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Volumn 2013, Issue , 2013, Pages

The nitrosopumilus maritimus cdvb, but not FtsZ, assembles into polymers

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; POLYMER; TUBULIN;

EID: 84880155009     PISSN: 14723646     EISSN: None     Source Type: Journal    
DOI: 10.1155/2013/104147     Document Type: Article
Times cited : (14)

References (44)
  • 1
    • 0030006337 scopus 로고    scopus 로고
    • An archaebacterial homologue of the essential eubacterial cell division protein FtsZ
    • 2-s2.0-0030006337 10.1073/pnas.93.13.6726
    • Baumann P., Jackson S. P., An archaebacterial homologue of the essential eubacterial cell division protein FtsZ. Proceedings of the National Academy of Sciences of the United States of America 1996 93 13 6726 6730 2-s2.0-0030006337 10.1073/pnas.93.13.6726
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.13 , pp. 6726-6730
    • Baumann, P.1    Jackson, S.P.2
  • 2
    • 0029864056 scopus 로고    scopus 로고
    • Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: Implications for the evolution of FtsZ and tubulin
    • 2-s2.0-0029864056
    • Margolin W., Wang R., Kumar M., Isolation of an ftsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. Journal of Bacteriology 1996 178 5 1320 1327 2-s2.0-0029864056
    • (1996) Journal of Bacteriology , vol.178 , Issue.5 , pp. 1320-1327
    • Margolin, W.1    Wang, R.2    Kumar, M.3
  • 3
    • 0033985478 scopus 로고    scopus 로고
    • The ftsZ gene of Haloferax mediterranei: Sequence, conserved gene order, and visualization of the FtsZ ring
    • 2-s2.0-0033985478 10.1016/S0378-1119(99)00517-X
    • Poplawski A., Gullbrand B., Bernander R., The ftsZ gene of Haloferax mediterranei: sequence, conserved gene order, and visualization of the FtsZ ring. Gene 2000 242 1-2 357 367 2-s2.0-0033985478 10.1016/S0378-1119(99)00517-X
    • (2000) Gene , vol.242 , Issue.1-2 , pp. 357-367
    • Poplawski, A.1    Gullbrand, B.2    Bernander, R.3
  • 4
    • 0029743706 scopus 로고    scopus 로고
    • FtsZ ring: The eubacterial division apparatus conserved in archaebacteria
    • 2-s2.0-0029743706
    • Wang X., Lutkenhaus J., FtsZ ring: the eubacterial division apparatus conserved in archaebacteria. Molecular Microbiology 1996 21 2 313 319 2-s2.0-0029743706
    • (1996) Molecular Microbiology , vol.21 , Issue.2 , pp. 313-319
    • Wang, X.1    Lutkenhaus, J.2
  • 6
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • 2-s2.0-58149230938 10.1126/science.1165322
    • Samson R. Y., Obita T., Freund S. M., Williams R. L., Bell S. D., A role for the ESCRT system in cell division in archaea. Science 2008 322 5908 1710 1713 2-s2.0-58149230938 10.1126/science.1165322
    • (2008) Science , vol.322 , Issue.5908 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3    Williams, R.L.4    Bell, S.D.5
  • 7
    • 78651468723 scopus 로고    scopus 로고
    • Molecular and structural basis of ESCRT-III recruitment to membranes during Archaeal cell division
    • 2-s2.0-78651468723 10.1016/j.molcel.2010.12.018
    • Samson R. Y., Obita T., Hodgson B., Shaw M. K., Chong P. L. G., Williams R. L., Bell S. D., Molecular and structural basis of ESCRT-III recruitment to membranes during Archaeal cell division. Molecular Cell 2011 41 2 186 196 2-s2.0-78651468723 10.1016/j.molcel.2010.12.018
    • (2011) Molecular Cell , vol.41 , Issue.2 , pp. 186-196
    • Samson, R.Y.1    Obita, T.2    Hodgson, B.3    Shaw, M.K.4    Chong, P.L.G.5    Williams, R.L.6    Bell, S.D.7
  • 8
    • 0036696804 scopus 로고    scopus 로고
    • ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting
    • 2-s2.0-0036696804 10.1016/S1534-5807(02)00220-4
    • Babst M., Katzmann D. J., Estepa-Sabal E. J., Meerloo T., Emr S. D., ESCRT-III: an endosome-associated heterooligomeric protein complex required for MVB sorting. Developmental Cell 2002 3 2 271 282 2-s2.0-0036696804 10.1016/S1534-5807(02)00220-4
    • (2002) Developmental Cell , vol.3 , Issue.2 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 10
    • 54949088988 scopus 로고    scopus 로고
    • Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55
    • 2-s2.0-54949088988 10.1126/science.1162042
    • Hyung H. L., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J. H., Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science 2008 322 5901 576 580 2-s2.0-54949088988 10.1126/science.1162042
    • (2008) Science , vol.322 , Issue.5901 , pp. 576-580
    • Hyung, H.L.1    Elia, N.2    Ghirlando, R.3    Lippincott-Schwartz, J.4    Hurley, J.H.5
  • 11
    • 34948911522 scopus 로고    scopus 로고
    • Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis
    • 2-s2.0-34948911522 10.1038/sj.emboj.7601850
    • Morita E., Sandrin V., Chung H. Y., Morham S. G., Gygi S. P., Rodesch C. K., Sundquist W. I., Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO Journal 2007 26 19 4215 4227 2-s2.0-34948911522 10.1038/sj.emboj.7601850
    • (2007) EMBO Journal , vol.26 , Issue.19 , pp. 4215-4227
    • Morita, E.1    Sandrin, V.2    Chung, H.Y.3    Morham, S.G.4    Gygi, S.P.5    Rodesch, C.K.6    Sundquist, W.I.7
  • 12
    • 39149118031 scopus 로고    scopus 로고
    • Mesophilic crenarchaeota: Proposal for a third archaeal phylum, the Thaumarchaeota
    • 2-s2.0-39149118031 10.1038/nrmicro1852
    • Brochier-Armanet C., Boussau B., Gribaldo S., Forterre P., Mesophilic crenarchaeota: proposal for a third archaeal phylum, the Thaumarchaeota. Nature Reviews Microbiology 2008 6 3 245 252 2-s2.0-39149118031 10.1038/nrmicro1852
    • (2008) Nature Reviews Microbiology , vol.6 , Issue.3 , pp. 245-252
    • Brochier-Armanet, C.1    Boussau, B.2    Gribaldo, S.3    Forterre, P.4
  • 14
    • 25644435673 scopus 로고    scopus 로고
    • Isolation of an autotrophic ammonia-oxidizing marine archaeon
    • 2-s2.0-25644435673 10.1038/nature03911
    • Könneke M., Bernhard A. E., De La Torre J. R., Walker C. B., Waterbury J. B., Stahl D. A., Isolation of an autotrophic ammonia-oxidizing marine archaeon. Nature 2005 437 7058 543 546 2-s2.0-25644435673 10.1038/nature03911
    • (2005) Nature , vol.437 , Issue.7058 , pp. 543-546
    • Könneke, M.1    Bernhard, A.E.2    De La Torre, J.R.3    Walker, C.B.4    Waterbury, J.B.5    Stahl, D.A.6
  • 15
    • 70350052417 scopus 로고    scopus 로고
    • Ammonia oxidation kinetics determine niche separation of nitrifying Archaea and Bacteria
    • 2-s2.0-70350052417 10.1038/nature08465
    • Martens-Habbena W., Berube P. M., Urakawa H., De La Torre J. R., Stahl D. A., Ammonia oxidation kinetics determine niche separation of nitrifying Archaea and Bacteria. Nature 2009 461 7266 976 979 2-s2.0-70350052417 10.1038/nature08465
    • (2009) Nature , vol.461 , Issue.7266 , pp. 976-979
    • Martens-Habbena, W.1    Berube, P.M.2    Urakawa, H.3    De La Torre, J.R.4    Stahl, D.A.5
  • 17
    • 80054845081 scopus 로고    scopus 로고
    • Cdv-based cell division and cell cycle organization in the thaumarchaeon Nitrosopumilus maritimus
    • 10.1111/j.1365-2958.2011.07834.x
    • Pelve E. A., Lindas A. C., Martens-Habbena W., de la Torre J. R., Stahl D. A., Cdv-based cell division and cell cycle organization in the thaumarchaeon Nitrosopumilus maritimus. Molecular Microbiology 2011 82 555 566 10.1111/j.1365-2958.2011.07834.x
    • (2011) Molecular Microbiology , vol.82 , pp. 555-566
    • Pelve, E.A.1    Lindas, A.C.2    Martens-Habbena, W.3    De La Torre, J.R.4    Stahl, D.A.5
  • 18
    • 84869509861 scopus 로고    scopus 로고
    • Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms
    • 10.1002/cm.21082
    • Balasubramanian M. K., Srinivasan R., Huang Y., Ng K. H., Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms. Cytoskeleton 2012 69 11 942 956 10.1002/cm.21082
    • (2012) Cytoskeleton , vol.69 , Issue.11 , pp. 942-956
    • Balasubramanian, M.K.1    Srinivasan, R.2    Huang, Y.3    Ng, K.H.4
  • 19
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • 2-s2.0-78650078263 10.1128/MMBR.00021-10
    • Erickson H. P., Anderson D. E., Osawa M., FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiology and Molecular Biology Reviews 2010 74 4 504 528 2-s2.0-78650078263 10.1128/MMBR.00021-10
    • (2010) Microbiology and Molecular Biology Reviews , vol.74 , Issue.4 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 20
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • 2-s2.0-27644540151 10.1038/nrm1745
    • Margolin W., FtsZ and the division of prokaryotic cells and organelles. Nature Reviews Molecular Cell Biology 2005 6 11 862 871 2-s2.0-27644540151 10.1038/nrm1745
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 862-871
    • Margolin, W.1
  • 21
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • 2-s2.0-44049091371 10.1126/science.1154520
    • Osawa M., Anderson D. E., Erickson H. P., Reconstitution of contractile FtsZ rings in liposomes. Science 2008 320 5877 792 794 2-s2.0-44049091371 10.1126/science.1154520
    • (2008) Science , vol.320 , Issue.5877 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 22
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • 2-s2.0-75749110614 10.1016/j.ceb.2009.11.010
    • Pollard T. D., Mechanics of cytokinesis in eukaryotes. Current Opinion in Cell Biology 2010 22 1 50 56 2-s2.0-75749110614 10.1016/j.ceb.2009.11.010
    • (2010) Current Opinion in Cell Biology , vol.22 , Issue.1 , pp. 50-56
    • Pollard, T.D.1
  • 23
    • 80052614055 scopus 로고    scopus 로고
    • The evolution of the cytoskeleton
    • 10.1083/jcb.201102065
    • Wickstead B., Gull K., The evolution of the cytoskeleton. The Journal of Cell Biology 2011 194 4 513 525 10.1083/jcb.201102065
    • (2011) The Journal of Cell Biology , vol.194 , Issue.4 , pp. 513-525
    • Wickstead, B.1    Gull, K.2
  • 24
    • 33846637436 scopus 로고    scopus 로고
    • Filament formation of the Escherichia coli actin-related protein, MreB, in fission yeast
    • 2-s2.0-33846637436 10.1016/j.cub.2006.11.069
    • Srinivasan R., Mishra M., Murata-Hori M., Balasubramanian M. K., Filament formation of the Escherichia coli actin-related protein, MreB, in fission yeast. Current Biology 2007 17 3 266 272 2-s2.0-33846637436 10.1016/j.cub.2006. 11.069
    • (2007) Current Biology , vol.17 , Issue.3 , pp. 266-272
    • Srinivasan, R.1    Mishra, M.2    Murata-Hori, M.3    Balasubramanian, M.K.4
  • 25
    • 46249087769 scopus 로고    scopus 로고
    • The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast
    • 2-s2.0-46249087769 10.1101/gad.1660908
    • Srinivasan R., Mishra M., Wu L., Yin Z., Balasubramanian M. K., The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast. Genes and Development 2008 22 13 1741 1746 2-s2.0-46249087769 10.1101/gad.1660908
    • (2008) Genes and Development , vol.22 , Issue.13 , pp. 1741-1746
    • Srinivasan, R.1    Mishra, M.2    Wu, L.3    Yin, Z.4    Balasubramanian, M.K.5
  • 26
    • 81155123699 scopus 로고    scopus 로고
    • Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane
    • 10.1074/jbc.M111.283671
    • Bodon G., Chassefeyre R., Pernet-Gallay K., Martinelli N., Effantin G., Charged multivesicular body protein 2B (CHMP2B) of the endosomal sorting complex required for transport-III (ESCRT-III) polymerizes into helical structures deforming the plasma membrane. The Journal of Biological Chemistry 2011 286 40276 40286 10.1074/jbc.M111.283671
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 40276-40286
    • Bodon, G.1    Chassefeyre, R.2    Pernet-Gallay, K.3    Martinelli, N.4    Effantin, G.5
  • 27
    • 80053206906 scopus 로고    scopus 로고
    • Association of the endosomal sorting complex ESCRT-II with the Vps20 subunit of ESCRT-III generates a curvature-sensitive complex capable of nucleating ESCRT-III filaments
    • 10.1074/jbc.M111.266411
    • Fyfe I., Schuh A. L., Edwardson J. M., Audhya A., Association of the endosomal sorting complex ESCRT-II with the Vps20 subunit of ESCRT-III generates a curvature-sensitive complex capable of nucleating ESCRT-III filaments. The Journal of Biological Chemistry 2011 286 34262 34270 10.1074/jbc.M111.266411
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 34262-34270
    • Fyfe, I.1    Schuh, A.L.2    Edwardson, J.M.3    Audhya, A.4
  • 29
    • 79953161074 scopus 로고    scopus 로고
    • Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments
    • 2-s2.0-79953161074 10.1126/science.1201847
    • Guizetti J., Schermelleh L., Mäntler J., Maar S., Poser I., Leonhardt H., Müller-Reichert T., Gerlich D. W., Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments. Science 2011 331 6024 1616 1620 2-s2.0-79953161074 10.1126/science.1201847
    • (2011) Science , vol.331 , Issue.6024 , pp. 1616-1620
    • Guizetti, J.1    Schermelleh, L.2    Mäntler, J.3    Maar, S.4    Poser, I.5    Leonhardt, H.6    Müller-Reichert, T.7    Gerlich, D.W.8
  • 30
    • 38749152820 scopus 로고    scopus 로고
    • Plasma membrane deformation by circular arrays of ESCRT-III protein filaments
    • 2-s2.0-38749152820 10.1083/jcb.200707031
    • Hanson P. I., Roth R., Lin Y., Heuser J. E., Plasma membrane deformation by circular arrays of ESCRT-III protein filaments. The Journal of Cell Biology 2008 180 2 389 402 2-s2.0-38749152820 10.1083/jcb.200707031
    • (2008) The Journal of Cell Biology , vol.180 , Issue.2 , pp. 389-402
    • Hanson, P.I.1    Roth, R.2    Lin, Y.3    Heuser, J.E.4
  • 31
    • 84867548612 scopus 로고    scopus 로고
    • The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices
    • 10.1016/j.cell.2012.08.039
    • Henne W. M., Buchkovich N. J., Zhao Y., Emr S. D., The endosomal sorting complex ESCRT-II mediates the assembly and architecture of ESCRT-III helices. Cell 2012 151 356 371 10.1016/j.cell.2012.08.039
    • (2012) Cell , vol.151 , pp. 356-371
    • Henne, W.M.1    Buchkovich, N.J.2    Zhao, Y.3    Emr, S.D.4
  • 32
    • 51149106799 scopus 로고    scopus 로고
    • Helical structures of ESCRT-III are disassembled by VPS4
    • 2-s2.0-51149106799 10.1126/science.1161070
    • Lata S., Schoehn G., Jain A., Pires R., Piehler J., Gottlinger H. G., Weissenhorn W., Helical structures of ESCRT-III are disassembled by VPS4. Science 2008 321 5894 1354 1357 2-s2.0-51149106799 10.1126/science.1161070
    • (2008) Science , vol.321 , Issue.5894 , pp. 1354-1357
    • Lata, S.1    Schoehn, G.2    Jain, A.3    Pires, R.4    Piehler, J.5    Gottlinger, H.G.6    Weissenhorn, W.7
  • 34
    • 58149103425 scopus 로고    scopus 로고
    • Functional Reconstitution of ESCRT-III assembly and disassembly
    • 2-s2.0-58149103425 10.1016/j.cell.2008.11.013
    • Saksena S., Wahlman J., Teis D., Johnson A. E., Emr S. D., Functional Reconstitution of ESCRT-III assembly and disassembly. Cell 2009 136 1 97 109 2-s2.0-58149103425 10.1016/j.cell.2008.11.013
    • (2009) Cell , vol.136 , Issue.1 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 35
    • 79960079427 scopus 로고    scopus 로고
    • Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB
    • 2-s2.0-79960079427 10.1371/journal.pone.0021921 e21921
    • Moriscot C., Gribaldo S., Jault J. M., Krupovic M., Arnaud J., Jamin M., Schoehn G., Forterre P., Weissenhorn W., Renesto P., Crenarchaeal CdvA forms double-helical filaments containing DNA and interacts with ESCRT-III-like CdvB. PLoS ONE 2011 6 7 2-s2.0-79960079427 10.1371/journal.pone.0021921 e21921
    • (2011) PLoS ONE , vol.6 , Issue.7
    • Moriscot, C.1    Gribaldo, S.2    Jault, J.M.3    Krupovic, M.4    Arnaud, J.5    Jamin, M.6    Schoehn, G.7    Forterre, P.8    Weissenhorn, W.9    Renesto, P.10
  • 36
    • 34447527768 scopus 로고    scopus 로고
    • Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain
    • 2-s2.0-34447527768 10.1111/j.1600-0854.2007.00584.x
    • Shim S., Kimpler L. A., Hanson P. I., Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain. Traffic 2007 8 8 1068 1079 2-s2.0-34447527768 10.1111/j.1600-0854.2007. 00584.x
    • (2007) Traffic , vol.8 , Issue.8 , pp. 1068-1079
    • Shim, S.1    Kimpler, L.A.2    Hanson, P.I.3
  • 37
    • 80054833492 scopus 로고    scopus 로고
    • Split decision: A thaumarchaeon encoding both FtsZ and Cdv cell division proteins chooses Cdv for cytokinesis
    • 10.1111/j.1365-2958.2011.07833.x
    • Busiek K. K., Margolin W., Split decision: a thaumarchaeon encoding both FtsZ and Cdv cell division proteins chooses Cdv for cytokinesis. Molecular Microbiology 2011 82 3 535 538 10.1111/j.1365-2958.2011.07833.x
    • (2011) Molecular Microbiology , vol.82 , Issue.3 , pp. 535-538
    • Busiek, K.K.1    Margolin, W.2
  • 38
    • 0035209228 scopus 로고    scopus 로고
    • Assembly of an FtsZ mutant deficient in GTpase activity has implications for FtsZ assembly and the role of the Z ring in cell division
    • 2-s2.0-0035209228 10.1128/JB.183.24.7190-7197.2001
    • Mukherjee A., Saez C., Lutkenhaus J., Assembly of an FtsZ mutant deficient in GTpase activity has implications for FtsZ assembly and the role of the Z ring in cell division. Journal of Bacteriology 2001 183 24 7190 7197 2-s2.0-0035209228 10.1128/JB.183.24.7190-7197.2001
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7190-7197
    • Mukherjee, A.1    Saez, C.2    Lutkenhaus, J.3
  • 39
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
    • 2-s2.0-0037080162 10.1021/bi011370i
    • Scheffers D. J., De Wit J. G., Den Blaauwen T., Driessen A. J. M., GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 2002 41 2 521 529 2-s2.0-0037080162 10.1021/bi011370i
    • (2002) Biochemistry , vol.41 , Issue.2 , pp. 521-529
    • Scheffers, D.J.1    De Wit, J.G.2    Den Blaauwen, T.3    Driessen, A.J.M.4
  • 40
    • 67650641167 scopus 로고    scopus 로고
    • Cell division and the ESCRT complex: A surprise from the Archaea
    • 2-s2.0-67650641167
    • Ettema T. J. G., Bernander R., Cell division and the ESCRT complex: a surprise from the Archaea. Communitative and Integrative Biology 2009 2 2 86 88 2-s2.0-67650641167
    • (2009) Communitative and Integrative Biology , vol.2 , Issue.2 , pp. 86-88
    • Ettema, T.J.G.1    Bernander, R.2
  • 41
    • 58149177342 scopus 로고    scopus 로고
    • Proteomic analysis of secreted membrane vesicles of archaeal Sulfolobus species reveals the presence of endosome sorting complex components
    • 2-s2.0-58149177342 10.1007/s00792-008-0199-x
    • Ellen A. F., Albers S. V., Huibers W., Pitcher A., Hobel C. F. V., Schwarz H., Folea M., Schouten S., Boekema E. J., Poolman B., Driessen A. J. M., Proteomic analysis of secreted membrane vesicles of archaeal Sulfolobus species reveals the presence of endosome sorting complex components. Extremophiles 2009 13 1 67 79 2-s2.0-58149177342 10.1007/s00792-008-0199-x
    • (2009) Extremophiles , vol.13 , Issue.1 , pp. 67-79
    • Ellen, A.F.1    Albers, S.V.2    Huibers, W.3    Pitcher, A.4    Hobel, C.F.V.5    Schwarz, H.6    Folea, M.7    Schouten, S.8    Boekema, E.J.9    Poolman, B.10    Driessen, A.J.M.11
  • 42
    • 0027441494 scopus 로고
    • TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility
    • 2-s2.0-0027441494 10.1016/0378-1119(93)90552-E
    • Basi G., Schmid E., Maundrell K., TATA box mutations in the Schizosaccharomyces pombe nmt1 promoter affect transcription efficiency but not the transcription start point or thiamine repressibility. Gene 1993 123 1 131 136 2-s2.0-0027441494 10.1016/0378-1119(93)90552-E
    • (1993) Gene , vol.123 , Issue.1 , pp. 131-136
    • Basi, G.1    Schmid, E.2    Maundrell, K.3
  • 43
    • 77950539826 scopus 로고    scopus 로고
    • Plasmid construction using recombination activity in the fission yeast Schizosaccharomyces pombe
    • 2-s2.0-77950539826 10.1371/journal.pone.0009652 e9652
    • Chino A., Watanabe K., Moriya H., Plasmid construction using recombination activity in the fission yeast Schizosaccharomyces pombe. PLoS ONE 2010 5 3 2-s2.0-77950539826 10.1371/journal.pone.0009652 e9652
    • (2010) PLoS ONE , vol.5 , Issue.3
    • Chino, A.1    Watanabe, K.2    Moriya, H.3
  • 44
    • 0026025891 scopus 로고
    • Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
    • 2-s2.0-0026025891 10.1016/0076-6879(91)94059-L
    • Moreno S., Klar A., Nurse P., Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Methods in Enzymology 1991 194 795 823 2-s2.0-0026025891 10.1016/0076-6879(91)94059-L
    • (1991) Methods in Enzymology , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3


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