • Zhang, Y., Appleton, B. A., Wu, P., Wiesmann, C., and Sidhu, S. S. (2007). Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain. 16, 1738-1750.
    • (2007) , vol.16 , pp. 1738-1750
    • Zhang, Y.1    Appleton, B.A.2    Wu, P.3    Wiesmann, C.4    Sidhu, S.S.5


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