메뉴 건너뛰기




Volumn 69, Issue 1, 2007, Pages 31-40

Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine

Author keywords

Cysteine; Dibromobimane; Fluorescence; His tag; Metal chelating; Protein tagging

Indexed keywords

AMINO ACID; CYSTEINE; FLUORESCENT DYE; HISTIDINE; NITRILOTRIACETIC ACID; PROTEIN TAG;

EID: 33847158264     PISSN: 17470277     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2007.00463.x     Document Type: Article
Times cited : (26)

References (43)
  • 1
    • 0141706507 scopus 로고    scopus 로고
    • Biotechnological applications of green fluorescent protein
    • March J.C., Rao G., Bentley W.E. (2003) Biotechnological applications of green fluorescent protein. Appl Microbiol Biotechnol;62:303-315.
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 303-315
    • March, J.C.1    Rao, G.2    Bentley, W.E.3
  • 2
    • 1042264072 scopus 로고    scopus 로고
    • Protein localization in proteomics
    • Davis T.N. (2004) Protein localization in proteomics. Curr Opin Chem Biol;8:49-53.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 49-53
    • Davis, T.N.1
  • 3
    • 27744485401 scopus 로고    scopus 로고
    • Adding amino acids to the genetic repertoire
    • Xie J., Schultz P.G. (2005) Adding amino acids to the genetic repertoire. Curr Opin Chem Biol;9:548-554.
    • (2005) Curr Opin Chem Biol , vol.9 , pp. 548-554
    • Xie, J.1    Schultz, P.G.2
  • 4
    • 4544231739 scopus 로고    scopus 로고
    • Site-specific incorporation of unnatural amino acids into proteins
    • Stromgaard A., Jensen A.A., Stromgaard K. (2004) Site-specific incorporation of unnatural amino acids into proteins. Chembiochem;5:909-916.
    • (2004) Chembiochem , vol.5 , pp. 909-916
    • Stromgaard, A.1    Jensen, A.A.2    Stromgaard, K.3
  • 7
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., Tsien R.Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science;281:269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 8
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., Adams S.R., Jones J., Tsien R.Y. (2000) Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol;327:565-578.
    • (2000) Methods Enzymol , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 9
    • 0035814333 scopus 로고    scopus 로고
    • Site-specific incorporation of fluorescent probes into protein: Hexahistidinetag-mediated fluorescent labeling with (Ni(2+):nitrilotriacetic acid (n)-fluorochrome conjugates
    • Kapanidis A.N., Ebright Y.W., Ebright R.H. (2001) Site-specific incorporation of fluorescent probes into protein: hexahistidinetag-mediated fluorescent labeling with (Ni(2+):nitrilotriacetic acid (n)-fluorochrome conjugates. J Am Chem Soc;123:12123-12125.
    • (2001) J Am Chem Soc , vol.123 , pp. 12123-12125
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ebright, R.H.3
  • 10
    • 1842582037 scopus 로고    scopus 로고
    • Reversible site-selective labeling of membrane proteins in live cells
    • Guignet E.G., Hovius R., Vogel H. (2004) Reversible site-selective labeling of membrane proteins in live cells. Nat Biotechnol;22:440-444.
    • (2004) Nat Biotechnol , vol.22 , pp. 440-444
    • Guignet, E.G.1    Hovius, R.2    Vogel, H.3
  • 11
    • 27744601234 scopus 로고    scopus 로고
    • Intein-mediated, in vitro and in vivo protein modifications with small molecules
    • Tan L.P., Yao S.Q. (2005) Intein-mediated, in vitro and in vivo protein modifications with small molecules. Protein Pept Lett;12:769-775.
    • (2005) Protein Pept Lett , vol.12 , pp. 769-775
    • Tan, L.P.1    Yao, S.Q.2
  • 13
    • 33644890438 scopus 로고    scopus 로고
    • Expanding the genetic code in a mammalian cell line by the introduction of four-base codon/anticodon pairs
    • Taki M., Matsushita J., Sisido M. (2006) Expanding the genetic code in a mammalian cell line by the introduction of four-base codon/anticodon pairs. Chembiochem;7:425-428.
    • (2006) Chembiochem , vol.7 , pp. 425-428
    • Taki, M.1    Matsushita, J.2    Sisido, M.3
  • 14
    • 23044460011 scopus 로고    scopus 로고
    • N-terminal labeling of proteins using initiator tRNA
    • Olejnik J., Gite S., Mamaev S., Rothschild K.J. (2005) N-terminal labeling of proteins using initiator tRNA. Methods;36:252-260.
    • (2005) Methods , vol.36 , pp. 252-260
    • Olejnik, J.1    Gite, S.2    Mamaev, S.3    Rothschild, K.J.4
  • 15
    • 33645325418 scopus 로고    scopus 로고
    • Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu Y., Schultz P.G. (2006) Efficient incorporation of unnatural amino acids into proteins in Escherichia coli. Nat Methods;3:263-265.
    • (2006) Nat Methods , vol.3 , pp. 263-265
    • Ryu, Y.1    Schultz, P.G.2
  • 16
    • 22944441978 scopus 로고    scopus 로고
    • High-affinity adaptors for switchable recognition of histidine-tagged proteins
    • Lata S., Reichel A., Brock R., Tampe R., Piehler J. (2005) High-affinity adaptors for switchable recognition of histidine-tagged proteins. J Am Chem Soc;127:10205-10215.
    • (2005) J Am Chem Soc , vol.127 , pp. 10205-10215
    • Lata, S.1    Reichel, A.2    Brock, R.3    Tampe, R.4    Piehler, J.5
  • 17
    • 33746006525 scopus 로고    scopus 로고
    • Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins
    • Tirat A., Freuler F., Stettler T., Mayr L.M., Leder L. (2006) Evaluation of two novel tag-based labelling technologies for site-specific modification of proteins. Int J Biol Macromol;39:66-76.
    • (2006) Int J Biol Macromol , vol.39 , pp. 66-76
    • Tirat, A.1    Freuler, F.2    Stettler, T.3    Mayr, L.M.4    Leder, L.5
  • 18
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., Tsien R.Y. (2002) New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc;124:6063-6076.
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 19
    • 0027289198 scopus 로고
    • The design of metal-binding sites in proteins
    • Regan L. (1993) The design of metal-binding sites in proteins. Annu Rev Biophys Biomol Struct;22:257-287.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 257-287
    • Regan, L.1
  • 20
    • 9944240387 scopus 로고    scopus 로고
    • Structural insights into protein-metal ion partnerships
    • Barondeau D.P., Getzoff E.D. (2004) Structural insights into protein-metal ion partnerships. Curr Opin Struct Biol;14:765-774.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 765-774
    • Barondeau, D.P.1    Getzoff, E.D.2
  • 21
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Dobeli H., Schacher A. (1987) New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr;411:177-184.
    • (1987) J Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 22
    • 0027673618 scopus 로고
    • Affinity purification of histidine-tagged proteins
    • Schmitt J., Hess H., Stunnenberg H.G. (1993) Affinity purification of histidine-tagged proteins. Mol Biol Rep;18:223-230.
    • (1993) Mol Biol Rep , vol.18 , pp. 223-230
    • Schmitt, J.1    Hess, H.2    Stunnenberg, H.G.3
  • 23
    • 10344265554 scopus 로고    scopus 로고
    • Oriented attachment and membrane reconstitution of His-tagged cytochrome c oxidase to a gold electrode: In situ monitoring by surface-enhanced infrared absorption spectroscopy
    • Ataka K., Giess F., Knoll W., Naumann R., Haber-Pohlmeier S., Richter B., Heberle J. (2004) Oriented attachment and membrane reconstitution of His-tagged cytochrome c oxidase to a gold electrode: in situ monitoring by surface-enhanced infrared absorption spectroscopy. J Am Chem Soc;126:16199-16206.
    • (2004) J Am Chem Soc , vol.126 , pp. 16199-16206
    • Ataka, K.1    Giess, F.2    Knoll, W.3    Naumann, R.4    Haber-Pohlmeier, S.5    Richter, B.6    Heberle, J.7
  • 24
    • 0034702972 scopus 로고    scopus 로고
    • Interaction of σ70 with Escherichia coli RNA polymerase core enzyme studied by surface plasmon resonance
    • Ferguson A.L., Hughes A.D., Tufail U., Baumann C.G., Scott D.J., Hoggett J.G. (2000) Interaction of σ70 with Escherichia coli RNA polymerase core enzyme studied by surface plasmon resonance. FEBS Lett;481:281-284.
    • (2000) FEBS Lett , vol.481 , pp. 281-284
    • Ferguson, A.L.1    Hughes, A.D.2    Tufail, U.3    Baumann, C.G.4    Scott, D.J.5    Hoggett, J.G.6
  • 25
    • 0347613015 scopus 로고    scopus 로고
    • Current and prospective applications of metal ion-protein binding
    • Ueda E.K., Gout P.W., Morganti L. (2003) Current and prospective applications of metal ion-protein binding. J Chromatogr A;988:1-23.
    • (2003) J Chromatogr A , vol.988 , pp. 1-23
    • Ueda, E.K.1    Gout, P.W.2    Morganti, L.3
  • 26
    • 33847105216 scopus 로고    scopus 로고
    • Preparation of Aminodicarboxylic acid N,N-diacetic acids as Biodegradable Chelating Agents to be used as Substitutes for EDTA. Japan Patent No. JKXXAF
    • JP 10077253 A2 19980324, Japan Patent Office, Tokyo, Japan
    • Saito M., Yamamoto T., Ikuya S. (1998) Preparation of Aminodicarboxylic acid N,N-diacetic acids as Biodegradable Chelating Agents to be used as Substitutes for EDTA. Japan Patent No. JKXXAF JP 10077253 A2 19980324, Japan Patent Office, Tokyo, Japan.
    • (1998)
    • Saito, M.1    Yamamoto, T.2    Ikuya, S.3
  • 27
    • 0029996505 scopus 로고    scopus 로고
    • Single-step synthesis and characterization of biotinylated nitrilotriacetic acid, a unique reagent for the detection of histidine-tagged proteins immobilized on nitrocellulose
    • McMahan S.A., Burgess R.R. (1996) Single-step synthesis and characterization of biotinylated nitrilotriacetic acid, a unique reagent for the detection of histidine-tagged proteins immobilized on nitrocellulose. Anal Biochem;236:101-106.
    • (1996) Anal Biochem , vol.236 , pp. 101-106
    • McMahan, S.A.1    Burgess, R.R.2
  • 28
    • 0348048559 scopus 로고    scopus 로고
    • Metal-chelating amino acids as building blocks for synthetic receptors sensing metal ions and histidine-tagged proteins
    • Hutschenreiter S., Neumann L., Radler U., Schmitt L., Tampe R. (2003) Metal-chelating amino acids as building blocks for synthetic receptors sensing metal ions and histidine-tagged proteins. Chembiochem;4:1340-1344.
    • (2003) Chembiochem , vol.4 , pp. 1340-1344
    • Hutschenreiter, S.1    Neumann, L.2    Radler, U.3    Schmitt, L.4    Tampe, R.5
  • 29
    • 33644516580 scopus 로고    scopus 로고
    • Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation
    • Lata S., Gavutis M., Tampe R., Piehler J. (2006) Specific and stable fluorescence labeling of histidine-tagged proteins for dissecting multi-protein complex formation. J Am Chem Soc;128:2365-2372.
    • (2006) J Am Chem Soc , vol.128 , pp. 2365-2372
    • Lata, S.1    Gavutis, M.2    Tampe, R.3    Piehler, J.4
  • 30
    • 0026724165 scopus 로고
    • Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability
    • Zhang J., Liu Z.P., Jones T.A., Gierasch L.M., Sambrook J.F. (1992) Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins;13:87-99.
    • (1992) Proteins , vol.13 , pp. 87-99
    • Zhang, J.1    Liu, Z.P.2    Jones, T.A.3    Gierasch, L.M.4    Sambrook, J.F.5
  • 31
    • 0031784567 scopus 로고    scopus 로고
    • Probing the folding pathway of a β-clam protein with single-tryptophan constructs
    • Clark P.L., Weston B.F., Gierasch L.M. (1998) Probing the folding pathway of a β-clam protein with single-tryptophan constructs. Fold Des;3:401-412.
    • (1998) Fold Des , vol.3 , pp. 401-412
    • Clark, P.L.1    Weston, B.F.2    Gierasch, L.M.3
  • 32
    • 0035377197 scopus 로고    scopus 로고
    • The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle
    • Cleverley R.M., Zheng N., Gierasch L.M. (2001) The cost of exposing a hydrophobic loop and implications for the functional role of 4.5 S RNA in the Escherichia coli signal recognition particle. J Biol Chem;276:19327- 19331.
    • (2001) J Biol Chem , vol.276 , pp. 19327-19331
    • Cleverley, R.M.1    Zheng, N.2    Gierasch, L.M.3
  • 34
    • 0000964662 scopus 로고
    • Bimane fluorescent labels: Labeling of normal human red cells under physiological conditions
    • Kosower N.S., Kosower E.M., Newton G.L., Ranney H.M. (1979) Bimane fluorescent labels: labeling of normal human red cells under physiological conditions. Proc Natl Acad Sci U S A;76:3382-3386.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 3382-3386
    • Kosower, N.S.1    Kosower, E.M.2    Newton, G.L.3    Ranney, H.M.4
  • 35
    • 0023084127 scopus 로고
    • Thiol labeling with bromobimanes
    • Kosower N.S., Kosower E.M. (1987) Thiol labeling with bromobimanes. Methods Enzymol;143:76-84.
    • (1987) Methods Enzymol , vol.143 , pp. 76-84
    • Kosower, N.S.1    Kosower, E.M.2
  • 36
    • 0019798675 scopus 로고
    • Dynamic changes of red cell membrane thiol groups followed by bimane fluorescent labeling
    • Kosower N.S., Kosower E.M., Zipser Y., Faltin Z., Shomrat R. (1981) Dynamic changes of red cell membrane thiol groups followed by bimane fluorescent labeling. Biochim Biophys Acta;640:748-759.
    • (1981) Biochim Biophys Acta , vol.640 , pp. 748-759
    • Kosower, N.S.1    Kosower, E.M.2    Zipser, Y.3    Faltin, Z.4    Shomrat, R.5
  • 37
    • 0023126341 scopus 로고
    • Bromobimanes - fluorescent labeling agents for histochemical detection of sulfur containing neuropeptides in semithin sections
    • Danielsohn P., Nolte A. (1987) Bromobimanes - fluorescent labeling agents for histochemical detection of sulfur containing neuropeptides in semithin sections. Histochemistry;86:281-285.
    • (1987) Histochemistry , vol.86 , pp. 281-285
    • Danielsohn, P.1    Nolte, A.2
  • 38
    • 0029022647 scopus 로고
    • Determination of biothiols by bromobimane labeling and high-performance liquid chromatography
    • Newton G.L., Fahey R.C. (1995) Determination of biothiols by bromobimane labeling and high-performance liquid chromatography. Methods Enzymol;251:148-166.
    • (1995) Methods Enzymol , vol.251 , pp. 148-166
    • Newton, G.L.1    Fahey, R.C.2
  • 39
    • 22444441692 scopus 로고    scopus 로고
    • Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET
    • Buskiewicz I., Peske F., Wieden H.J., Gryczynski I., Rodnina M.V., Wintermeyer W. (2005) Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET. J Mol Biol;351:417-430.
    • (2005) J Mol Biol , vol.351 , pp. 417-430
    • Buskiewicz, I.1    Peske, F.2    Wieden, H.J.3    Gryczynski, I.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 40
    • 3042799329 scopus 로고    scopus 로고
    • Mapping spatial proximities of sulfhydryl groups in proteins using a fluorogenic cross-linker and mass spectrometry
    • Sinz A., Wang K. (2004) Mapping spatial proximities of sulfhydryl groups in proteins using a fluorogenic cross-linker and mass spectrometry. Anal Biochem;331:27-32.
    • (2004) Anal Biochem , vol.331 , pp. 27-32
    • Sinz, A.1    Wang, K.2
  • 42
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • Arnau J., Lauritzen C., Petersen G.E., Pedersen J. (2006) Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr Purif;48:1-13.
    • (2006) Protein Expr Purif , vol.48 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.