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Volumn 53, Issue 7, 2012, Pages 1255-1266

Characterization of the subdomains in the N-terminal region of histidine kinase Hik33 in the cyanobacterium synechocystis sp. PCC 6803

Author keywords

Chimeric protein; Cyanobacterium; Sensory kinase; Signal perception; Synechocystis; Two component system

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; PAS DOMAIN KINASES; PROTEIN HISTIDINE KINASE; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; PROTEIN-HISTIDINE KINASE;

EID: 84863913438     PISSN: 00320781     EISSN: 14719053     Source Type: Journal    
DOI: 10.1093/pcp/pcs068     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 0027511714 scopus 로고
    • Sensor and regulator proteins from the cyanobacterium Synechocystis species PCC7942 that belong to the bacterial signal-transduction protein families: Implication in the adaptive response to phosphate limitation
    • Aiba, H., Nagaya, M. and Mizuno, T. (1993) Sensor and regulator proteins from the cyanobacterium Synechocystis species PCC7942 that belong to the bacterial signal-transduction protein families: implication in the adaptive response to phosphate limitation. Mol. Microbiol. 8: 81-91.
    • (1993) Mol. Microbiol. , vol.8 , pp. 81-91
    • Aiba, H.1    Nagaya, M.2    Mizuno, T.3
  • 2
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L. and Ponting, C.P. (1999) The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176: 111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 3
    • 56249132984 scopus 로고    scopus 로고
    • Changes in quaternary structure in the signaling mechanisms of PAS domains
    • Ayers, R.A. and Moffat, K. (2008) Changes in quaternary structure in the signaling mechanisms of PAS domains. Biochemistry 47: 12078-12086.
    • (2008) Biochemistry , vol.47 , pp. 12078-12086
    • Ayers, R.A.1    Moffat, K.2
  • 4
    • 34247348691 scopus 로고    scopus 로고
    • A subset of GAF domains are evolutionarily conserved sodium sensors
    • Cann, M. (2007) A subset of GAF domains are evolutionarily conserved sodium sensors. Mol. Microbiol. 64: 461-472.
    • (2007) Mol. Microbiol. , vol.64 , pp. 461-472
    • Cann, M.1
  • 6
    • 77957051006 scopus 로고
    • Complementary chromatic adaptation: Physiological conditions and action spectra
    • Demarsac, N.T. and Houmard, J. (1988) Complementary chromatic adaptation: physiological conditions and action spectra. Methods Enzymol. 167: 318-328.
    • (1988) Methods Enzymol. , vol.167 , pp. 318-328
    • Demarsac, N.T.1    Houmard, J.2
  • 7
    • 33845427412 scopus 로고    scopus 로고
    • NrrA directly regulates expression of hetR during heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120
    • Ehira, S. and Ohmori, M. (2006) NrrA directly regulates expression of hetR during heterocyst differentiation in the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 188: 8520-8525.
    • (2006) J. Bacteriol. , vol.188 , pp. 8520-8525
    • Ehira, S.1    Ohmori, M.2
  • 8
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP domain structure implies helix rotation in transmembrane signaling
    • Hulko, M., Berndt, F., Gruber, M., Linder, J.U., Truffault, V., Schultz, A. et al. (2006) The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126: 929-940.
    • (2006) Cell , vol.126 , pp. 929-940
    • Hulko, M.1    Berndt, F.2    Gruber, M.3    Linder, J.U.4    Truffault, V.5    Schultz, A.6
  • 9
    • 0345600953 scopus 로고    scopus 로고
    • Structural analysis of four large plasmids harboring in a unicellular cyanobacterium, Synechocystis sp. PCC 6803
    • Kaneko, T., Nakamura, Y., Sasamoto, S., Watanabe, A., Kohara, M., Matsumoto, M. et al. (2003) Structural analysis of four large plasmids harboring in a unicellular cyanobacterium, Synechocystis sp. PCC 6803. DNA Res. 10: 221-228.
    • (2003) DNA Res. , vol.10 , pp. 221-228
    • Kaneko, T.1    Nakamura, Y.2    Sasamoto, S.3    Watanabe, A.4    Kohara, M.5    Matsumoto, M.6
  • 10
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y. et al. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3: 109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 11
    • 33846068839 scopus 로고    scopus 로고
    • Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803
    • Kanesaki, Y., Yamamoto, H., Paithoonrangsarid, K., Shoumskaya, M., Suzuki, I., Hayashi, H. et al. (2007) Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803. Plant J. 49: 313-324.
    • (2007) Plant J. , vol.49 , pp. 313-324
    • Kanesaki, Y.1    Yamamoto, H.2    Paithoonrangsarid, K.3    Shoumskaya, M.4    Suzuki, I.5    Hayashi, H.6
  • 12
    • 69949135353 scopus 로고    scopus 로고
    • Function of the N-terminal region of the phosphate-sensing histidine kinase, SphS, in Synechocystis sp. PCC 6803
    • Kimura, S., Shiraiwa, Y. and Suzuki, I. (2009) Function of the N-terminal region of the phosphate-sensing histidine kinase, SphS, in Synechocystis sp. PCC 6803. Microbiology 155: 2256-2264.
    • (2009) Microbiology , vol.155 , pp. 2256-2264
    • Kimura, S.1    Shiraiwa, Y.2    Suzuki, I.3
  • 13
    • 18644372435 scopus 로고    scopus 로고
    • Cis-trans isomerase gene in psychrophilic Pseudomonas syringae is constitutively expressed during growth and under conditions of temperature and solvent stress
    • Kiran, M.D., Annapoorni, S., Suzuki, I., Murata, N. and Shivaji, S. (2005) Cis-trans isomerase gene in psychrophilic Pseudomonas syringae is constitutively expressed during growth and under conditions of temperature and solvent stress. Extremophiles 9: 117-125.
    • (2005) Extremophiles , vol.9 , pp. 117-125
    • Kiran, M.D.1    Annapoorni, S.2    Suzuki, I.3    Murata, N.4    Shivaji, S.5
  • 14
    • 0034608882 scopus 로고    scopus 로고
    • The histidine kinase-related domain participates in phytochrome B function but is dispensable
    • Krall, L. and Reed, J.W. (2000) The histidine kinase-related domain participates in phytochrome B function but is dispensable. Proc. Natl Acad. Sci. USA 97: 8169-8174.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8169-8174
    • Krall, L.1    Reed, J.W.2
  • 15
    • 41449111029 scopus 로고    scopus 로고
    • Changes at the KinA PAS-A dimerization interface influence histidine kinase function
    • Lee, J., Tomchick, D.R., Brautigam, C.A., Machius, M., Kort, R., Hellingwerf, K.J. et al. (2008) Changes at the KinA PAS-A dimerization interface influence histidine kinase function. Biochemistry 47: 4051-4064.
    • (2008) Biochemistry , vol.47 , pp. 4051-4064
    • Lee, J.1    Tomchick, D.R.2    Brautigam, C.A.3    MacHius, M.4    Kort, R.5    Hellingwerf, K.J.6
  • 16
    • 0036194664 scopus 로고    scopus 로고
    • A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803
    • López-Maury, L., Garća-Doḿnguez, M., Florencio, F.J. and Reyes, J.C. (2002) A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803. Mol. Microbiol. 43: 247-256.
    • (2002) Mol. Microbiol. , vol.43 , pp. 247-256
    • López-Maury, L.1    Garća-Doḿnguez, M.2    Florencio, F.J.3    Reyes, J.C.4
  • 17
  • 18
    • 0041305844 scopus 로고    scopus 로고
    • Identification of histidine kinases that act as sensors in the perception of salt stress in Synechocystis sp. PCC 6803
    • Marin, K., Suzuki, I., Yamaguchi, K., Ribbeck, K., Yamamoto, H., Kanesaki, Y. et al. (2003) Identification of histidine kinases that act as sensors in the perception of salt stress in Synechocystis sp. PCC 6803. Proc. Natl Acad. Sci. USA 100: 9061-9066.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9061-9066
    • Marin, K.1    Suzuki, I.2    Yamaguchi, K.3    Ribbeck, K.4    Yamamoto, H.5    Kanesaki, Y.6
  • 19
    • 63649126694 scopus 로고    scopus 로고
    • Functional in vitro assembly of the integral membrane bacterial thermosensor DesK
    • Mart́n, M., Albanesi, D., Alzari, P.M. and de Mendoza, D. (2009) Functional in vitro assembly of the integral membrane bacterial thermosensor DesK. Protein Expr. Purif. 66: 39-45.
    • (2009) Protein Expr. Purif. , vol.66 , pp. 39-45
    • Mart́n, M.1    Albanesi, D.2    Alzari, P.M.3    De Mendoza, D.4
  • 20
    • 0036433494 scopus 로고    scopus 로고
    • The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp PCC 6803
    • Mikami, K., Kanesaki, Y., Suzuki, I. and Murata, N. (2002) The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp PCC 6803. Mol. Microbiol. 46: 905-915.
    • (2002) Mol. Microbiol. , vol.46 , pp. 905-915
    • Mikami, K.1    Kanesaki, Y.2    Suzuki, I.3    Murata, N.4
  • 21
    • 0030608407 scopus 로고    scopus 로고
    • Compilation of all genes encoding bacterial two-component signal transducers in the genome of the cyanobacterium, Synechocystis sp. strain PCC 6803
    • Mizuno, T., Kaneko, T. and Tabata, S. (1996) Compilation of all genes encoding bacterial two-component signal transducers in the genome of the cyanobacterium, Synechocystis sp. strain PCC 6803. DNA Res. 3: 407-414.
    • (1996) DNA Res. , vol.3 , pp. 407-414
    • Mizuno, T.1    Kaneko, T.2    Tabata, S.3
  • 22
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of light-regulated histidine kinases
    • Möglich, A., Ayers, R.A. and Moffat, K. (2009) Design and signaling mechanism of light-regulated histidine kinases. J. Mol. Biol. 385: 1433-1444.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 23
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a hemebinding oxygen-sensing domain and a functional C-terminal kinase domain
    • Monson, E.K., Weinstein, M., Ditta, G.S. and Helinski, D.R. (1992) The FixL protein of Rhizobium meliloti can be separated into a hemebinding oxygen-sensing domain and a functional C-terminal kinase domain. Proc. Natl Acad. Sci. USA 89: 4280-4284.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 24
    • 30344453059 scopus 로고    scopus 로고
    • Exploitation of genomic sequences in a systematic analysis to access how cyanobacteria sense environmental stress
    • Murata, N. and Suzuki, I. (2006) Exploitation of genomic sequences in a systematic analysis to access how cyanobacteria sense environmental stress. J. Exp. Bot. 57: 235-247.
    • (2006) J. Exp. Bot. , vol.57 , pp. 235-247
    • Murata, N.1    Suzuki, I.2
  • 25
    • 0027305566 scopus 로고
    • Cloning of a sensorykinase-encoding gene that belongs to the two-component regulatory family from the cyanobacterium Synechococcus sp. PCC7942
    • Nagaya, M., Aiba, H. and Mizuno, T. (1993) Cloning of a sensorykinase-encoding gene that belongs to the two-component regulatory family from the cyanobacterium Synechococcus sp. PCC7942. Gene 131: 119-124.
    • (1993) Gene , vol.131 , pp. 119-124
    • Nagaya, M.1    Aiba, H.2    Mizuno, T.3
  • 26
    • 19944425793 scopus 로고    scopus 로고
    • Five histidine kinases perceive osmotic stress and regulate distinct sets of genes in Synechocystis
    • Paithoonrangsarid, K., Shoumskaya, M.A., Kanesaki, Y., Satoh, S., Tabata, S., Los, D.A. et al. (2004) Five histidine kinases perceive osmotic stress and regulate distinct sets of genes in Synechocystis. J. Biol. Chem. 279: 53078-53086.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53078-53086
    • Paithoonrangsarid, K.1    Shoumskaya, M.A.2    Kanesaki, Y.3    Satoh, S.4    Tabata, S.5    Los, D.A.6
  • 27
    • 0031262875 scopus 로고    scopus 로고
    • PAS: A multifunctional domain family comes to light
    • Ponting, C.P. and Aravind, L. (1997) PAS: a multifunctional domain family comes to light. Curr. Biol. 7: R674-R677.
    • (1997) Curr. Biol. , vol.7
    • Ponting, C.P.1    Aravind, L.2
  • 28
    • 66849106736 scopus 로고    scopus 로고
    • Chloroplast two-component systems: Evolution of the link between photosynthesis and gene expression
    • Puthiyaveetil, S. and Allen, J.F. (2009) Chloroplast two-component systems: evolution of the link between photosynthesis and gene expression. Proc. Biol. Sci. 276: 2133-2145.
    • (2009) Proc. Biol. Sci. , vol.276 , pp. 2133-2145
    • Puthiyaveetil, S.1    Allen, J.F.2
  • 29
    • 0038153182 scopus 로고    scopus 로고
    • Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure
    • Reiser, V., Raitt, D.C. and Saito, H. (2003) Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. J. Cell Biol. 161: 1035-1040.
    • (2003) J. Cell Biol. , vol.161 , pp. 1035-1040
    • Reiser, V.1    Raitt, D.C.2    Saito, H.3
  • 30
  • 31
    • 68949130186 scopus 로고    scopus 로고
    • A Synechocystis homolog of SipA protein, Ssl3451, enhances the activity of the histidine kinase Hik33
    • Sakayori, T., Shiraiwa, Y. and Suzuki, I. (2009) A Synechocystis homolog of SipA protein, Ssl3451, enhances the activity of the histidine kinase Hik33. Plant Cell Physiol. 50: 1439-1448.
    • (2009) Plant Cell Physiol. , vol.50 , pp. 1439-1448
    • Sakayori, T.1    Shiraiwa, Y.2    Suzuki, I.3
  • 32
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • Salomon, M., Christie, J.M., Knieb, E., Lempert, U. and Briggs, W.R. (2000) Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39: 9401-9410.
    • (2000) Biochemistry , vol.39 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 33
    • 37549025443 scopus 로고    scopus 로고
    • Induction of a group 2 s factor, RPOD3, by high light and the underlying mechanism in Synechococcus elongatus PCC 7942
    • Seki, A., Hanaoka, M., Akimoto, Y., Masuda, S., Iwasaki, H. and Tanaka, K. (2007) Induction of a group 2 s factor, RPOD3, by high light and the underlying mechanism in Synechococcus elongatus PCC 7942. J. Biol. Chem. 282: 36887-36894.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36887-36894
    • Seki, A.1    Hanaoka, M.2    Akimoto, Y.3    Masuda, S.4    Iwasaki, H.5    Tanaka, K.6
  • 34
    • 20444367654 scopus 로고    scopus 로고
    • Identical Hik-Rre systems are involved in perception and transduction of salt signals and hyperosmotic signals but regulate the expression of individual genes to different extents in Synechocystis
    • Shoumskaya, M.A., Paithoonrangsarid, K., Kanesaki, Y., Los, D.A., Zinchenko, V.V., Tanticharoen, M. et al. (2005) Identical Hik-Rre systems are involved in perception and transduction of salt signals and hyperosmotic signals but regulate the expression of individual genes to different extents in Synechocystis. J. Biol. Chem. 280: 21531-21538.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21531-21538
    • Shoumskaya, M.A.1    Paithoonrangsarid, K.2    Kanesaki, Y.3    Los, D.A.4    Zinchenko, V.V.5    Tanticharoen, M.6
  • 35
  • 36
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue-green algae (order Chroococcales
    • Stanier, R.Y., Kunisawa, R., Mandel, M. and Cohen-Bazire, G. (1971) Purification and properties of unicellular blue-green algae (order Chroococcales). Bacteriol. Rev. 35: 171-205.
    • (1971) Bacteriol. Rev. , vol.35 , pp. 171-205
    • Stanier, R.Y.1    Kunisawa, R.2    Mandel, M.3    Cohen-Bazire, G.4
  • 38
    • 0035051326 scopus 로고    scopus 로고
    • Cold-regulated genes under control of the cold sensor Hik33 in Synechocystis
    • Suzuki, I., Kanesaki, Y., Mikami, K., Kanehisa, M. and Murata, N. (2001) Cold-regulated genes under control of the cold sensor Hik33 in Synechocystis. Mol. Microbiol. 40: 235-244.
    • (2001) Mol. Microbiol. , vol.40 , pp. 235-244
    • Suzuki, I.1    Kanesaki, Y.2    Mikami, K.3    Kanehisa, M.4    Murata, N.5
  • 39
    • 0342546000 scopus 로고    scopus 로고
    • The pathway for perception and transduction of low-temperature signals in Synechocystis
    • Suzuki, I., Los, D.A., Kanesaki, Y., Mikami, K. and Murata, N. (2000) The pathway for perception and transduction of low-temperature signals in Synechocystis. EMBO J. 19: 1327-1334.
    • (2000) EMBO J. , vol.19 , pp. 1327-1334
    • Suzuki, I.1    Los, D.A.2    Kanesaki, Y.3    Mikami, K.4    Murata, N.5
  • 40
    • 1842424639 scopus 로고    scopus 로고
    • The SphS-SphR two component system is the exclusive sensor for the induction of gene expression in response to phosphate limitation in Synechocystis
    • Suzuki, S., Ferjani, A., Suzuki, I. and Murata, N. (2004) The SphS-SphR two component system is the exclusive sensor for the induction of gene expression in response to phosphate limitation in Synechocystis. J. Biol. Chem. 279: 13234-13240.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13234-13240
    • Suzuki, S.1    Ferjani, A.2    Suzuki, I.3    Murata, N.4
  • 41
    • 79960654163 scopus 로고    scopus 로고
    • Structural characterization of AS1-membrane interactions from a subset of HAMP domains
    • Unnerstale, S., Maler, L. and Draheim, R.R. (2011) Structural characterization of AS1-membrane interactions from a subset of HAMP domains. Biochim. Biophys. Acta 1808: 2403-2412.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2403-2412
    • Unnerstale, S.1    Maler, L.2    Draheim, R.R.3
  • 42
    • 0036231347 scopus 로고    scopus 로고
    • NblS, a gene involved in controlling photosynthesis-related gene expression during high light and nutrient stress in Synechococcus elongatus PCC 7942
    • Van Waasbergen, L.G., Dolganov, N. and Grossman, A.R. (2002) nblS, a gene involved in controlling photosynthesis-related gene expression during high light and nutrient stress in Synechococcus elongatus PCC 7942. J. Bacteriol. 184: 2481-2490.
    • (2002) J. Bacteriol. , vol.184 , pp. 2481-2490
    • Van Waasbergen, L.G.1    Dolganov, N.2    Grossman, A.R.3
  • 43
    • 77957024978 scopus 로고
    • Construction of specific mutations in photosystem II photosynthetic reaction center by geneticengineering methods in Synechocystis 6803
    • Williams, J.G.K. (1988) Construction of specific mutations in photosystem II photosynthetic reaction center by geneticengineering methods in Synechocystis 6803. Methods Enzymol. 167: 766-778.
    • (1988) Methods Enzymol. , vol.167 , pp. 766-778
    • Williams, J.G.K.1
  • 44
    • 34250857579 scopus 로고    scopus 로고
    • The design and development of Tar-EnvZ chimeric receptors
    • Yoshida, T., Phadtare, S. and Inouye, M. (2007) The design and development of Tar-EnvZ chimeric receptors. Methods Enzymol. 423: 166-183.
    • (2007) Methods Enzymol. , vol.423 , pp. 166-183
    • Yoshida, T.1    Phadtare, S.2    Inouye, M.3
  • 45
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F. and Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3


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