메뉴 건너뛰기




Volumn 402, Issue 2, 2007, Pages 397-403

Mechanism for the degradation of origin recognition complex containing Orc5p with a defective Walker A motif and its suppression by over-production of Orc4p in yeast cells

Author keywords

DNA replication; Orc4p; Orc5 ap; Origin recognition complex (ORC); Walker A motif; Yeast

Indexed keywords

DNA REPLICATION; ORC4P; ORC5-AP; ORIGIN RECOGNITION COMPLEX (ORC); WALKER A MOTIF;

EID: 33847734266     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060841     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0023658349 scopus 로고
    • ATP activates DnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu, K., Bramhill, D. and Kornberg, A. (1987) ATP activates DnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell 50, 259-265
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 2
    • 0029817925 scopus 로고    scopus 로고
    • Molecular design of inhibitors of in vitro oriC DNA replication based on the potential to block the ATP binding of DnaA protein
    • Mizushima, T., Sasaki, S., Ohishi, H., Kobayashi, M., Katayama, T., Miki, T., Maeda, M. and Sekimizu, K. (1996) Molecular design of inhibitors of in vitro oriC DNA replication based on the potential to block the ATP binding of DnaA protein. J. Biol. Chem. 271, 25178-25183
    • (1996) J. Biol. Chem , vol.271 , pp. 25178-25183
    • Mizushima, T.1    Sasaki, S.2    Ohishi, H.3    Kobayashi, M.4    Katayama, T.5    Miki, T.6    Maeda, M.7    Sekimizu, K.8
  • 3
    • 0032516840 scopus 로고    scopus 로고
    • Site-directed mutational analysis for the ATP binding of DnaA protein. Functions of two conserved amino acids (Lys-178 and Asp-235) located in the ATP-binding domain of DnaA protein in vitro and in vivo
    • Mizushima, T., Takaki, T., Kubota, T., Tsuchiya, T., Miki, T., Katayama, T. and Sekimizu, K. (1998) Site-directed mutational analysis for the ATP binding of DnaA protein. Functions of two conserved amino acids (Lys-178 and Asp-235) located in the ATP-binding domain of DnaA protein in vitro and in vivo. J. Biol. Chem. 273, 20847-20851
    • (1998) J. Biol. Chem , vol.273 , pp. 20847-20851
    • Mizushima, T.1    Takaki, T.2    Kubota, T.3    Tsuchiya, T.4    Miki, T.5    Katayama, T.6    Sekimizu, K.7
  • 4
    • 0032504050 scopus 로고    scopus 로고
    • The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase
    • Katayama, T., Kubota, T., Kurokawa, K., Crooke, E. and Sekimizu, K. (1998) The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase. Cell 94, 61-71
    • (1998) Cell , vol.94 , pp. 61-71
    • Katayama, T.1    Kubota, T.2    Kurokawa, K.3    Crooke, E.4    Sekimizu, K.5
  • 5
    • 0030983404 scopus 로고    scopus 로고
    • Negative control of DNA replication by hydrolysis of ATP bound to DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli
    • Mizushima, T., Nishida, S., Kurokawa, K., Katayama, T., Miki, T. and Sekimizu, K. (1997) Negative control of DNA replication by hydrolysis of ATP bound to DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli. EMBO J. 16, 3724-3730
    • (1997) EMBO J , vol.16 , pp. 3724-3730
    • Mizushima, T.1    Nishida, S.2    Kurokawa, K.3    Katayama, T.4    Miki, T.5    Sekimizu, K.6
  • 6
    • 0035831539 scopus 로고    scopus 로고
    • Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: Identification of important amino acids
    • Makise, M., Mima, S., Tsuchiya, T. and Mizushima, T. (2001) Molecular mechanism for functional interaction between DnaA protein and acidic phospholipids: identification of important amino acids. J. Biol. Chem. 276, 7450-7456
    • (2001) J. Biol. Chem , vol.276 , pp. 7450-7456
    • Makise, M.1    Mima, S.2    Tsuchiya, T.3    Mizushima, T.4
  • 7
    • 0034635464 scopus 로고    scopus 로고
    • Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids
    • Makise, M., Mima, S., Tsuchiya, T. and Mizushima, T. (2000) Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids. J. Biol. Chem. 275, 4513-4518
    • (2000) J. Biol. Chem , vol.275 , pp. 4513-4518
    • Makise, M.1    Mima, S.2    Tsuchiya, T.3    Mizushima, T.4
  • 8
    • 0036035220 scopus 로고    scopus 로고
    • Acidic phospholipids inhibit the DNA-binding activity of DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli
    • Makise, M., Mima, S., Katsu, T., Tsuchiya, T. and Mizushima, T. (2002) Acidic phospholipids inhibit the DNA-binding activity of DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli. Mol. Microbiol. 46, 245-256
    • (2002) Mol. Microbiol , vol.46 , pp. 245-256
    • Makise, M.1    Mima, S.2    Katsu, T.3    Tsuchiya, T.4    Mizushima, T.5
  • 9
    • 0023904203 scopus 로고
    • Cardiolipin activation of DnaA protein, the initiation protein of replication in Escherichia coli
    • Sekimizu, K. and Kornberg, A. (1988) Cardiolipin activation of DnaA protein, the initiation protein of replication in Escherichia coli. J. Biol. Chem. 263, 7131-7135
    • (1988) J. Biol. Chem , vol.263 , pp. 7131-7135
    • Sekimizu, K.1    Kornberg, A.2
  • 10
    • 0028837935 scopus 로고
    • In vivo evidence for the involvement of anionic phospholipids in initiation of DNA replication in Escherichia coli
    • Xia, W. and Dowhan, W. (1995) In vivo evidence for the involvement of anionic phospholipids in initiation of DNA replication in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 92, 783-787
    • (1995) Proc. Natl. Acad. Sci. U.S.A , vol.92 , pp. 783-787
    • Xia, W.1    Dowhan, W.2
  • 11
    • 0026607331 scopus 로고
    • ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex
    • Bell, S. P. and Stillman, B. (1992) ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex. Nature 357, 128-134
    • (1992) Nature , vol.357 , pp. 128-134
    • Bell, S.P.1    Stillman, B.2
  • 12
    • 0031002795 scopus 로고    scopus 로고
    • Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex
    • Klemm, R. D., Austin, R. J. and Bell, S. P. (1997) Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex. Cell 88, 493-502
    • (1997) Cell , vol.88 , pp. 493-502
    • Klemm, R.D.1    Austin, R.J.2    Bell, S.P.3
  • 14
    • 0344012565 scopus 로고    scopus 로고
    • Kinetics of ATP-binding to origin recognition complex of Saccharomyces cerevisiae
    • Makise, M., Takenaka, H., Kuwae, W., Takahashi, N., Tsuchiya, T. and Mizushima, T. (2003) Kinetics of ATP-binding to origin recognition complex of Saccharomyces cerevisiae. J. Biol. Chem. 278, 46440-46445
    • (2003) J. Biol. Chem , vol.278 , pp. 46440-46445
    • Makise, M.1    Takenaka, H.2    Kuwae, W.3    Takahashi, N.4    Tsuchiya, T.5    Mizushima, T.6
  • 15
    • 0031467141 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic cells
    • Dutta, A. and Bell, S. P. (1997) Initiation of DNA replication in eukaryotic cells. Annu. Rev. Cell Dev. Biol. 13, 293-332
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 293-332
    • Dutta, A.1    Bell, S.P.2
  • 17
    • 0034616108 scopus 로고    scopus 로고
    • Impaired proteasome function rescues thermosensitivity of yeast cells lacking the coatomer subunit epsilon-COP
    • Kimata, Y., Higashio, H. and Kohno, K. (2000) Impaired proteasome function rescues thermosensitivity of yeast cells lacking the coatomer subunit epsilon-COP. J. Biol. Chem. 275, 10655-10660
    • (2000) J. Biol. Chem , vol.275 , pp. 10655-10660
    • Kimata, Y.1    Higashio, H.2    Kohno, K.3
  • 18
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with in vitro measurements
    • Estojak, J., Brent, R. and Golemis, E. A. (1995) Correlation of two-hybrid affinity data with in vitro measurements. Mol. Cell. Biol. 15, 5820-5829
    • (1995) Mol. Cell. Biol , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 19
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B. J. and Rothstein, R. (1989) Elevated recombination rates in transcriptionally active DNA. Cell 56, 619-630
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 20
    • 0037115555 scopus 로고    scopus 로고
    • Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae
    • Tone, Y. and Toh-E, A. (2002) Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae. Genes Dev. 16, 3142-3157
    • (2002) Genes Dev , vol.16 , pp. 3142-3157
    • Tone, Y.1    Toh-E, A.2
  • 21
    • 0009453976 scopus 로고
    • Replacement of chromosome segments with altered DNA sequences constructed in vitro
    • Scherer, S. and Davis, R. W. (1979) Replacement of chromosome segments with altered DNA sequences constructed in vitro. Proc. Natl. Acad. Sci. U.S.A. 76, 4951-4955
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 4951-4955
    • Scherer, S.1    Davis, R.W.2
  • 22
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, III, A., Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P. and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14, 953-961
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 23
    • 0037013301 scopus 로고    scopus 로고
    • Functions of sensor 1 and sensor 2 regions of Saccharomyces cerevisiae Cdc6p in vivo and in vitro
    • Takahashi, N., Tsutsumi, S., Tsuchiya, T., Stillman, B. and Mizushima, T. (2002) Functions of sensor 1 and sensor 2 regions of Saccharomyces cerevisiae Cdc6p in vivo and in vitro. J. Biol. Chem. 277, 16033-16040
    • (2002) J. Biol. Chem , vol.277 , pp. 16033-16040
    • Takahashi, N.1    Tsutsumi, S.2    Tsuchiya, T.3    Stillman, B.4    Mizushima, T.5
  • 24
    • 0031455421 scopus 로고    scopus 로고
    • Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants
    • Liang, C. and Stillman, B. (1997) Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants. Genes Dev. 11, 3375-3386
    • (1997) Genes Dev , vol.11 , pp. 3375-3386
    • Liang, C.1    Stillman, B.2
  • 25
    • 0034234223 scopus 로고    scopus 로고
    • Cdc6p modulates the structure and DNA binding activity of the origin recognition complex in vitro
    • Mizushima, T., Takahashi, N. and Stillman, B. (2000) Cdc6p modulates the structure and DNA binding activity of the origin recognition complex in vitro. Genes Dev. 14, 1631-1641
    • (2000) Genes Dev , vol.14 , pp. 1631-1641
    • Mizushima, T.1    Takahashi, N.2    Stillman, B.3
  • 26
    • 0034791090 scopus 로고    scopus 로고
    • Ubiquitin enters the new millennium
    • Pickart, C. M. (2001) Ubiquitin enters the new millennium. Mol. Cell 8, 499-504
    • (2001) Mol. Cell , vol.8 , pp. 499-504
    • Pickart, C.M.1
  • 27
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. and Goldberg, A. L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biocnem. 65, 801-847
    • (1996) Annu. Rev. Biocnem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 29
    • 0029095673 scopus 로고
    • Roles of ubiquitinylation in proteolysis and cellular regulation
    • Wilkinson, K. D. (1995) Roles of ubiquitinylation in proteolysis and cellular regulation. Annu. Rev. Nutr. 15, 161-189
    • (1995) Annu. Rev. Nutr , vol.15 , pp. 161-189
    • Wilkinson, K.D.1
  • 30
    • 0025647715 scopus 로고
    • The structure-function relationship between peptide aldehyde derivatives on initiation of neurite outgrowth in PC12h cells
    • Saito, Y., Tsubuki, S., Ito, H. and Kawashima, S. (1990) The structure-function relationship between peptide aldehyde derivatives on initiation of neurite outgrowth in PC12h cells. Neurosci. Lett. 120, 1-4
    • (1990) Neurosci. Lett , vol.120 , pp. 1-4
    • Saito, Y.1    Tsubuki, S.2    Ito, H.3    Kawashima, S.4
  • 31
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T. J., Loo, M. A., Pind, S., Williams, D. B., Goldberg, A. L. and Riordan, J. R. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 32
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S. and Song, O. (1989) A novel genetic system to detect protein-protein interactions. Nature 340, 245-246
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 33
    • 0037047637 scopus 로고    scopus 로고
    • Orc6 involved in DNA replication, chromosome segregation, and cytokinesis
    • Prasanth, S. G., Prasanth, K. V. and Stillman, B. (2002) Orc6 involved in DNA replication, chromosome segregation, and cytokinesis. Science 297, 1026-1031
    • (2002) Science , vol.297 , pp. 1026-1031
    • Prasanth, S.G.1    Prasanth, K.V.2    Stillman, B.3
  • 34
    • 0030712877 scopus 로고    scopus 로고
    • Architecture of the yeast origin recognition complex bound to origins of DNA replication
    • Lee, D. G. and Bell, S. P. (1997) Architecture of the yeast origin recognition complex bound to origins of DNA replication. Mol. Cell. Biol. 17, 7159-7168
    • (1997) Mol. Cell. Biol , vol.17 , pp. 7159-7168
    • Lee, D.G.1    Bell, S.P.2
  • 35
    • 0037436391 scopus 로고    scopus 로고
    • Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells
    • Kneissl, M., Putter, V., Szalay, A. A. and Grummt, F. (2003) Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells. J. Mol. Biol. 327, 111-128
    • (2003) J. Mol. Biol , vol.327 , pp. 111-128
    • Kneissl, M.1    Putter, V.2    Szalay, A.A.3    Grummt, F.4
  • 36
    • 0344012565 scopus 로고    scopus 로고
    • Kinetics of ATP binding to the origin recognition complex of Saccharomyces cerevisiae
    • Makise, M., Takenaka, H., Kuwae, W., Takahashi, N., Tsuchiya, T. and Mizushima, T. (2003) Kinetics of ATP binding to the origin recognition complex of Saccharomyces cerevisiae. J. Biol. Chem. 278, 46440-46445
    • (2003) J. Biol. Chem , vol.278 , pp. 46440-46445
    • Makise, M.1    Takenaka, H.2    Kuwae, W.3    Takahashi, N.4    Tsuchiya, T.5    Mizushima, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.