메뉴 건너뛰기




Volumn 423, Issue , 2007, Pages 436-457

Phenotypic Suppression Methods for Analyzing Intra- and Inter-Molecular Signaling Interactions of Chemoreceptors

(2)  Ames, Peter a   Parkinson, John S a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

AGAR; AMINO ACID;

EID: 34250865723     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)23021-6     Document Type: Chapter
Times cited : (7)

References (50)
  • 2
    • 0024276608 scopus 로고
    • Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output
    • Ames P., and Parkinson J.S. Transmembrane signaling by bacterial chemoreceptors: E. coli transducers with locked signal output. Cell 55 (1988) 817-826
    • (1988) Cell , vol.55 , pp. 817-826
    • Ames, P.1    Parkinson, J.S.2
  • 3
    • 0028097182 scopus 로고
    • Constitutively signaling fragments of Tsr, the Escherichia coli serine chemoreceptor
    • Ames P., and Parkinson J.S. Constitutively signaling fragments of Tsr, the Escherichia coli serine chemoreceptor. J. Bacteriol. 176 (1994) 6340-6348
    • (1994) J. Bacteriol. , vol.176 , pp. 6340-6348
    • Ames, P.1    Parkinson, J.S.2
  • 4
    • 33745172449 scopus 로고    scopus 로고
    • Conformational suppression of inter-receptor signaling defects
    • Ames P., and Parkinson J.S. Conformational suppression of inter-receptor signaling defects. Proc. Natl. Acad. Sci. USA 103 (2006) 9292-9297
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9292-9297
    • Ames, P.1    Parkinson, J.S.2
  • 6
    • 0033277365 scopus 로고    scopus 로고
    • Bacterial tactic responses
    • Armitage J.P. Bacterial tactic responses. Adv. Microb. Physiol. 41 (1999) 229-289
    • (1999) Adv. Microb. Physiol. , vol.41 , pp. 229-289
    • Armitage, J.P.1
  • 7
    • 33646597727 scopus 로고    scopus 로고
    • Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer
    • Buron-Barral M., Gosink K.K., and Parkinson J.S. Loss- and gain-of-function mutations in the F1-HAMP region of the Escherichia coli aerotaxis transducer Aer. J. Bacteriol. 188 (2006) 3477-3486
    • (2006) J. Bacteriol. , vol.188 , pp. 3477-3486
    • Buron-Barral, M.1    Gosink, K.K.2    Parkinson, J.S.3
  • 8
    • 0032575326 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor
    • Butler S.L., and Falke J.J. Cysteine and disulfide scanning reveals two amphiphilic helices in the linker region of the aspartate chemoreceptor. Biochem. 37 (1998) 10746-10756
    • (1998) Biochem. , vol.37 , pp. 10746-10756
    • Butler, S.L.1    Falke, J.J.2
  • 10
    • 0028818765 scopus 로고
    • Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor
    • Chervitz S.A., and Falke J.J. Lock on/off disulfides identify the transmembrane signaling helix of the aspartate receptor. J. Biol. Chem. 270 (1995) 24043-24053
    • (1995) J. Biol. Chem. , vol.270 , pp. 24043-24053
    • Chervitz, S.A.1    Falke, J.J.2
  • 11
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz S.A., and Falke J.J. Molecular mechanism of transmembrane signaling by the aspartate receptor: A model. Proc. Natl. Acad. Sci. USA 93 (1996) 2545-2550
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 12
    • 19644374667 scopus 로고    scopus 로고
    • Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching
    • Coleman M.D., Bass R.B., Mehan R.S., and Falke J.J. Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching. Biochem. 44 (2005) 7687-7695
    • (2005) Biochem. , vol.44 , pp. 7687-7695
    • Coleman, M.D.1    Bass, R.B.2    Mehan, R.S.3    Falke, J.J.4
  • 13
    • 0031451150 scopus 로고    scopus 로고
    • Cysteine and disulfide scanning reveals a regulatory a-helix in the cytoplasmic domain of the aspartate receptor
    • Danielson M., Bass R., and Falke J. Cysteine and disulfide scanning reveals a regulatory a-helix in the cytoplasmic domain of the aspartate receptor. J. Biol. Chem. 272 (1997) 32878-32888
    • (1997) J. Biol. Chem. , vol.272 , pp. 32878-32888
    • Danielson, M.1    Bass, R.2    Falke, J.3
  • 14
    • 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
  • 15
    • 0029851704 scopus 로고    scopus 로고
    • Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain
    • Gardina P.J., and Manson M.D. Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain. Science 274 (1996) 425-426
    • (1996) Science , vol.274 , pp. 425-426
    • Gardina, P.J.1    Manson, M.D.2
  • 16
    • 0028294190 scopus 로고
    • A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function
    • Jeffery C.J., and Koshland Jr. D.E. A single hydrophobic to hydrophobic substitution in the transmembrane domain impairs aspartate receptor function. Biochem. 33 (1994) 3457-3463
    • (1994) Biochem. , vol.33 , pp. 3457-3463
    • Jeffery, C.J.1    Koshland Jr., D.E.2
  • 17
    • 0032692145 scopus 로고    scopus 로고
    • The Escherichia coli aspartate receptor: Sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis
    • Jeffery C.J., and Koshland Jr. D.E. The Escherichia coli aspartate receptor: Sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis. Protein Eng. 12 (1999) 863-872
    • (1999) Protein Eng. , vol.12 , pp. 863-872
    • Jeffery, C.J.1    Koshland Jr., D.E.2
  • 18
    • 0025058595 scopus 로고
    • Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli
    • Lee L., and Imae Y. Role of threonine residue 154 in ligand recognition of the Tar chemoreceptor in Escherichia coli. J. Bacteriol. 172 (1990) 377-382
    • (1990) J. Bacteriol. , vol.172 , pp. 377-382
    • Lee, L.1    Imae, Y.2
  • 19
    • 0026317733 scopus 로고
    • Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli
    • Liu J.D., and Parkinson J.S. Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signaling by Escherichia coli. J. Bacteriol. 173 (1991) 4941-4951
    • (1991) J. Bacteriol. , vol.173 , pp. 4941-4951
    • Liu, J.D.1    Parkinson, J.S.2
  • 20
    • 11144338821 scopus 로고    scopus 로고
    • Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix
    • Ma Q., Johnson M.S., and Taylor B.L. Genetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix. J. Bacteriol. 187 (2005) 193-201
    • (2005) J. Bacteriol. , vol.187 , pp. 193-201
    • Ma, Q.1    Johnson, M.S.2    Taylor, B.L.3
  • 21
    • 0034092676 scopus 로고    scopus 로고
    • Allele-specific suppression as a tool to study protein-protein interactions in bacteria
    • Manson M.D. Allele-specific suppression as a tool to study protein-protein interactions in bacteria. Methods 20 (2000) 18-34
    • (2000) Methods , vol.20 , pp. 18-34
    • Manson, M.D.1
  • 22
    • 0028845410 scopus 로고
    • A model for transmembrane signaling by the aspartate receptor based on random-cassette mutagenesis and site-directed disulfide cross-linking
    • Maruyama I.N., Mikawa Y.G., and Maruyama H.I. A model for transmembrane signaling by the aspartate receptor based on random-cassette mutagenesis and site-directed disulfide cross-linking. J. Mol. Biol. 253 (1995) 530-546
    • (1995) J. Mol. Biol. , vol.253 , pp. 530-546
    • Maruyama, I.N.1    Mikawa, Y.G.2    Maruyama, H.I.3
  • 23
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn M.V., Prive G.G., Milligan D.L., Scott W.G., Yeh J., Jancarik J., Koshland Jr. D.E., and Kim S.H. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254 (1991) 1342-1347
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland Jr., D.E.7    Kim, S.H.8
  • 24
    • 1242352964 scopus 로고    scopus 로고
    • Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor
    • Miller A.S., and Falke J.J. Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor. Biochem. 43 (2004) 1763-1770
    • (2004) Biochem. , vol.43 , pp. 1763-1770
    • Miller, A.S.1    Falke, J.J.2
  • 25
    • 0022470992 scopus 로고
    • Characterization of Escherichia coli chemotaxis receptor mutants with null phenotypes
    • Mutoh N., Oosawa K., and Simon M.I. Characterization of Escherichia coli chemotaxis receptor mutants with null phenotypes. J. Bacteriol. 167 (1986) 992-998
    • (1986) J. Bacteriol. , vol.167 , pp. 992-998
    • Mutoh, N.1    Oosawa, K.2    Simon, M.I.3
  • 26
    • 0029893938 scopus 로고    scopus 로고
    • Modulation of the thermosensing profile of the Escherichia coli aspartate receptor tar by covalent modification of its methyl-accepting sites
    • Nara T., Kawagishi I., Nishiyama S., Homma M., and Imae Y. Modulation of the thermosensing profile of the Escherichia coli aspartate receptor tar by covalent modification of its methyl-accepting sites. J. Biol. Chem. 271 (1996) 17932-17936
    • (1996) J. Biol. Chem. , vol.271 , pp. 17932-17936
    • Nara, T.1    Kawagishi, I.2    Nishiyama, S.3    Homma, M.4    Imae, Y.5
  • 27
    • 0033548704 scopus 로고    scopus 로고
    • Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region
    • Nishiyama S., Maruyama I.N., Homma M., and Kawagishi I. Inversion of thermosensing property of the bacterial receptor Tar by mutations in the second transmembrane region. J. Mol. Biol. 286 (1999) 1275-1284
    • (1999) J. Mol. Biol. , vol.286 , pp. 1275-1284
    • Nishiyama, S.1    Maruyama, I.N.2    Homma, M.3    Kawagishi, I.4
  • 28
    • 0030696872 scopus 로고    scopus 로고
    • Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine
    • Nishiyama S., Nara T., Homma M., Imae Y., and Kawagishi I. Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine. J. Bacteriol. 179 (1997) 6573-6580
    • (1997) J. Bacteriol. , vol.179 , pp. 6573-6580
    • Nishiyama, S.1    Nara, T.2    Homma, M.3    Imae, Y.4    Kawagishi, I.5
  • 29
    • 0022465940 scopus 로고
    • Analysis of mutations in the transmembrane region of the aspartate chemoreceptor in Escherichia coli
    • Oosawa K., and Simon M. Analysis of mutations in the transmembrane region of the aspartate chemoreceptor in Escherichia coli. Proc. Natl. Acad. Sci. USA 83 (1986) 6930-6934
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6930-6934
    • Oosawa, K.1    Simon, M.2
  • 30
    • 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
  • 31
    • 0017680859 scopus 로고
    • Behavioral genetics in bacteria
    • Parkinson J.S. Behavioral genetics in bacteria. Annu. Rev. Genet. 11 (1977) 397-414
    • (1977) Annu. Rev. Genet. , vol.11 , pp. 397-414
    • Parkinson, J.S.1
  • 32
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • Parkinson J.S. Signal transduction schemes of bacteria. Cell 73 (1993) 857-871
    • (1993) Cell , vol.73 , pp. 857-871
    • Parkinson, J.S.1
  • 34
    • 12744255176 scopus 로고    scopus 로고
    • Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo
    • Sal-Man N., and Shai Y. Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo. Biochem. J. 385 (2005) 29-36
    • (2005) Biochem. J. , vol.385 , pp. 29-36
    • Sal-Man, N.1    Shai, Y.2
  • 35
    • 0028800723 scopus 로고
    • Contributions made by individual methylation sites of the Escherichia coli aspartate receptor to chemotactic behavior
    • Shapiro M.J., Chakrabarti I., and Koshland Jr. D.E. Contributions made by individual methylation sites of the Escherichia coli aspartate receptor to chemotactic behavior. Proc. Natl. Acad. Sci. USA 92 (1995) 1053-1056
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1053-1056
    • Shapiro, M.J.1    Chakrabarti, I.2    Koshland Jr., D.E.3
  • 36
    • 0036773079 scopus 로고    scopus 로고
    • Intragenic suppressors of a mutation in the aspartate chemoreceptor gene that abolishes binding of the receptor to methyltransferase
    • Shiomi D., Homma M., and Kawagishi I. Intragenic suppressors of a mutation in the aspartate chemoreceptor gene that abolishes binding of the receptor to methyltransferase. Microbiology 148 (2002) 3265-3275
    • (2002) Microbiology , vol.148 , pp. 3265-3275
    • Shiomi, D.1    Homma, M.2    Kawagishi, I.3
  • 37
    • 0034079029 scopus 로고    scopus 로고
    • The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction
    • Shiomi D., Okumura H., Homma M., and Kawagishi I. The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction. Mol. Microbiol. 36 (2000) 132-140
    • (2000) Mol. Microbiol. , vol.36 , pp. 132-140
    • Shiomi, D.1    Okumura, H.2    Homma, M.3    Kawagishi, I.4
  • 38
    • 7944221332 scopus 로고    scopus 로고
    • Receptor clustering and signal processing in E. coli chemotaxis
    • Sourjik V. Receptor clustering and signal processing in E. coli chemotaxis. Trends Microbiol. 12 (2004) 569-576
    • (2004) Trends Microbiol. , vol.12 , pp. 569-576
    • Sourjik, V.1
  • 39
    • 0037039384 scopus 로고    scopus 로고
    • Receptor sensitivity in bacterial chemotaxis
    • Sourjik V., and Berg H.C. Receptor sensitivity in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 99 (2002) 123-127
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 123-127
    • Sourjik, V.1    Berg, H.C.2
  • 40
    • 1842473065 scopus 로고    scopus 로고
    • Functional interactions between receptors in bacterial chemotaxis
    • Sourjik V., and Berg H.C. Functional interactions between receptors in bacterial chemotaxis. Nature 428 (2004) 437-441
    • (2004) Nature , vol.428 , pp. 437-441
    • Sourjik, V.1    Berg, H.C.2
  • 41
    • 13444301196 scopus 로고    scopus 로고
    • Adaptation mechanism of the aspartate receptor: Electrostatics of the adaptation subdomain play a key role in modulating kinase activity
    • Starrett D.J., and Falke J.J. Adaptation mechanism of the aspartate receptor: Electrostatics of the adaptation subdomain play a key role in modulating kinase activity. Biochem. 44 (2005) 1550-1560
    • (2005) Biochem. , vol.44 , pp. 1550-1560
    • Starrett, D.J.1    Falke, J.J.2
  • 42
    • 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
  • 43
    • 27344455900 scopus 로고    scopus 로고
    • Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies
    • Studdert C.A., and Parkinson J.S. Insights into the organization and dynamics of bacterial chemoreceptor clusters through in vivo crosslinking studies. Proc. Natl. Acad. Sci. USA 102 (2005) 15623-15628
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15623-15628
    • Studdert, C.A.1    Parkinson, J.S.2
  • 44
    • 0033524489 scopus 로고    scopus 로고
    • Identification of a site critical for kinase regulation on the central processing unit (CPU) helix of the aspartate receptor
    • Trammell M.A., and Falke J.J. Identification of a site critical for kinase regulation on the central processing unit (CPU) helix of the aspartate receptor. Biochem. 38 (1999) 329-336
    • (1999) Biochem. , vol.38 , pp. 329-336
    • Trammell, M.A.1    Falke, J.J.2
  • 45
    • 0032515058 scopus 로고    scopus 로고
    • Intersubunit interaction between transmembrane helices of the bacterial aspartate chemoreceptor homodimer
    • Umemura T., Tatsuno I., Shibasaki M., Homma M., and Kawagishi I. Intersubunit interaction between transmembrane helices of the bacterial aspartate chemoreceptor homodimer. J. Biol. Chem. 273 (1998) 30110-30115
    • (1998) J. Biol. Chem. , vol.273 , pp. 30110-30115
    • Umemura, T.1    Tatsuno, I.2    Shibasaki, M.3    Homma, M.4    Kawagishi, I.5
  • 46
    • 10044252242 scopus 로고    scopus 로고
    • Making sense of it all: Bacterial chemotaxis
    • Wadhams G.H., and Armitage J.P. Making sense of it all: Bacterial chemotaxis. Nat. Rev. Mol. Cell Biol. 5 (2004) 1024-1037
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 1024-1037
    • Wadhams, G.H.1    Armitage, J.P.2
  • 47
    • 3042869465 scopus 로고
    • Acetyladenylate plays a role in controlling the direction of flagellar rotation
    • Wolfe A.J., Conley M.P., and Berg H.C. Acetyladenylate plays a role in controlling the direction of flagellar rotation. Proc. Natl. Acad. Sci. USA 85 (1988) 6711-6715
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6711-6715
    • Wolfe, A.J.1    Conley, M.P.2    Berg, H.C.3
  • 48
    • 0026730093 scopus 로고
    • Ligand occupancy mimicked by single residue substitutions in a receptor: Transmembrane signaling induced by mutation
    • Yaghmai R., and Hazelbauer G.L. Ligand occupancy mimicked by single residue substitutions in a receptor: Transmembrane signaling induced by mutation. Proc. Natl. Acad. Sci. USA 89 (1992) 7890-7894
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7890-7894
    • Yaghmai, R.1    Hazelbauer, G.L.2
  • 49
    • 0027156912 scopus 로고
    • Strategies for differential sensory responses mediated through the same transmembrane receptor
    • Yaghmai R., and Hazelbauer G.L. Strategies for differential sensory responses mediated through the same transmembrane receptor. EMBO J. 12 (1993) 1897-1905
    • (1993) EMBO J. , vol.12 , pp. 1897-1905
    • Yaghmai, R.1    Hazelbauer, G.L.2
  • 50
    • 0034964703 scopus 로고    scopus 로고
    • The superfamily of chemotaxis transducers: From physiology to genomics and back
    • Zhulin I.B. The superfamily of chemotaxis transducers: From physiology to genomics and back. Adv. Microb. Physiol. 45 (2001) 157-198
    • (2001) Adv. Microb. Physiol. , vol.45 , pp. 157-198
    • Zhulin, I.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.