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Volumn 423, Issue , 2007, Pages 299-316

Analyzing Transmembrane Chemoreceptors Using In Vivo Disulfide Formation Between Introduced Cysteines

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISULFIDE; REAGENT;

EID: 34250830373     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)23013-7     Document Type: Chapter
Times cited : (9)

References (27)
  • 1
    • 31344454302 scopus 로고    scopus 로고
    • Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli
    • Amin D.N., Taylor B.L., and Johnson M.S. Topology and boundaries of the aerotaxis receptor Aer in the membrane of Escherichia coli. J. Bacteriol. 188 (2006) 894-901
    • (2006) J. Bacteriol. , vol.188 , pp. 894-901
    • Amin, D.N.1    Taylor, B.L.2    Johnson, M.S.3
  • 2
    • 0035717504 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in Escherichia coli
    • Bader M.W., and Bardwell J.C.A. Catalysis of disulfide bond formation and isomerization in Escherichia coli. Adv. Protein Chem. 59 (2001) 283-301
    • (2001) Adv. Protein Chem. , vol.59 , pp. 283-301
    • Bader, M.W.1    Bardwell, J.C.A.2
  • 3
    • 0035010155 scopus 로고    scopus 로고
    • Signaling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain
    • Beel B.D., and Hazelbauer G.L. Signaling substitutions in the periplasmic domain of chemoreceptor Trg induce or reduce helical sliding in the transmembrane domain. Mol. Microbiol. 40 (2001) 824-834
    • (2001) Mol. Microbiol. , vol.40 , pp. 824-834
    • Beel, B.D.1    Hazelbauer, G.L.2
  • 4
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette P.H., Aslund F., Beckwith J., and Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96 (1999) 13703-13708
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 5
    • 2442720144 scopus 로고    scopus 로고
    • Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues
    • Boldog T., and Hazelbauer G.L. Accessibility of introduced cysteines in chemoreceptor transmembrane helices reveals boundaries interior to bracketing charged residues. Protein Sci. 13 (2004) 1466-1475
    • (2004) Protein Sci. , vol.13 , pp. 1466-1475
    • Boldog, T.1    Hazelbauer, G.L.2
  • 6
    • 0026489631 scopus 로고
    • Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga C.L., and Falke J.J. Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226 (1992) 1219-1235
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 7
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman A.I., Prinz W.A., Belin D., and Beckwith J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262 (1993) 1744-1747
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 8
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg D., Weiss R.M., and Terwilliger T.C. The helical hydrophobic moment: A measure of the amphiphilicity of a helix. Nature 299 (1982) 371-374
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 9
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke J.J., and Hazelbauer G.L. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26 (2001) 257-265
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 10
    • 0029910912 scopus 로고    scopus 로고
    • Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
    • Hughson A.G., and Hazelbauer G.L. Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc. Natl. Acad. Sci. USA 93 (1996) 11546-11551
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11546-11551
    • Hughson, A.G.1    Hazelbauer, G.L.2
  • 11
    • 0031056669 scopus 로고    scopus 로고
    • Analysis of protein structure in intact cells: Crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor
    • Hughson A.G., Lee G.F., and Hazelbauer G.L. Analysis of protein structure in intact cells: Crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor. Protein Sci. 6 (1997) 315-322
    • (1997) Protein Sci. , vol.6 , pp. 315-322
    • Hughson, A.G.1    Lee, G.F.2    Hazelbauer, G.L.3
  • 12
    • 0014284027 scopus 로고
    • Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex
    • Kobashi K. Catalytic oxidation of sulfhydryl groups by o-phenanthroline copper complex. Biochimica et Biophysica Acta (BBA)-General Subjects 158 (1968) 239-245
    • (1968) Biochimica et Biophysica Acta (BBA)-General Subjects , vol.158 , pp. 239-245
    • Kobashi, K.1
  • 13
    • 0029006990 scopus 로고
    • Diamide: An oxidant probe for thiols
    • Kosower N.S., and Kosower E.M. Diamide: An oxidant probe for thiols. Methods Enzymol. 251 (1995) 123-133
    • (1995) Methods Enzymol. , vol.251 , pp. 123-133
    • Kosower, N.S.1    Kosower, E.M.2
  • 14
    • 29344452198 scopus 로고    scopus 로고
    • Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity
    • Lai W.-C., Peach M.L., Lybrand T.P., and Hazelbauer G.L. Diagnostic cross-linking of paired cysteine pairs demonstrates homologous structures for two chemoreceptor domains with low sequence identity. Protein Sci. 15 (2006) 94-101
    • (2006) Protein Sci. , vol.15 , pp. 94-101
    • Lai, W.-C.1    Peach, M.L.2    Lybrand, T.P.3    Hazelbauer, G.L.4
  • 15
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg
    • Lee G.F., Burrows G.G., Lebert M.R., Dutton D.P., and Hazelbauer G.L. Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg. J. Biol. Chem. 269 (1994) 29920-29927
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 16
    • 0029003146 scopus 로고
    • Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain
    • Lee G.F., and Hazelbauer G.L. Quantitative approaches to utilizing mutational analysis and disulfide crosslinking for modeling a transmembrane domain. Protein Sci. 4 (1995) 1100-1107
    • (1995) Protein Sci. , vol.4 , pp. 1100-1107
    • Lee, G.F.1    Hazelbauer, G.L.2
  • 17
    • 0028924963 scopus 로고
    • Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo
    • Lee G.F., Lebert M.R., Lilly A.A., and Hazelbauer G.L. Transmembrane signaling characterized in bacterial chemoreceptors by using sulfhydryl cross-linking in vivo. Proc. Natl. Acad. Sci. USA 92 (1995) 3391-3395
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3391-3395
    • Lee, G.F.1    Lebert, M.R.2    Lilly, A.A.3    Hazelbauer, G.L.4
  • 18
    • 6044247517 scopus 로고    scopus 로고
    • The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding
    • Ma Q., Roy F., Herrmann S., Taylor B.L., and Johnson M.S. The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding. J. Bacteriol. 186 (2004) 7456-7459
    • (2004) J. Bacteriol. , vol.186 , pp. 7456-7459
    • Ma, Q.1    Roy, F.2    Herrmann, S.3    Taylor, B.L.4    Johnson, M.S.5
  • 19
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • Nakamoto H., and Bardwell J.C.A. Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochimica et Biophysica Acta 1694 (2004) 111-119
    • (2004) Biochimica et Biophysica Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.A.2
  • 20
    • 0026605299 scopus 로고
    • Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor
    • Pakula A.A., and Simon M.I. Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor. Proc. Natl. Acad. Sci. USA 89 (1992) 4144-4148
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4144-4148
    • Pakula, A.A.1    Simon, M.I.2
  • 21
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz W.A., Aslund F., Holmgren A., and Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272 (1997) 15661-15667
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 22
    • 0032411723 scopus 로고    scopus 로고
    • The genetics of disulfide bond metabolism
    • Rietsch A., and Beckwith J. The genetics of disulfide bond metabolism. Annu. Rev. Genet. 32 (1998) 163-184
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 163-184
    • Rietsch, A.1    Beckwith, J.2
  • 24
    • 1242274351 scopus 로고    scopus 로고
    • Crosslinking snapshots of bacterial chemoreceptor squads
    • Studdert C.A., and Parkinson J.S. Crosslinking snapshots of bacterial chemoreceptor squads. Proc. Natl. Acad. Sci. USA 101 (2004) 2117-2122
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2117-2122
    • Studdert, C.A.1    Parkinson, J.S.2
  • 25
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton J.M. Disulphide bridges in globular proteins. J. Mol. Biol. 151 (1981) 261-287
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 27
    • 33644854244 scopus 로고    scopus 로고
    • Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer
    • Watts K.J., Sommer K., Fry S.L., Johnson M.S., and Taylor B.L. Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer. J. Bacteriol. 188 (2006) 2154-2162
    • (2006) J. Bacteriol. , vol.188 , pp. 2154-2162
    • Watts, K.J.1    Sommer, K.2    Fry, S.L.3    Johnson, M.S.4    Taylor, B.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.