메뉴 건너뛰기




Volumn 184, Issue 1, 2013, Pages 2-11

Role of trimer-trimer interaction of bacteriorhodopsin studied by optical spectroscopy and high-speed atomic force microscopy

Author keywords

Bacteriorhodopsin; High speed atomic force microscopy; Low temperature UV visible spectroscopy; Point mutation; Proton pumping efficiency; Trimer

Indexed keywords

AMINO ACID; BACTERIORHODOPSIN; N (4 AMINOBUTYL) 2 NAPSYLAMIDE; PROTON;

EID: 84884820053     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2013.02.011     Document Type: Article
Times cited : (38)

References (41)
  • 1
    • 0035940402 scopus 로고    scopus 로고
    • A high-speed atomic force microscope for studying biological macromolecules
    • Ando T., Kodera N., Takai E., Maruyama D., Saito K., et al. A high-speed atomic force microscope for studying biological macromolecules. Proc. Natl. Acad. Sci. USA 2001, 98:12468-12472.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12468-12472
    • Ando, T.1    Kodera, N.2    Takai, E.3    Maruyama, D.4    Saito, K.5
  • 2
    • 54149113310 scopus 로고    scopus 로고
    • High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes
    • Ando T., Uchihashi T., Fukuma T. High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes. Prog. Surf. Sci. 2008, 83:337-437.
    • (2008) Prog. Surf. Sci. , vol.83 , pp. 337-437
    • Ando, T.1    Uchihashi, T.2    Fukuma, T.3
  • 4
    • 0023099215 scopus 로고
    • Efficient transfection of the archaebacterium Halobacterium halobium
    • Cline S.W., Doolittle W.F. Efficient transfection of the archaebacterium Halobacterium halobium. J. Bacteriol. 1987, 169:1341-1344.
    • (1987) J. Bacteriol. , vol.169 , pp. 1341-1344
    • Cline, S.W.1    Doolittle, W.F.2
  • 5
    • 84866492389 scopus 로고    scopus 로고
    • High-speed atomic force microscopy: cooperative adhesion and dynamic equilibrium of junctional microdomain membrane proteins
    • Colom A., Casuso I., Boudier T., Scheuring S. High-speed atomic force microscopy: cooperative adhesion and dynamic equilibrium of junctional microdomain membrane proteins. J. Mol. Biol. 2012, 423:249-256.
    • (2012) J. Mol. Biol. , vol.423 , pp. 249-256
    • Colom, A.1    Casuso, I.2    Boudier, T.3    Scheuring, S.4
  • 6
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex
    • Essen L.O., Siegert R., Lehmannn W.D., Oesterhelt D. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. USA 1998, 95:11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmannn, W.D.3    Oesterhelt, D.4
  • 7
    • 0028136025 scopus 로고
    • Combined optical and photoelectric study of the photocycle of 13-cis bacteriorhodopsin
    • Gergely C., Ganea C., Varo G. Combined optical and photoelectric study of the photocycle of 13-cis bacteriorhodopsin. Biophys. J. 1994, 67:855-861.
    • (1994) Biophys. J. , vol.67 , pp. 855-861
    • Gergely, C.1    Ganea, C.2    Varo, G.3
  • 8
  • 9
    • 69249098842 scopus 로고    scopus 로고
    • Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin
    • Hirai T., Subramaniam S., Lanyi J.K. Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin. Curr. Opin. Struct. Biol. 2009, 19:433-439.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 433-439
    • Hirai, T.1    Subramaniam, S.2    Lanyi, J.K.3
  • 10
    • 84885879445 scopus 로고    scopus 로고
    • Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses
    • Hirai T., Subramaniam S. Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses. J. Mol. Biol. 2009, 328:439-450.
    • (2009) J. Mol. Biol. , vol.328 , pp. 439-450
    • Hirai, T.1    Subramaniam, S.2
  • 11
    • 0029981423 scopus 로고    scopus 로고
    • Structure of the N intermediate of bacteriorhodopsin revealed by X-ray diffraction
    • Kamikubo H., Kataoka M., Varo G., Oka T., Tokunaga F., et al. Structure of the N intermediate of bacteriorhodopsin revealed by X-ray diffraction. Proc. Natl. Acad. Sci. USA 1996, 93:1386-1390.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1386-1390
    • Kamikubo, H.1    Kataoka, M.2    Varo, G.3    Oka, T.4    Tokunaga, F.5
  • 12
    • 2342460436 scopus 로고    scopus 로고
    • Bacteriorhodopsin
    • Lanyi J.K. Bacteriorhodopsin. Annu. Rev. Physiol. 2004, 66:665-688.
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 665-688
    • Lanyi, J.K.1
  • 13
    • 33748903643 scopus 로고    scopus 로고
    • Review: proton transfers in the bacteriorhodopsin photocycle
    • Lanyi J.K. Review: proton transfers in the bacteriorhodopsin photocycle. Biochim. Biophys. Acta 2006, 1757:1012-1018.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1012-1018
    • Lanyi, J.K.1
  • 14
  • 15
    • 0033536594 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution
    • Luecke H., Schobert B., Richter H.T., Cartailler J.P., Lanyi J.K. Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution. Science 1999, 286:255-261.
    • (1999) Science , vol.286 , pp. 255-261
    • Luecke, H.1    Schobert, B.2    Richter, H.T.3    Cartailler, J.P.4    Lanyi, J.K.5
  • 16
    • 0034714159 scopus 로고    scopus 로고
    • Reversible loss of crystallinity on photobleaching purple membrane in the presence of hydroxylamine
    • Moller C., Buldt G., Dencher N.A., Engel A., Muller D.J. Reversible loss of crystallinity on photobleaching purple membrane in the presence of hydroxylamine. J. Mol. Biol. 2000, 301:869-879.
    • (2000) J. Mol. Biol. , vol.301 , pp. 869-879
    • Moller, C.1    Buldt, G.2    Dencher, N.A.3    Engel, A.4    Muller, D.J.5
  • 17
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D., Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat. New Biol. 1971, 233:149-152.
    • (1971) Nat. New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 18
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt D., Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Meth. Enzymol. 1974, 31:667-678.
    • (1974) Meth. Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 19
    • 0033962956 scopus 로고    scopus 로고
    • Homologous gene knockout in the archaeon Halobacterium salinarum with ura3 as a counterselectable marker
    • Peck R.F., Dassarma S., Krebs M.P. Homologous gene knockout in the archaeon Halobacterium salinarum with ura3 as a counterselectable marker. Mol. Microbiol. 2000, 35:667-676.
    • (2000) Mol. Microbiol. , vol.35 , pp. 667-676
    • Peck, R.F.1    Dassarma, S.2    Krebs, M.P.3
  • 20
    • 0035919807 scopus 로고    scopus 로고
    • Direct observation of different surface structures on high-resolution images of native halorhodopsin
    • Persike N., Pfeiffer M., Guckenberger R., Radmacher M., Fritz M. Direct observation of different surface structures on high-resolution images of native halorhodopsin. J. Mol. Biol. 2001, 310:773-780.
    • (2001) J. Mol. Biol. , vol.310 , pp. 773-780
    • Persike, N.1    Pfeiffer, M.2    Guckenberger, R.3    Radmacher, M.4    Fritz, M.5
  • 22
    • 0028966756 scopus 로고
    • Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 a resolution
    • Qian M., Haser R., Payan F. Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 a resolution. Protein Sci. 1995, 4:747-755.
    • (1995) Protein Sci. , vol.4 , pp. 747-755
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 23
    • 0018805369 scopus 로고
    • Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient
    • Rehorek M., Heyn M.P. Binding of all-trans-retinal to the purple membrane. Evidence for cooperativity and determination of the extinction coefficient. Biochemistry 1979, 18:4977-4983.
    • (1979) Biochemistry , vol.18 , pp. 4977-4983
    • Rehorek, M.1    Heyn, M.P.2
  • 24
    • 0026703071 scopus 로고
    • Protein changes associated with reprotonation of the schiff base in the photocycle of Asp96 Asn bacteriorhodopsin. The MN intermediate with unprotonated schiff base but N-like protein structure
    • Sasaki J., Shichida Y., Lanyi J.K., Maeda A. Protein changes associated with reprotonation of the schiff base in the photocycle of Asp96 Asn bacteriorhodopsin. The MN intermediate with unprotonated schiff base but N-like protein structure. J. Biol. Chem. 1992, 267:20782-20786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20782-20786
    • Sasaki, J.1    Shichida, Y.2    Lanyi, J.K.3    Maeda, A.4
  • 25
    • 0342646933 scopus 로고    scopus 로고
    • Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
    • Sass H.J., Buldt G., Gessenich R., Hehn D., Neff D., et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature 2000, 406:649-653.
    • (2000) Nature , vol.406 , pp. 649-653
    • Sass, H.J.1    Buldt, G.2    Gessenich, R.3    Hehn, D.4    Neff, D.5
  • 26
    • 34347224775 scopus 로고    scopus 로고
    • Halide binding by the D212N mutant of bacteriorhodopsin affects hydrogen bonding of water in the active site
    • Shibata M., Yoshitsugu M., Mizuide N., Ihara K., Kandori H. Halide binding by the D212N mutant of bacteriorhodopsin affects hydrogen bonding of water in the active site. Biochemistry 2007, 46:7525-7535.
    • (2007) Biochemistry , vol.46 , pp. 7525-7535
    • Shibata, M.1    Yoshitsugu, M.2    Mizuide, N.3    Ihara, K.4    Kandori, H.5
  • 27
    • 77749324964 scopus 로고    scopus 로고
    • High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
    • Shibata M., Yamashita H., Uchihashi T., Kandori H., Ando T. High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin. Nat. Nanotechnol. 2010, 5:208-212.
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 208-212
    • Shibata, M.1    Yamashita, H.2    Uchihashi, T.3    Kandori, H.4    Ando, T.5
  • 28
    • 79955510966 scopus 로고    scopus 로고
    • Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy
    • Shibata M., Uchihashi T., Yamashita H., Kandori H., Ando T. Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy. Angew. Chem. Int. Ed. Engl. 2011, 50:4410-4413.
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 4410-4413
    • Shibata, M.1    Uchihashi, T.2    Yamashita, H.3    Kandori, H.4    Ando, T.5
  • 29
    • 0035576064 scopus 로고    scopus 로고
    • Environment around the chromophore in pharaonis phoborhodopsin: mutation analysis of the retinal binding site
    • Shimono K., Ikeura Y., Sudo Y., Iwamoto M., Kamo N. Environment around the chromophore in pharaonis phoborhodopsin: mutation analysis of the retinal binding site. Biochim. Biophys. Acta 2001, 1515:92-100.
    • (2001) Biochim. Biophys. Acta , vol.1515 , pp. 92-100
    • Shimono, K.1    Ikeura, Y.2    Sudo, Y.3    Iwamoto, M.4    Kamo, N.5
  • 30
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 31
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S., Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 2000, 406:653-657.
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 32
    • 79953178993 scopus 로고    scopus 로고
    • A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties
    • Sudo Y., Ihara K., Kobayashi S., Suzuki D., Irieda H., et al. A microbial rhodopsin with a unique retinal composition shows both sensory rhodopsin II and bacteriorhodopsin-like properties. J. Biol. Chem. 2011, 286:5967-5976.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5967-5976
    • Sudo, Y.1    Ihara, K.2    Kobayashi, S.3    Suzuki, D.4    Irieda, H.5
  • 33
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions
    • Szidonya L., Cserzo M., Hunyady L. Dimerization and oligomerization of G-protein-coupled receptors: debated structures with established and emerging functions. J. Endocrinol. 2008, 196:435-453.
    • (2008) J. Endocrinol. , vol.196 , pp. 435-453
    • Szidonya, L.1    Cserzo, M.2    Hunyady, L.3
  • 34
    • 0027177539 scopus 로고
    • Dimeric-like kinetic cooperativity of the bacteriorhodopsin molecules in purple membranes
    • Tokaji Z. Dimeric-like kinetic cooperativity of the bacteriorhodopsin molecules in purple membranes. Biophys. J. 1993, 65:1130-1134.
    • (1993) Biophys. J. , vol.65 , pp. 1130-1134
    • Tokaji, Z.1
  • 35
    • 84865814021 scopus 로고    scopus 로고
    • Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy
    • Uchihashi T., Kodera N., Ando T. Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nat. Protoc. 2012, 7:1193-1206.
    • (2012) Nat. Protoc. , vol.7 , pp. 1193-1206
    • Uchihashi, T.1    Kodera, N.2    Ando, T.3
  • 36
    • 0032765325 scopus 로고    scopus 로고
    • Images of oligomeric Kv beta 2, a modulatory subunit of potassium channels
    • van Huizen R., Czajkowsky D.M., Shi D., Shao Z., Li M. Images of oligomeric Kv beta 2, a modulatory subunit of potassium channels. FEBS Lett. 1999, 457:107-111.
    • (1999) FEBS Lett. , vol.457 , pp. 107-111
    • van Huizen, R.1    Czajkowsky, D.M.2    Shi, D.3    Shao, Z.4    Li, M.5
  • 37
    • 0030065552 scopus 로고    scopus 로고
    • Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle
    • Varo G., Needleman R., Lanyi J.K. Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle. Biophys. J. 1996, 70:461-467.
    • (1996) Biophys. J. , vol.70 , pp. 461-467
    • Varo, G.1    Needleman, R.2    Lanyi, J.K.3
  • 38
    • 0029886089 scopus 로고    scopus 로고
    • A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition
    • Vonck J. A three-dimensional difference map of the N intermediate in the bacteriorhodopsin photocycle: part of the F helix tilts in the M to N transition. Biochemistry 1996, 35:5870-5878.
    • (1996) Biochemistry , vol.35 , pp. 5870-5878
    • Vonck, J.1
  • 39
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck J. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 2000, 19:2152-2160.
    • (2000) EMBO J. , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 40
    • 0031990356 scopus 로고    scopus 로고
    • Localization of glycolipids in membranes by in vivo labeling and neutron diffraction
    • Weik M., Patzelt H., Zaccai G., Oesterhelt D. Localization of glycolipids in membranes by in vivo labeling and neutron diffraction. Mol. Cell. 1998, 1:411-419.
    • (1998) Mol. Cell. , vol.1 , pp. 411-419
    • Weik, M.1    Patzelt, H.2    Zaccai, G.3    Oesterhelt, D.4
  • 41
    • 67649823413 scopus 로고    scopus 로고
    • Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy
    • Yamashita H., Voitchovsky K., Uchihashi T., Contera S.A., Ryan J.F., et al. Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy. J. Struct. Biol. 2009, 167:153-158.
    • (2009) J. Struct. Biol. , vol.167 , pp. 153-158
    • Yamashita, H.1    Voitchovsky, K.2    Uchihashi, T.3    Contera, S.A.4    Ryan, J.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.