메뉴 건너뛰기




Volumn 55, Issue 5, 2005, Pages 1538-1552

In vivo analysis of the roles of conserved aspartate and histidine residues within a complex response regulator

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; HISTIDINE; PHYCOCYANIN;

EID: 14844336332     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04491.x     Document Type: Article
Times cited : (34)

References (68)
  • 1
    • 0037346498 scopus 로고    scopus 로고
    • Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus
    • Aldridge, P., Paul, R., Goymer, P., Rainey, P., and Jenal, U. (2003) Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol Microbiol 47: 1695-1708.
    • (2003) Mol Microbiol , vol.47 , pp. 1695-1708
    • Aldridge, P.1    Paul, R.2    Goymer, P.3    Rainey, P.4    Jenal, U.5
  • 2
    • 84984087585 scopus 로고
    • Simple conditions for growth of unicellular blue-green algae on plates
    • Allen, M.M. (1968) Simple conditions for growth of unicellular blue-green algae on plates. J Phycol 4: 1-4.
    • (1968) J Phycol , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 4
    • 0142092355 scopus 로고    scopus 로고
    • Lesions in phycoerythrin chromophore biosynthesis in Fremyella diplosiphon reveal coordinated light regulation of apoprotein and pigment biosynthetic enzyme gene expression
    • Alvey, R.M., Karty, J.A., Roos, E., Reilly, J.P., and Kehoe, D.M. (2003) Lesions in phycoerythrin chromophore biosynthesis in Fremyella diplosiphon reveal coordinated light regulation of apoprotein and pigment biosynthetic enzyme gene expression. Plant Cell 15: 2448-2463.
    • (2003) Plant Cell , vol.15 , pp. 2448-2463
    • Alvey, R.M.1    Karty, J.A.2    Roos, E.3    Reilly, J.P.4    Kehoe, D.M.5
  • 5
    • 0032739281 scopus 로고    scopus 로고
    • C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli
    • Ames, S.K., Frankema, N., and Kenny, L.J. (1999) C-terminal DNA binding stimulates N-terminal phosphorylation of the outer membrane protein regulator OmpR from Escherichia coli. Proc Natl Acad Sci USA 96: 11792-11797.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11792-11797
    • Ames, S.K.1    Frankema, N.2    Kenny, L.J.3
  • 6
    • 0032491213 scopus 로고    scopus 로고
    • Activation of methylesterase CheB: Evidence of a dual role for the regulatory domain
    • Anand, G.S., Goudreau, P.N., and Stock, A.M. (1998) Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 37: 14038-14047.
    • (1998) Biochemistry , vol.37 , pp. 14038-14047
    • Anand, G.S.1    Goudreau, P.N.2    Stock, A.M.3
  • 7
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multi-step phosphorelay: Not necessarily a road less traveled
    • Appleby, J.L., Parkinson, J.S., and Bourret, R.B. (1996) Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled. Cell 86: 845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 8
    • 0000979294 scopus 로고
    • Phycobiliproteins and complementary chromatic adaptation
    • Bogorad, L. (1975) Phycobiliproteins and complementary chromatic adaptation. Annu Rev Plant Physiol 26: 369-401.
    • (1975) Annu Rev Plant Physiol , vol.26 , pp. 369-401
    • Bogorad, L.1
  • 9
    • 0029967298 scopus 로고    scopus 로고
    • Complementary chromatic adaptation alters photosynthetic strategies in the cyanobacterium. Calothrix
    • Campbell, D. (1996) Complementary chromatic adaptation alters photosynthetic strategies in the cyanobacterium. Calothrix. Microbiology 142: 1255-1263.
    • (1996) Microbiology , vol.142 , pp. 1255-1263
    • Campbell, D.1
  • 10
    • 0026686670 scopus 로고
    • Complementation of a red-light-indifferent cyanobacterial mutant
    • Chiang, G.G., Schaefer, M.R., and Grossman, A.R. (1992) Complementation of a red-light-indifferent cyanobacterial mutant. Proc Natl Acad Sci USA 89: 9415-9419.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9415-9419
    • Chiang, G.G.1    Schaefer, M.R.2    Grossman, A.R.3
  • 11
    • 0027209903 scopus 로고
    • Construction of shuttle plasmids which can be efficiently mobilized from Escherichia coli into the chromatically adapting cyanobacterium, Fremyella diplosiphon
    • Cobley, J.G., Zerweck, E., Reyes, R., Mody, A., Seludo-Unson, J.R., Jaeger, H., et al. (1993) Construction of shuttle plasmids which can be efficiently mobilized from Escherichia coli into the chromatically adapting cyanobacterium, Fremyella diplosiphon. Plasmid 30: 90-105.
    • (1993) Plasmid , vol.30 , pp. 90-105
    • Cobley, J.G.1    Zerweck, E.2    Reyes, R.3    Mody, A.4    Seludo-Unson, J.R.5    Jaeger, H.6
  • 12
    • 0022393404 scopus 로고
    • Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts
    • Conley, P.B., Lemaux, P.G., and Grossman, A.R. (1985) Cyanobacterial light-harvesting complex subunits encoded in two red light-induced transcripts. Science 230: 550-553.
    • (1985) Science , vol.230 , pp. 550-553
    • Conley, P.B.1    Lemaux, P.G.2    Grossman, A.R.3
  • 13
    • 0024278122 scopus 로고
    • Molecular characterization and evolution of sequences encoding light-harvesting components in the chromatically adapting cyanobacterium Fremyella diplosiphon
    • Conley, P.B., Lemaux, P.G., and Grossman, A.R. (1988) Molecular characterization and evolution of sequences encoding light-harvesting components in the chromatically adapting cyanobacterium Fremyella diplosiphon. J Mol Biol 199: 447-465.
    • (1988) J Mol Biol , vol.199 , pp. 447-465
    • Conley, P.B.1    Lemaux, P.G.2    Grossman, A.R.3
  • 14
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W.P., and Nickoloff, J.A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal Biochem 200: 81-88.
    • (1992) Anal Biochem , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 15
    • 0030747761 scopus 로고    scopus 로고
    • Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle
    • Domian, I.J., Quon, K.C., and Shapiro, L. (1997) Cell type-specific phosphorylation and proteolysis of a transcriptional regulator controls the G1-to-S transition in a bacterial cell cycle. Cell 90: 415-424.
    • (1997) Cell , vol.90 , pp. 415-424
    • Domian, I.J.1    Quon, K.C.2    Shapiro, L.3
  • 16
    • 0037168492 scopus 로고    scopus 로고
    • Effect of phosphorylation on the interdomain interaction of the response regulator NarL
    • Eldridge, A.M., Kang, H.-S., Johnson, E., Gunsalus, R., and Dahlquist, F.W. (2002) Effect of phosphorylation on the interdomain interaction of the response regulator NarL. Biochemistry 41: 15173-15880.
    • (2002) Biochemistry , vol.41 , pp. 15173-15880
    • Eldridge, A.M.1    Kang, H.-S.2    Johnson, E.3    Gunsalus, R.4    Dahlquist, F.W.5
  • 17
    • 0025293533 scopus 로고
    • Characterization of the light-regulated operon encoding the phycoerythrin-associated linker proteins from the cyanobacterium Fremyella diplosiphon
    • Federspiel, N.A., and Grossman, A.R. (1990) Characterization of the light-regulated operon encoding the phycoerythrin-associated linker proteins from the cyanobacterium Fremyella diplosiphon. J Bacteriol 172: 4072-4081.
    • (1990) J Bacteriol , vol.172 , pp. 4072-4081
    • Federspiel, N.A.1    Grossman, A.R.2
  • 18
    • 0026674274 scopus 로고
    • Characterization of a light-regulated gene encoding a new phycoerythrin-associated linker protein from the cyanobacterium Fremyella diplosiphon
    • Federspiel, N.A., and Scott, L. (1992) Characterization of a light-regulated gene encoding a new phycoerythrin-associated linker protein from the cyanobacterium Fremyella diplosiphon. J Bacteriol 174: 5994-5998.
    • (1992) J Bacteriol , vol.174 , pp. 5994-5998
    • Federspiel, N.A.1    Scott, L.2
  • 19
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin, M.Y., Nikolskaya, A.N., and Koonin, E.V. (2001) Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 203: 11-21.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 20
    • 0032484001 scopus 로고    scopus 로고
    • Signal decay through a reverse phosphorelay in the Arc two-component signal transduction system
    • Georgellis, D., Kwon, O., Wulf, P.D., and Lin, E.C.C. (1998) Signal decay through a reverse phosphorelay in the Arc two-component signal transduction system. J Biol Chem 273: 32864-32869.
    • (1998) J Biol Chem , vol.273 , pp. 32864-32869
    • Georgellis, D.1    Kwon, O.2    Wulf, P.D.3    Lin, E.C.C.4
  • 21
    • 0347994995 scopus 로고    scopus 로고
    • Heterocyst development in Anabaena
    • Golden, J.W., and Yoon, H.-S. (2003) Heterocyst development in Anabaena. Curr Opin Microbiol 6: 557-563.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 557-563
    • Golden, J.W.1    Yoon, H.-S.2
  • 22
    • 0027522844 scopus 로고
    • Environmental effects on the light-harvesting complex of cyanobacteria
    • Grossman, A.R., Schaefer, M.R., Chiang, G.G., and Collier, J.L. (1993) Environmental effects on the light-harvesting complex of cyanobacteria. J Bacteriol 175: 575-582.
    • (1993) J Bacteriol , vol.175 , pp. 575-582
    • Grossman, A.R.1    Schaefer, M.R.2    Chiang, G.G.3    Collier, J.L.4
  • 23
    • 0028844985 scopus 로고
    • Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus
    • Hecht, G.B., and Newton, A. (1995) Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus. J Bacteriol 177: 6223-6229.
    • (1995) J Bacteriol , vol.177 , pp. 6223-6229
    • Hecht, G.B.1    Newton, A.2
  • 24
    • 0033941615 scopus 로고    scopus 로고
    • Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1
    • Janiak-Spens, F., and West, A.M. (2000) Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1. Mol Microbiol 37: 136-144.
    • (2000) Mol Microbiol , vol.37 , pp. 136-144
    • Janiak-Spens, F.1    West, A.M.2
  • 25
    • 0035980822 scopus 로고    scopus 로고
    • Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Kaneko, T., Nakamura, Y., Wolk, C.P., Kuritz, T., Sasamoto, S., Watanabe, A., et al. (2001) Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 8: 205-213.
    • (2001) DNA Res , vol.8 , pp. 205-213
    • Kaneko, T.1    Nakamura, Y.2    Wolk, C.P.3    Kuritz, T.4    Sasamoto, S.5    Watanabe, A.6
  • 26
    • 0033591455 scopus 로고    scopus 로고
    • Activation of a cyanobacterial adenylate cyclase, CyaC, by autophosphorylation and a subsequent phosphotransfer reaction
    • Kasahara, M., and Ohmori, M. (1999) Activation of a cyanobacterial adenylate cyclase, CyaC, by autophosphorylation and a subsequent phosphotransfer reaction. J Biol Chem 274: 15167-15172.
    • (1999) J Biol Chem , vol.274 , pp. 15167-15172
    • Kasahara, M.1    Ohmori, M.2
  • 27
    • 0028526272 scopus 로고
    • Complementary chromatic adaptation: Photoperception to gene regulation
    • Kehoe, D.M., and Grossman, A.R. (1994) Complementary chromatic adaptation: photoperception to gene regulation. Semin Cell Dev Biol 5: 303-313.
    • (1994) Semin Cell Dev Biol , vol.5 , pp. 303-313
    • Kehoe, D.M.1    Grossman, A.R.2
  • 28
    • 0029818880 scopus 로고    scopus 로고
    • Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors
    • Kehoe, D.M., and Grossman, A.R. (1996) Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors. Science 273: 1409-1412.
    • (1996) Science , vol.273 , pp. 1409-1412
    • Kehoe, D.M.1    Grossman, A.R.2
  • 29
    • 0030912553 scopus 로고    scopus 로고
    • New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system
    • Kehoe, D.M., and Grossman, A.R. (1997) New classes of mutants in complementary chromatic adaptation provide evidence for a novel four-step phosphorelay system. J Bacteriol 179: 3914-3921.
    • (1997) J Bacteriol , vol.179 , pp. 3914-3921
    • Kehoe, D.M.1    Grossman, A.R.2
  • 30
    • 0031721898 scopus 로고    scopus 로고
    • Use of molecular genetics to investigate complementary chromatic adaptation: Advances in transformation and complementation
    • Kehoe, D.M., and Grossman, A.R. (1998) Use of molecular genetics to investigate complementary chromatic adaptation: advances in transformation and complementation. Methods Enzymol 297: 279-290.
    • (1998) Methods Enzymol , vol.297 , pp. 279-290
    • Kehoe, D.M.1    Grossman, A.R.2
  • 31
    • 0029026859 scopus 로고
    • Phosphorylation-dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli
    • Kenny, L.J., Bauer, M.D., and Silhavy, T.J. (1995) Phosphorylation- dependent conformational changes in OmpR, an osmoregulatory DNA-binding protein of Escherichia coli. Proc Natl Acad Sci USA 92: 8866-88760.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8866-88760
    • Kenny, L.J.1    Bauer, M.D.2    Silhavy, T.J.3
  • 32
    • 0027162310 scopus 로고
    • Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein
    • Klose, K.E., Weiss, D.S., and Kustu, S. (1993) Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. J Mol Biol 232: 67-78.
    • (1993) J Mol Biol , vol.232 , pp. 67-78
    • Klose, K.E.1    Weiss, D.S.2    Kustu, S.3
  • 33
    • 0034123699 scopus 로고    scopus 로고
    • Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli
    • Kwon, O., Georgellis, D., and Lin, E.C.C. (2000) Phosphorelay as the sole physiological route of signal transmission by the arc two-component system of Escherichia coli. J Bacteriol 182: 3858-3862.
    • (2000) J Bacteriol , vol.182 , pp. 3858-3862
    • Kwon, O.1    Georgellis, D.2    Lin, E.C.C.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmll, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmll, U.K.1
  • 35
    • 0031973725 scopus 로고    scopus 로고
    • Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR
    • Lan, C.-Y., and Igo, M.M. (1998) Differential expression of the OmpF and OmpC porin proteins in Escherichia coli K-12 depends upon the level of active OmpR. J Bacteriol 180: 171-174.
    • (1998) J Bacteriol , vol.180 , pp. 171-174
    • Lan, C.-Y.1    Igo, M.M.2
  • 36
    • 0023183344 scopus 로고
    • Isolation and characterization of light-regulated phycobilisome linker polypeptide genes and their transcription as a polycistronic mRNA
    • Lomax, T.L., Conley, P.B., Schilling, J., and Grossman, A.R. (1987) Isolation and characterization of light-regulated phycobilisome linker polypeptide genes and their transcription as a polycistronic mRNA. J Bacteriol 169: 2675-2684.
    • (1987) J Bacteriol , vol.169 , pp. 2675-2684
    • Lomax, T.L.1    Conley, P.B.2    Schilling, J.3    Grossman, A.R.4
  • 37
    • 0023047208 scopus 로고
    • Green light induces transcription of the phycoerythrin operon in the cyanobacterium Calothrix 7601
    • Mazel, D., Guglielmi, G., Houmard, J., Sidler, W., Bryant, D.A., and Tandeau de Marsac, N. (1986) Green light induces transcription of the phycoerythrin operon in the cyanobacterium Calothrix 7601. Nucleic Acids Res 14: 8279-8290.
    • (1986) Nucleic Acids Res , vol.14 , pp. 8279-8290
    • Mazel, D.1    Guglielmi, G.2    Houmard, J.3    Sidler, W.4    Bryant, D.A.5    Tandeau De Marsac, N.6
  • 38
    • 0035707917 scopus 로고    scopus 로고
    • An overview of the genome of Nostoc punctiforme, a multicellular, symbiotic cyanobacterium
    • Meeks, J.C., Elhai, J., Thiel, T., Potts, M., Larimer, F., Lamerdin, J., et al. (2001) An overview of the genome of Nostoc punctiforme, a multicellular, symbiotic cyanobacterium. Photosynth Res 70: 85-106.
    • (2001) Photosynth Res , vol.70 , pp. 85-106
    • Meeks, J.C.1    Elhai, J.2    Thiel, T.3    Potts, M.4    Larimer, F.5    Lamerdin, J.6
  • 39
    • 0036428641 scopus 로고    scopus 로고
    • Cellular differentiation in the cyanobacterium Nostoc punctiforme
    • Meeks, J.C., Campbell, E.L., Summers, M.L., and Wong, F.C. (2002) Cellular differentiation in the cyanobacterium Nostoc punctiforme. Arch Microbiol 178: 395-403.
    • (2002) Arch Microbiol , vol.178 , pp. 395-403
    • Meeks, J.C.1    Campbell, E.L.2    Summers, M.L.3    Wong, F.C.4
  • 40
    • 6044223542 scopus 로고    scopus 로고
    • AplA, a member of a new class of phycobiliproteins lacking a traditional role in photosynthetic light harvesting
    • Montgomery, B.L., Casey, E.S., Grossman, A.R., and Kehoe, D.M. (2004) AplA, a member of a new class of phycobiliproteins lacking a traditional role in photosynthetic light harvesting. J Bacteriol 186: 7420-7428.
    • (2004) J Bacteriol , vol.186 , pp. 7420-7428
    • Montgomery, B.L.1    Casey, E.S.2    Grossman, A.R.3    Kehoe, D.M.4
  • 41
    • 0027262522 scopus 로고
    • Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli
    • Moore, J.B., Shiau, S.-P., and Reitzer, L.J. (1993) Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli. J Bacteriol 175: 2692-2701.
    • (1993) J Bacteriol , vol.175 , pp. 2692-2701
    • Moore, J.B.1    Shiau, S.-P.2    Reitzer, L.J.3
  • 42
    • 0023984847 scopus 로고
    • Optimal alignments in linear space
    • Myers, E.W., and Miller, W. (1989) Optimal alignments in linear space. CABIOS 4: 11-17.
    • (1989) CABIOS , vol.4 , pp. 11-17
    • Myers, E.W.1    Miller, W.2
  • 43
    • 11144288242 scopus 로고    scopus 로고
    • Characterization of genes encoding multi-domain proteins in the genome of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Narikawa, R., Okamoto, S., Ikeuchi, M., and Ohmori, M. (2004) Characterization of genes encoding multi-domain proteins in the genome of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 11: 69-81.
    • (2004) DNA Res , vol.11 , pp. 69-81
    • Narikawa, R.1    Okamoto, S.2    Ikeuchi, M.3    Ohmori, M.4
  • 44
    • 0008085210 scopus 로고
    • Changes in accumulation and synthesis of transcripts encoding phycobilisome components during acclimation of Fremyella diplosiphon to different light qualities
    • Oelmüller, R., Conley, P.B., Federspiel, N., Briggs, W.R., and Grossman, A.R. (1988) Changes in accumulation and synthesis of transcripts encoding phycobilisome components during acclimation of Fremyella diplosiphon to different light qualities. Plant Physiol 88: 1077-1083.
    • (1988) Plant Physiol , vol.88 , pp. 1077-1083
    • Oelmüller, R.1    Conley, P.B.2    Federspiel, N.3    Briggs, W.R.4    Grossman, A.R.5
  • 45
    • 0035981243 scopus 로고    scopus 로고
    • Characterization of genes encoding multi-domain proteins in the genome of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Ohmori, M., Ikeuchi, M., Sato, N., Wolk, P., Kaneko, T., Ogawa, T., et al. (2001) Characterization of genes encoding multi-domain proteins in the genome of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 8: 271-284.
    • (2001) DNA Res , vol.8 , pp. 271-284
    • Ohmori, M.1    Ikeuchi, M.2    Sato, N.3    Wolk, P.4    Kaneko, T.5    Ogawa, T.6
  • 46
    • 0002113982 scopus 로고
    • Genetic approaches for signaling pathways and proteins
    • Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society for Microbiology Press
    • Parkinson, J.S. (1995) Genetic approaches for signaling pathways and proteins. In: Two-Component Signal Transduction. Hoch, J.A., and Silhavy, T.J. (eds). Washington, DC: American Society for Microbiology Press, pp. 9-23.
    • (1995) Two-Component Signal Transduction , pp. 9-23
    • Parkinson, J.S.1
  • 47
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson, W.R. (1990) Rapid and sensitive sequence comparison with FASTP and FASTA. Methods Enzymol 183: 63-98.
    • (1990) Methods Enzymol , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 48
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W.R., and Lipman, D.J. (1988) Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 85: 2444-2448.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 49
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 'two-component' osmosensor
    • Posas, F., Wurgler-Murphy, S.M., Maeda, T., Witten, E.A., Thai, T.C., and Saito, H. (1996) Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 'two-component' osmosensor. Cell 86: 865-875.
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 50
    • 0036443740 scopus 로고    scopus 로고
    • The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis
    • Ryan, K.R., Judd, E.M., and Shapiro, L. (2002) The CtrA response regulator essential for Caulobacter crescentus cell-cycle progression requires a bipartite degradation signal for temporally controlled proteolysis. J Mol Biol 324: 443-455.
    • (2002) J Mol Biol , vol.324 , pp. 443-455
    • Ryan, K.R.1    Judd, E.M.2    Shapiro, L.3
  • 51
    • 0037443967 scopus 로고    scopus 로고
    • Glutamate at the phosphorylation site of response regulator CtrA provides essential activities without increasing DNA binding
    • Saim, R., and Marczynski, G.T. (2003) Glutamate at the phosphorylation site of response regulator CtrA provides essential activities without increasing DNA binding. Nucleic Acids Res 31: 1775-1779.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1775-1779
    • Saim, R.1    Marczynski, G.T.2
  • 53
    • 0036154464 scopus 로고    scopus 로고
    • A Turquoise mutant genetically separates expression of genes encoding phycoerythrin and its associated linker peptides
    • Seib, L.O., and Kehoe, D.M. (2002) A Turquoise mutant genetically separates expression of genes encoding phycoerythrin and its associated linker peptides. J Bacteriol 184: 962-970.
    • (2002) J Bacteriol , vol.184 , pp. 962-970
    • Seib, L.O.1    Kehoe, D.M.2
  • 54
    • 0001792698 scopus 로고
    • Two-component signal transduction systems: Structure-function relationships and mechanisms of catalysis
    • Hoch, J.A., and Silhavy, T.J. (eds). Washington DC: American Society for Microbiology Press
    • Stock, J.B., Surette, M.G., Levit, M., and Park, P. (1995) Two-component signal transduction systems: structure-function relationships and mechanisms of catalysis. In: Two-Component Signal Transduction. Hoch, J.A., and Silhavy, T.J. (eds). Washington DC: American Society for Microbiology Press, pp. 25-51.
    • (1995) Two-Component Signal Transduction , pp. 25-51
    • Stock, J.B.1    Surette, M.G.2    Levit, M.3    Park, P.4
  • 55
    • 3242788085 scopus 로고    scopus 로고
    • Signal transduction during light-quality acclimation in cyanobacteria: A model system for understanding phytochrome-response pathways in prokaryotes
    • Stowe-Evans, E.L., and Kehoe, D.M. (2004) Signal transduction during light-quality acclimation in cyanobacteria: a model system for understanding phytochrome-response pathways in prokaryotes. J Photochem Photobiol 3: 495-502.
    • (2004) J Photochem Photobiol , vol.3 , pp. 495-502
    • Stowe-Evans, E.L.1    Kehoe, D.M.2
  • 56
    • 0000774691 scopus 로고
    • Phycobilisomes and complementary chromatic adaptation in cyanobacteria
    • Tandeau de Marsac, N. (1983) Phycobilisomes and complementary chromatic adaptation in cyanobacteria. Bull Inst Pasteur 81: 201-254.
    • (1983) Bull Inst Pasteur , vol.81 , pp. 201-254
    • Tandeau De Marsac, N.1
  • 57
    • 0027397937 scopus 로고
    • Adaptation of cyanobacteria to environmental stimuli: New steps towards molecular mechanisms
    • Tandeau de Marsac, N., and Houmard, J. (1993) Adaptation of cyanobacteria to environmental stimuli: new steps towards molecular mechanisms. FEMS Microbiol Rev 104: 119-190.
    • (1993) FEMS Microbiol Rev , vol.104 , pp. 119-190
    • Tandeau De Marsac, N.1    Houmard, J.2
  • 58
    • 0942268739 scopus 로고    scopus 로고
    • RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness
    • Terauchi, K., Montgomery, B.L., Grossman, A.R., Lagarias, J.C., and Kehoe, D.M. (2004) RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness. Mol Microbiol 51: 567-577.
    • (2004) Mol Microbiol , vol.51 , pp. 567-577
    • Terauchi, K.1    Montgomery, B.L.2    Grossman, A.R.3    Lagarias, J.C.4    Kehoe, D.M.5
  • 59
    • 1942440975 scopus 로고    scopus 로고
    • PsfR, a factor that stimulates psbAI expression in the cyanobacterium Synechococcus elongatus PCC 7942
    • Thomas, C., Andersson, C.R., Canales, S.R., and Golden, S.S. (2004) PsfR, a factor that stimulates psbAI expression in the cyanobacterium Synechococcus elongatus PCC 7942. Microbiology 150: 1031-1040.
    • (2004) Microbiology , vol.150 , pp. 1031-1040
    • Thomas, C.1    Andersson, C.R.2    Canales, S.R.3    Golden, S.S.4
  • 60
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 61
    • 0029968548 scopus 로고    scopus 로고
    • Identification and characterization of FrzZ, a novel response regulator necessary for swarming and fruiting-body formation in Myxococcus xanthus
    • Trudeau, K.G., Ward, M.J., and Zusman, D.R. (1996) Identification and characterization of FrzZ, a novel response regulator necessary for swarming and fruiting-body formation in Myxococcus xanthus. Mol Microbiol 20: 645-655.
    • (1996) Mol Microbiol , vol.20 , pp. 645-655
    • Trudeau, K.G.1    Ward, M.J.2    Zusman, D.R.3
  • 62
    • 0027977068 scopus 로고
    • Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS signal transduction cascade
    • Uhl, M.A., and Miller, J.F. (1994) Autophosphorylation and phosphotransfer in the Bordetella pertussis BvgAS signal transduction cascade. Proc Natl Acad Sci USA 91: 1163-1167.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1163-1167
    • Uhl, M.A.1    Miller, J.F.2
  • 63
    • 0029871035 scopus 로고    scopus 로고
    • Integration of multiple domains in a two-component sensor protein: The Bordetella pertussis BvgAS phosphorelay
    • Uhl, M.A., and Miller, J.F. (1996a) Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay. EMBO J 15: 1028-1036.
    • (1996) EMBO J , vol.15 , pp. 1028-1036
    • Uhl, M.A.1    Miller, J.F.2
  • 64
    • 0030466066 scopus 로고    scopus 로고
    • Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay
    • Uhl, M.A., and Miller, J.F. (1996b) Central role of the BvgS receiver as a phosphorylated intermediate in a complex two-component phosphorelay. J Biol Chem 271: 33176-33180.
    • (1996) J Biol Chem , vol.271 , pp. 33176-33180
    • Uhl, M.A.1    Miller, J.F.2
  • 65
    • 14844305591 scopus 로고    scopus 로고
    • Signal transmission and specificity in the sporulation phosphorelay of Bacillus subtilis
    • Inouya, M., and Dutta, R. (eds). San Diego, CA: Academic Press
    • Varughese, L.I. (2003) Signal transmission and specificity in the sporulation phosphorelay of Bacillus subtilis. In: Histidine Kinases in Signal Transduction. Inouya, M., and Dutta, R. (eds). San Diego, CA: Academic Press, pp. 204-218.
    • (2003) Histidine Kinases in Signal Transduction , pp. 204-218
    • Varughese, L.I.1
  • 66
    • 0027366420 scopus 로고
    • Structural conservation in the CheY superfamily
    • Volz, K. (1993) Structural conservation in the CheY superfamily. Biochemistry 32: 11741-11753.
    • (1993) Biochemistry , vol.32 , pp. 11741-11753
    • Volz, K.1
  • 67
    • 0036334570 scopus 로고    scopus 로고
    • Phosphorylation of the Pseudomonas aeruginosa response regulator AlgR is essential for type IV fimbria-mediated twitching motility
    • Whitchurch, C.B., Erova, T.E., Emery, J.A., Sargent, J.L., Harris, J.M., Semmler, A.B.T., et al. (2002) Phosphorylation of the Pseudomonas aeruginosa response regulator AlgR is essential for type IV fimbria-mediated twitching motility. J Bacteriol 184: 4544-4554.
    • (2002) J Bacteriol , vol.184 , pp. 4544-4554
    • Whitchurch, C.B.1    Erova, T.E.2    Emery, J.A.3    Sargent, J.L.4    Harris, J.M.5    Semmler, A.B.T.6
  • 68
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wootton, J.C., and Drummond, M.H. (1989) The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng 2: 535-543.
    • (1989) Protein Eng , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.