메뉴 건너뛰기




Volumn 188, Issue 10, 2006, Pages 3442-3448

Diffusion of green fluorescent protein in three cell environments in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN;

EID: 33646594697     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.10.3442-3448.2006     Document Type: Article
Times cited : (177)

References (26)
  • 1
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett, C. M. L., N. Ray, J. D. Thomas, C. Robinson, and A. Bolhuis. 2003. Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem. Biophys. Res. Commun. 304:279-284.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 279-284
    • Barrett, C.M.L.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 2
    • 0034697250 scopus 로고    scopus 로고
    • Subunit interactions in the twin-arginine translocase complex of Escherichia coli
    • Bolhuis, A., E. G. Bogsch, and C. Robinson. 2000. Subunit interactions in the twin-arginine translocase complex of Escherichia coli. FEBS Lett. 472:88-92.
    • (2000) FEBS Lett. , vol.472 , pp. 88-92
    • Bolhuis, A.1    Bogsch, E.G.2    Robinson, C.3
  • 3
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis, A., J. E. Mathers, J. D. Thomas, C. Barrett, and C. Robinson. 2001. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 276:20213-20219.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20213-20219
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.4    Robinson, C.5
  • 5
    • 0034009901 scopus 로고    scopus 로고
    • An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells
    • Cluzel, P., M. Surette, and S. Leibler. 2000. An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells. Science 287:1652-1654.
    • (2000) Science , vol.287 , pp. 1652-1654
    • Cluzel, P.1    Surette, M.2    Leibler, S.3
  • 6
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., R. H. Valdivia, and S. Falkow. 1996. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 7
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis, R. J. 2001. Macromolecular crowding: an important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 11:114-119.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 9
    • 0024740844 scopus 로고
    • Compartmentalization of the periplasm at cell division sites in Escherichia coli as shown by fluorescence photobleaching experiments
    • Foley, M., J. M. Brass, J. Birmingham, W. R. Cook, P. B. Garland, C. F. Higgins, and L. I. Rothfield. 1989. Compartmentalization of the periplasm at cell division sites in Escherichia coli as shown by fluorescence photobleaching experiments. Mol. Microbiol. 3:1329-1336.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1329-1336
    • Foley, M.1    Brass, J.M.2    Birmingham, J.3    Cook, W.R.4    Garland, P.B.5    Higgins, C.F.6    Rothfield, L.I.7
  • 10
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose P-BAD promoter
    • Guzman, L.-M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose P-BAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 11
    • 0028142423 scopus 로고
    • Lateral diffusion measurement at high spatial resolution by scanning microphotolysis in a confocal microscope
    • Kubitscheck, U., P. Wedekind, and R. Peters. 1994. Lateral diffusion measurement at high spatial resolution by scanning microphotolysis in a confocal microscope. Biophys. J. 67:948-956.
    • (1994) Biophys. J. , vol.67 , pp. 948-956
    • Kubitscheck, U.1    Wedekind, P.2    Peters, R.3
  • 12
    • 0036897884 scopus 로고    scopus 로고
    • Dynamic proteins in bacteria
    • Lutkenhaus, J. 2002. Dynamic proteins in bacteria. Curr. Opin. Microbiol. 5:548-552.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 548-552
    • Lutkenhaus, J.1
  • 13
    • 12344260570 scopus 로고    scopus 로고
    • Increasing complexity of the bacterial cytoskeleton
    • Møller-Jensen, J., and J. Löwe. 2005. Increasing complexity of the bacterial cytoskeleton. Curr. Opin. Cell Biol. 17:75-81.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 75-81
    • Møller-Jensen, J.1    Löwe, J.2
  • 14
    • 0031456377 scopus 로고    scopus 로고
    • Mobility of photosynthetic complexes in thylakoid membranes
    • Mullineaux, C. W., M. J. Tobin, and G. R. Jones. 1997. Mobility of photosynthetic complexes in thylakoid membranes. Nature 390:421-424.
    • (1997) Nature , vol.390 , pp. 421-424
    • Mullineaux, C.W.1    Tobin, M.J.2    Jones, G.R.3
  • 15
    • 0036615686 scopus 로고    scopus 로고
    • Probing the dynamics of photosynthetic membranes with fluorescence recovery after photobleaching
    • Mullineaux, C. W., and M. Sarcina. 2002. Probing the dynamics of photosynthetic membranes with fluorescence recovery after photobleaching. Trends Plant Sci. 7:237-240.
    • (2002) Trends Plant Sci. , vol.7 , pp. 237-240
    • Mullineaux, C.W.1    Sarcina, M.2
  • 16
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins-a putative bottleneck in heterologous expression
    • Opekarova, M., and W. Tanner. 2003. Specific lipid requirements of membrane proteins-a putative bottleneck in heterologous expression. Biochim. Biophys. Acta 1610:11-22.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 18
    • 0034804337 scopus 로고    scopus 로고
    • Reduced protein diffusion rate by cytoskeleton in vegetative and polarized Dictyostelium cells
    • Potma, E. O., W. P. de Boeij, L. Bosgraaf, J. Roelofs, P. J. M. van Haastert, and D. A. Wiersma. 2001. Reduced protein diffusion rate by cytoskeleton in vegetative and polarized Dictyostelium cells. Biophys. J. 81:2010-2019.
    • (2001) Biophys. J. , vol.81 , pp. 2010-2019
    • Potma, E.O.1    De Boeij, W.P.2    Bosgraaf, L.3    Roelofs, J.4    Van Haastert, P.J.M.5    Wiersma, D.A.6
  • 19
    • 24044516873 scopus 로고    scopus 로고
    • Location and mobility of twin-arginine translocase subunits in the Escherichia coli plasma membrane
    • Ray, N., A. Nenninger, C. W. Mullineaux, and C. Robinson. 2005. Location and mobility of twin-arginine translocase subunits in the Escherichia coli plasma membrane. J. Biol. Chem. 280:17961-17968.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17961-17968
    • Ray, N.1    Nenninger, A.2    Mullineaux, C.W.3    Robinson, C.4
  • 20
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits, E. A. J., and J. J. Neefjes. 2001. From fixed to FRAP: measuring protein mobility and activity in living cells. Nature Cell Biol. 3:145-147.
    • (2001) Nature Cell Biol. , vol.3 , pp. 145-147
    • Reits, E.A.J.1    Neefjes, J.J.2
  • 21
    • 0035861656 scopus 로고    scopus 로고
    • Diffusion of phycobilisomes on the thylakoid membranes of the cyanobacterium Synechococcus 7942: Effects of phycobilisome size, temperature and membrane lipid composition
    • Sarcina, M., M. J. Tobin, and C. W. Mullineaux. 2001. Diffusion of phycobilisomes on the thylakoid membranes of the cyanobacterium Synechococcus 7942: effects of phycobilisome size, temperature and membrane lipid composition. J. Biol. Chem. 276:46830-46834.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46830-46834
    • Sarcina, M.1    Tobin, M.J.2    Mullineaux, C.W.3
  • 22
    • 0142200346 scopus 로고    scopus 로고
    • Lipid diffusion in the thylakoid membranes of the cyanobacterium Synechococcus sp.: Effect of fatty acid desaturation
    • Sarcina, M., N. Murata, M. J. Tobin, and C. W. Mullineaux. 2003. Lipid diffusion in the thylakoid membranes of the cyanobacterium Synechococcus sp.: effect of fatty acid desaturation. FEBS Lett. 553:295-298.
    • (2003) FEBS Lett. , vol.553 , pp. 295-298
    • Sarcina, M.1    Murata, N.2    Tobin, M.J.3    Mullineaux, C.W.4
  • 23
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli
    • Thomas, J. D., R. A. Daniel, J. Errington, and C. Robinson. 2001. Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol. Microbiol. 39:47-53.
    • (2001) Mol. Microbiol. , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 24
    • 0034595796 scopus 로고    scopus 로고
    • TatD is a cytoplasmic protein with DNase activity-no requirement for TatD family proteins in Sec-independent protein export
    • Wexler, M., F. Sargent, R. L. Jack, N. R. Stanley, E. G. Bogsch, C. Robinson, B. C. Berks, and T. Palmer. 2000. TatD is a cytoplasmic protein with DNase activity-no requirement for TatD family proteins in Sec-independent protein export. J. Biol. Chem. 275:16717-16722.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16717-16722
    • Wexler, M.1    Sargent, F.2    Jack, R.L.3    Stanley, N.R.4    Bogsch, E.G.5    Robinson, C.6    Berks, B.C.7    Palmer, T.8
  • 25
    • 0033912430 scopus 로고    scopus 로고
    • Multidrug resistance mechanisms: Drug efflux across two membranes
    • Zgurskaya, H. I., and H. Nikaido. 2000. Multidrug resistance mechanisms: drug efflux across two membranes. Mol. Microbiol. 37:219-225.
    • (2000) Mol. Microbiol. , vol.37 , pp. 219-225
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 26
    • 0027661274 scopus 로고
    • Protein lateral mobility as a reflection of membrane microstructure
    • Zhang, F., G. M. Lee, and K. Jacobson. 1993. Protein lateral mobility as a reflection of membrane microstructure. Bioessays 15:579-588.
    • (1993) Bioessays , vol.15 , pp. 579-588
    • Zhang, F.1    Lee, G.M.2    Jacobson, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.