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Volumn 8, Issue 3, 2003, Pages 287-296

ATP-induced hexameric ring structure of the cyanobacterial circadian clock protein KaiC

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BINDING PROTEIN; CHAPERONE; GUANINE NUCLEOTIDE BINDING PROTEIN; HELICASE; KAIA PROTEIN; KAIB PROTEIN; KAIC PROTEIN; NUCLEOTIDE; PHOSPHATE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 0348026753     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2443.2003.00633.x     Document Type: Article
Times cited : (117)

References (28)
  • 1
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G., Lutter, R. & Walker, J.E. (1994) Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 2
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Beuron, F., Maurizi, M.R., Belnap, D.M., et al. (1998) At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123, 248-259.
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, F.1    Maurizi, M.R.2    Belnap, D.M.3
  • 4
    • 0035830896 scopus 로고    scopus 로고
    • RNA passes through the hole of the protein hexamer in the complex with the Escherichia coli Rho factor
    • Burgess, B.R. & Richardson, J.P. (2001) RNA passes through the hole of the protein hexamer in the complex with the Escherichia coli Rho factor. J. Biol. Chem. 276, 4182-4189.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4182-4189
    • Burgess, B.R.1    Richardson, J.P.2
  • 5
    • 0033593306 scopus 로고    scopus 로고
    • Molecular bases for circadian clocks
    • Dunlap, J.C. (1999) Molecular bases for circadian clocks. Cell 96, 271-290.
    • (1999) Cell , vol.96 , pp. 271-290
    • Dunlap, J.C.1
  • 6
    • 0035252083 scopus 로고    scopus 로고
    • The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase
    • Gomis-Rüth, F.X., Moncalian, G., Perez-Luque, R., et al. (2001) The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase. Nature 409, 637-641.
    • (2001) Nature , vol.409 , pp. 637-641
    • Gomis-Rüth, F.X.1    Moncalian, G.2    Perez-Luque, R.3
  • 7
    • 0033520395 scopus 로고    scopus 로고
    • Role of Walker motif A of RuvB protein in promoting branch migration of Holliday junctions. Walker motif A mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB
    • Hishida, T., Iwasaki, H., Yagi, T. & Shinagawa, H. (1999) Role of Walker motif A of RuvB protein in promoting branch migration of Holliday junctions. Walker motif A mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB. J. Biol. Chem. 274, 25335-25342.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25335-25342
    • Hishida, T.1    Iwasaki, H.2    Yagi, T.3    Shinagawa, H.4
  • 8
    • 0032503002 scopus 로고    scopus 로고
    • Assembly characteristics of flagellar cap protein HAP2 of Salmonella: Decamer and pentamer in the pH-sensitive equilibrium
    • Imada, K., Vonderviszt, F., Furukawa, Y., Oosawa, K. & Namba, K. (1998) Assembly characteristics of flagellar cap protein HAP2 of Salmonella: Decamer and pentamer in the pH-sensitive equilibrium. J. Mol. Biol. 277, 883-891.
    • (1998) J. Mol. Biol. , vol.277 , pp. 883-891
    • Imada, K.1    Vonderviszt, F.2    Furukawa, Y.3    Oosawa, K.4    Namba, K.5
  • 9
    • 0032483510 scopus 로고    scopus 로고
    • Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria
    • Ishiura, M., Kutsuna, S., Aoki, S., et al. (1998) Expression of a gene cluster kaiABC as a circadian feedback process in cyanobacteria. Sience 281, 1519-1523.
    • (1998) Sience , vol.281 , pp. 1519-1523
    • Ishiura, M.1    Kutsuna, S.2    Aoki, S.3
  • 10
    • 0033104504 scopus 로고    scopus 로고
    • Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria
    • Iwasaki, H., Taniguchi, Y., Ishiura, M. & Kondo, T. (1999) Physical interactions among circadian clock proteins KaiA, KaiB and KaiC in cyanobacteria. EMBO J. 18, 1137-1145.
    • (1999) EMBO J. , vol.18 , pp. 1137-1145
    • Iwasaki, H.1    Taniguchi, Y.2    Ishiura, M.3    Kondo, T.4
  • 11
    • 0034646509 scopus 로고    scopus 로고
    • A KaiC-interacting sensory histidine kinase, SasA, necessary to sustain robust circadian oscillation in cyanobacteria
    • Iwasaki, H., Williams, S.B., Kitayama, Y., Ishiura, M., Golden, S.S. & Kondo, T. (2000) A KaiC-interacting sensory histidine kinase, SasA, necessary to sustain robust circadian oscillation in cyanobacteria. Cell 101, 223-233.
    • (2000) Cell , vol.101 , pp. 223-233
    • Iwasaki, H.1    Williams, S.B.2    Kitayama, Y.3    Ishiura, M.4    Golden, S.S.5    Kondo, T.6
  • 12
    • 0034634334 scopus 로고    scopus 로고
    • Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
    • Kim, K.I., Cheong, G.W., Park, S.C., et al. (1998) Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. J. Mol. Biol. 303, 655-666.
    • (1998) J. Mol. Biol. , vol.303 , pp. 655-666
    • Kim, K.I.1    Cheong, G.W.2    Park, S.C.3
  • 13
    • 0033895197 scopus 로고    scopus 로고
    • AAA domains and organization of the dynein motor unit
    • King, S.M. (2000) AAA domains and organization of the dynein motor unit. J. Cell Sci. 113, 2521-2526.
    • (2000) J. Cell Sci. , vol.113 , pp. 2521-2526
    • King, S.M.1
  • 14
    • 0027190489 scopus 로고
    • Circadian rhythms in prokaryotes: Luciferase as a reporter of circadian gene expression in cyanobacteria
    • Kondo, T., Strayer, C.A., Kulkarni, R.D., et al. (1993) Circadian rhythms in prokaryotes: luciferase as a reporter of circadian gene expression in cyanobacteria. Proc. Natl. Acad. Sci. USA 90, 5672-5676.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5672-5676
    • Kondo, T.1    Strayer, C.A.2    Kulkarni, R.D.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, 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
    • Laemmli, U.K.1
  • 16
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen, C.U., Steinmann, D., Whiteheart, S.W. & Weis, W.I. (1998) Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 17
    • 0034602708 scopus 로고    scopus 로고
    • Nucleotide binding and autophosphorylation of the clock protein KaiC as a circadian timing process of cyanobacteria
    • Nishiwaki, T., Iwasaki, H., Ishiura, M. & Kondo, T. (2000) Nucleotide binding and autophosphorylation of the clock protein KaiC as a circadian timing process of cyanobacteria. Proc. Natl. Acad. Sci. USA 96, 495-499.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 495-499
    • Nishiwaki, T.1    Iwasaki, H.2    Ishiura, M.3    Kondo, T.4
  • 18
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega, J., Singh, S.K., Ishikawa, T., Maurizi, M.R. & Steven, A.C. (2000) Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6, 1515-1521.
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 19
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel, S.S. & Picha, K.M. (2000) Structure and function of hexameric helicases. Annu. Rev. Biochem. 69, 651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 20
    • 0031563799 scopus 로고    scopus 로고
    • Photosystem I of Synechococcus elongatus at 4 Å resolution: Comprehensive structure analysis
    • Schubert, W.D., Klukas, O., Krauss, N., Saenger, W., Fromme, P. & Witt, H.T. (1997) Photosystem I of Synechococcus elongatus at 4 Å resolution: comprehensive structure analysis. J. Mol. Biol. 272, 741-769.
    • (1997) J. Mol. Biol. , vol.272 , pp. 741-769
    • Schubert, W.D.1    Klukas, O.2    Krauss, N.3    Saenger, W.4    Fromme, P.5    Witt, H.T.6
  • 21
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Steven, J.L., Philip, R.B. & Wah, C. (1999) EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Steven, J.L.1    Philip, R.B.2    Wah, C.3
  • 22
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I.T. & Steitz, T.A. (1992) The structure of the E. coli recA protein monomer and polymer. Nature 355, 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 23
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. & Gay, N.J. (1982) Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 24
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. & Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 25
    • 0035852703 scopus 로고    scopus 로고
    • Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8
    • Yamada, K., Kunishima, N., Mayanagi, K., et al. (2001) Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8. Proc. Natl. Acad. Sci. USA 98, 1442-1447.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1442-1447
    • Yamada, K.1    Kunishima, N.2    Mayanagi, K.3
  • 26
    • 77957187961 scopus 로고
    • Photosynthetic activities of a thermophilic blue-green alga
    • Yamaoka, T., Satoh, K. & Katoh, S. (1978) photosynthetic activities of a thermophilic blue-green alga. Plant Cell Physiol. 19, 943-954.
    • (1978) Plant Cell Physiol. , vol.19 , pp. 943-954
    • Yamaoka, T.1    Satoh, K.2    Katoh, S.3
  • 27
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • Yu, X. & Egelman, E.H. (1997) The RecA hexamer is a structural homologue of ring helicases. Nature Struct. Biol. 4, 101-104.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 101-104
    • Yu, X.1    Egelman, E.H.2
  • 28
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni, A., Witt, H.T., Kern, J., et al. (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.