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Volumn 290, Issue 9, 2015, Pages 5341-5353

In situ localization of N and C termini of subunits of the flagellar nexin-dynein regulatory complex (N-DRC) using SNAP tag and cryo-electron tomography

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ELECTRIC IMPEDANCE TOMOGRAPHY; FLUORESCENCE MICROSCOPY; MACROMOLECULES; TOMOGRAPHY;

EID: 84923862726     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.626556     Document Type: Article
Times cited : (42)

References (44)
  • 1
    • 33847196039 scopus 로고    scopus 로고
    • Electron microscopy of microtubulebased cytoskeletal machinery
    • Hoenger, A., and Nicastro, D. (2007) Electron microscopy of microtubulebased cytoskeletal machinery. Methods Cell Biol. 79, 437-462
    • (2007) Methods Cell Biol. , vol.79 , pp. 437-462
    • Hoenger, A.1    Nicastro, D.2
  • 3
    • 84857616757 scopus 로고    scopus 로고
    • Electron tomography of cells
    • Gan, L., and Jensen, G. J. (2012) Electron tomography of cells. Q. Rev. Biophys. 45, 27-56
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 27-56
    • Gan, L.1    Jensen, G.J.2
  • 4
    • 0020082250 scopus 로고
    • Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function
    • Huang, B., Ramanis, Z., and Luck, D. J. (1982) Suppressor mutations in Chlamydomonas reveal a regulatory mechanism for flagellar function. Cell 28, 115-124
    • (1982) Cell , vol.28 , pp. 115-124
    • Huang, B.1    Ramanis, Z.2    Luck, D.J.3
  • 6
    • 84876552918 scopus 로고    scopus 로고
    • The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes
    • Bower, R., Tritschler, D., Vanderwaal, K., Perrone, C. A., Mueller, J., Fox, L., Sale, W. S., and Porter, M. E. (2013) The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes. Mol. Biol. Cell 24, 1134-1152
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1134-1152
    • Bower, R.1    Tritschler, D.2    Vanderwaal, K.3    Perrone, C.A.4    Mueller, J.5    Fox, L.6    Sale, W.S.7    Porter, M.E.8
  • 7
    • 0028170976 scopus 로고
    • Components of a "dynein regulatory complex" are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella
    • Gardner, L. C., O'Toole, E., Perrone, C. A., Giddings, T., and Porter, M. E. (1994) Components of a "dynein regulatory complex" are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella. J. Cell Biol. 127, 1311-1325
    • (1994) J. Cell Biol. , vol.127 , pp. 1311-1325
    • Gardner, L.C.1    O'Toole, E.2    Perrone, C.A.3    Giddings, T.4    Porter, M.E.5
  • 12
    • 84866371836 scopus 로고    scopus 로고
    • Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme
    • Bui, K. H., Yagi, T., Yamamoto, R., Kamiya, R., and Ishikawa, T. (2012) Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme. J. Cell Biol. 198, 913-925
    • (2012) J. Cell Biol. , vol.198 , pp. 913-925
    • Bui, K.H.1    Yagi, T.2    Yamamoto, R.3    Kamiya, R.4    Ishikawa, T.5
  • 13
    • 74049111826 scopus 로고    scopus 로고
    • The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella
    • Heuser, T., Raytchev, M., Krell, J., Porter, M. E., and Nicastro, D. (2009) The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella. J. Cell Biol. 187, 921-933
    • (2009) J. Cell Biol. , vol.187 , pp. 921-933
    • Heuser, T.1    Raytchev, M.2    Krell, J.3    Porter, M.E.4    Nicastro, D.5
  • 15
    • 34548627873 scopus 로고    scopus 로고
    • Concatenated metallothionein as a clonable gold label for electron microscopy
    • Mercogliano, C. P., and DeRosier, D. J. (2007) Concatenated metallothionein as a clonable gold label for electron microscopy. J. Struct. Biol. 160, 70-82
    • (2007) J. Struct. Biol. , vol.160 , pp. 70-82
    • Mercogliano, C.P.1    DeRosier, D.J.2
  • 16
    • 84883455230 scopus 로고    scopus 로고
    • Novel structural labeling method using cryo-electron tomography and biotin-streptavidin system
    • Oda, T., and Kikkawa, M. (2013) Novel structural labeling method using cryo-electron tomography and biotin-streptavidin system. J. Struct. Biol. 183, 305-311
    • (2013) J. Struct. Biol. , vol.183 , pp. 305-311
    • Oda, T.1    Kikkawa, M.2
  • 17
    • 59149094180 scopus 로고    scopus 로고
    • Visualization of proteins in intact cells with a clonable tag for electron microscopy
    • Diestra, E., Fontana, J., Guichard, P., Marco, S., and Risco, C. (2009) Visualization of proteins in intact cells with a clonable tag for electron microscopy. J. Struct. Biol. 165, 157-168
    • (2009) J. Struct. Biol. , vol.165 , pp. 157-168
    • Diestra, E.1    Fontana, J.2    Guichard, P.3    Marco, S.4    Risco, C.5
  • 19
    • 79955504165 scopus 로고    scopus 로고
    • A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms
    • Shu, X., Lev-Ram, V., Deerinck, T. J., Qi, Y., Ramko, E. B., Davidson, M. W., Jin, Y., Ellisman, M. H., and Tsien, R. Y. (2011) A genetically encoded tag for correlated light and electron microscopy of intact cells, tissues, and organisms. PLoS Biol. 9, e1001041
    • (2011) PLoS Biol. , vol.9 , pp. e1001041
    • Shu, X.1    Lev-Ram, V.2    Deerinck, T.J.3    Qi, Y.4    Ramko, E.B.5    Davidson, M.W.6    Jin, Y.7    Ellisman, M.H.8    Tsien, R.Y.9
  • 20
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion pro-teins with small molecules in vivo
    • Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H., Vogel, H., and Johnsson, K. (2003) A general method for the covalent labeling of fusion pro-teins with small molecules in vivo. Nat. Biotechnol. 21, 86-89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 21
    • 84907369495 scopus 로고    scopus 로고
    • Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells
    • Bosch, P. J., Corrêa, I. R., Jr., Sonntag, M. H., Ibach, J., Brunsveld, L., Kanger, J. S., and Subramaniam, V. (2014) Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells. Biophys. J. 107, 803-814
    • (2014) Biophys. J. , vol.107 , pp. 803-814
    • Bosch, P.J.1    Corrêa, I.R.2    Sonntag, M.H.3    Ibach, J.4    Brunsveld, L.5    Kanger, J.S.6    Subramaniam, V.7
  • 22
    • 84901044155 scopus 로고    scopus 로고
    • Live-cell reporters for fluorescence imaging
    • Corrêa, I. R., Jr. (2014) Live-cell reporters for fluorescence imaging. Curr. Opin. Chem. Biol. 20, 36-45
    • (2014) Curr. Opin. Chem. Biol. , vol.20 , pp. 36-45
    • Corrêa, I.R.1
  • 24
    • 0037810853 scopus 로고    scopus 로고
    • A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product
    • Rupp, G., and Porter, M. E. (2003) A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product. J. Cell Biol. 162, 47-57
    • (2003) J. Cell Biol. , vol.162 , pp. 47-57
    • Rupp, G.1    Porter, M.E.2
  • 25
    • 0035904396 scopus 로고    scopus 로고
    • A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii
    • Sizova, I., Fuhrmann, M., and Hegemann, P. (2001) A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii. Gene 277, 221-229
    • (2001) Gene , vol.277 , pp. 221-229
    • Sizova, I.1    Fuhrmann, M.2    Hegemann, P.3
  • 27
    • 0036967786 scopus 로고    scopus 로고
    • An engineered Streptomyces hygroscopicus aph 7″gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii
    • Berthold, P., Schmitt, R., and Mages, W. (2002) An engineered Streptomyces hygroscopicus aph 7″gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii. Protist 153, 401-412
    • (2002) Protist , vol.153 , pp. 401-412
    • Berthold, P.1    Schmitt, R.2    Mages, W.3
  • 28
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii
    • Gorman, D. S., and Levine, R. P. (1965) Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. 54, 1665-1669
    • (1965) Proc. Natl. Acad. Sci. , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 29
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • Witman, G. B. (1986) Isolation of Chlamydomonas flagella and flagellar axonemes. Methods Enzymol. 134, 280-290
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.B.1
  • 30
    • 77954673280 scopus 로고    scopus 로고
    • Genetic and phenotypic analysis of flagellar assembly mutants in Chlamydomonas reinhardtii
    • Iomini, C., Till, J. E., and Dutcher, S. K. (2009) Genetic and phenotypic analysis of flagellar assembly mutants in Chlamydomonas reinhardtii. Methods Cell Biol. 93, 121-143
    • (2009) Methods Cell Biol. , vol.93 , pp. 121-143
    • Iomini, C.1    Till, J.E.2    Dutcher, S.K.3
  • 31
    • 12844261585 scopus 로고    scopus 로고
    • Dimeric novel HSP40 is incorporated into the radial spoke complex during the assembly process in flagella
    • Yang, C., Compton, M. M., and Yang, P. (2005) Dimeric novel HSP40 is incorporated into the radial spoke complex during the assembly process in flagella. Mol. Biol. Cell 16, 637-648
    • (2005) Mol. Biol. Cell , vol.16 , pp. 637-648
    • Yang, C.1    Compton, M.M.2    Yang, P.3
  • 33
    • 77954685629 scopus 로고    scopus 로고
    • Cryo-electron microscope tomography to study axonemal organization
    • Nicastro, D. (2009) Cryo-electron microscope tomography to study axonemal organization. Methods Cell Biol. 91, 1-39
    • (2009) Methods Cell Biol. , vol.91 , pp. 1-39
    • Nicastro, D.1
  • 35
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. (2005) Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 36
    • 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
  • 37
    • 79960900012 scopus 로고    scopus 로고
    • Clustering and variance maps for cryo-electron tomography using wedge-masked differences
    • Heumann, J. M., Hoenger, A., and Mastronarde, D. N. (2011) Clustering and variance maps for cryo-electron tomography using wedge-masked differences. J. Struct. Biol. 175, 288-299
    • (2011) J. Struct. Biol. , vol.175 , pp. 288-299
    • Heumann, J.M.1    Hoenger, A.2    Mastronarde, D.N.3
  • 39
    • 0000313739 scopus 로고
    • Exact filters for general geometry three dimensional reconstruction
    • Harauz, G., and Van Heel, M. (1986) Exact filters for general geometry three dimensional reconstruction. Optik 73, 146-156
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    Van Heel, M.2
  • 40
    • 84895754343 scopus 로고    scopus 로고
    • Mechanosignaling between central apparatus and radial spokes controls axonemal dynein activity
    • Oda, T., Yanagisawa, H., Yagi, T., and Kikkawa, M. (2014) Mechanosignaling between central apparatus and radial spokes controls axonemal dynein activity. J. Cell Biol. 204, 807-819
    • (2014) J. Cell Biol. , vol.204 , pp. 807-819
    • Oda, T.1    Yanagisawa, H.2    Yagi, T.3    Kikkawa, M.4
  • 41
    • 84910633774 scopus 로고    scopus 로고
    • Cilia and flagella. A molecular ruler determines the repeat length in eukaryotic cilia and flagella
    • Oda, T., Yanagisawa, H., Kamiya, R., and Kikkawa, M. (2014) Cilia and flagella. A molecular ruler determines the repeat length in eukaryotic cilia and flagella. Science 346, 857-860
    • (2014) Science , vol.346 , pp. 857-860
    • Oda, T.1    Yanagisawa, H.2    Kamiya, R.3    Kikkawa, M.4
  • 42
    • 84923928307 scopus 로고    scopus 로고
    • Detailed structural and biochemical characterization of the nexin-dynein regulatory complex
    • Oda, T., Yanagisawa, H., and Kikkawa, M. (2014) Detailed structural and biochemical characterization of the nexin-dynein regulatory complex. Mol. Biol. Cell mbc.E14-09-1367
    • (2014) Mol. Biol. Cel , vol.E14 , Issue.9 , pp. 1367
    • Oda, T.1    Yanagisawa, H.2    Kikkawa, M.3
  • 43
    • 0029043047 scopus 로고
    • Electron microscopic visualization of insulin translocation into the cytoplasm and nuclei of intact H35 hepatoma cells using covalently linked Nanogoldinsulin
    • Shah, N., Zhang, S., Harada, S., Smith, R. M., and Jarett, L. (1995) Electron microscopic visualization of insulin translocation into the cytoplasm and nuclei of intact H35 hepatoma cells using covalently linked Nanogoldinsulin. Endocrinology 136, 2825-2835
    • (1995) Endocrinology , vol.136 , pp. 2825-2835
    • Shah, N.1    Zhang, S.2    Harada, S.3    Smith, R.M.4    Jarett, L.5
  • 44
    • 49449084062 scopus 로고    scopus 로고
    • Clathrin-dependent and independent endocytic pathways in tobacco protoplasts revealed by labelling with charged nanogold
    • Onelli, E., Prescianotto-Baschong, C., Caccianiga, M., and Moscatelli, A. (2008) Clathrin-dependent and independent endocytic pathways in tobacco protoplasts revealed by labelling with charged nanogold. J. Exp. Bot. 59, 3051-3068
    • (2008) J. Exp. Bot. , vol.59 , pp. 3051-3068
    • Onelli, E.1    Prescianotto-Baschong, C.2    Caccianiga, M.3    Moscatelli, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.