메뉴 건너뛰기




Volumn 1591, Issue 1-3, 2002, Pages 119-128

A cyclin-dependent protein kinase homologue associated with the basal body domains in the ciliate Tetrahymena thermophila

Author keywords

Cell cycle; Ciliate; Cyclin dependent kinase; Gene knockout; Membrane skeleton; p13suc1

Indexed keywords

ANTIBODY; CYCLIN DEPENDENT KINASE; HISTONE H1; PHOSPHOTRANSFERASE; POLYPEPTIDE;

EID: 0037135693     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(02)00258-6     Document Type: Article
Times cited : (8)

References (45)
  • 1
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper J.W., Adami G.R., Wei N., Keyomarsi K., Elledge S.J. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 75:1993;805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 2
    • 0029317904 scopus 로고
    • Cyclin-dependent protein kinases: Key regulators of the eukaryotic cell cycle
    • Nigg E.A. Cyclin-dependent protein kinases: key regulators of the eukaryotic cell cycle. BioEssays. 17:1995;471-480.
    • (1995) BioEssays , vol.17 , pp. 471-480
    • Nigg, E.A.1
  • 3
    • 0028363519 scopus 로고
    • P27, a novel inhibitor of G1 cyclin-cdk protein kinase activity, is related to p21
    • Toyoshima H., Hunter T. p27, a novel inhibitor of G1 cyclin-cdk protein kinase activity, is related to p21. Cell. 78:1994;67-74.
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 4
  • 5
    • 0005117783 scopus 로고
    • Synthesis of deoxyribonucleic acid by micro- and macronuclei of Tetrahymena pyriformis
    • McDonald B.B. Synthesis of deoxyribonucleic acid by micro- and macronuclei of Tetrahymena pyriformis. J. Cell Biol. 13:1962;193-203.
    • (1962) J. Cell Biol. , vol.13 , pp. 193-203
    • McDonald, B.B.1
  • 6
    • 0016684618 scopus 로고
    • Amount of DNA produced during extra S-phase in Tetrahymena
    • Cleffmann G. Amount of DNA produced during extra S-phase in Tetrahymena. J. Cell Biol. 66:1975;204-209.
    • (1975) J. Cell Biol. , vol.66 , pp. 204-209
    • Cleffmann, G.1
  • 7
    • 0002655512 scopus 로고
    • Regulation of macronuclear DNA content in Tetrahymena thermophila
    • Doerder F.P. Regulation of macronuclear DNA content in Tetrahymena thermophila. J. Protozool. 26:1979;28-35.
    • (1979) J. Protozool. , vol.26 , pp. 28-35
    • Doerder, F.P.1
  • 8
    • 0026949157 scopus 로고
    • Meiosis-reinitiation-inducing factor of Tetrahymena functions upstream of M-phase-promoting factor
    • Fujishima M., Katsu Y., Ogawa E., Sakimura M., Yamashita M., Nagahama Y. Meiosis-reinitiation-inducing factor of Tetrahymena functions upstream of M-phase-promoting factor. J. Protozool. 39:1992;683-690.
    • (1992) J. Protozool. , vol.39 , pp. 683-690
    • Fujishima, M.1    Katsu, Y.2    Ogawa, E.3    Sakimura, M.4    Yamashita, M.5    Nagahama, Y.6
  • 9
    • 4243932575 scopus 로고
    • Identification of molecular components of the MPF cyclin system in Tetrahymena
    • Nellinger N., Klima M., Cleffmann G. Identification of molecular components of the MPF cyclin system in Tetrahymena. J. Protozool. 39:1992;16A.
    • (1992) J. Protozool. , vol.39
    • Nellinger, N.1    Klima, M.2    Cleffmann, G.3
  • 10
    • 0028913248 scopus 로고
    • Isolation of the cell cycle control gene cdc2 from Paramecium tetraurelia
    • Tang L., Pelech S.L., Berger J.D. Isolation of the cell cycle control gene cdc2 from Paramecium tetraurelia. Biochim. Biophys. Acta. 1265:1995;161-167.
    • (1995) Biochim. Biophys. Acta , vol.1265 , pp. 161-167
    • Tang, L.1    Pelech, S.L.2    Berger, J.D.3
  • 11
    • 0033230876 scopus 로고    scopus 로고
    • Two distinct classes of mitotic cyclins homologues, Cyc1 and Cyc2, are involved in cell cycle regulation in the ciliate Paramecium tetraurelia
    • Zhang H., Adl S.M., Berger J.D. Two distinct classes of mitotic cyclins homologues, Cyc1 and Cyc2, are involved in cell cycle regulation in the ciliate Paramecium tetraurelia. J. Eukaryot. Microbiol. 46:1999;585-596.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 585-596
    • Zhang, H.1    Adl, S.M.2    Berger, J.D.3
  • 12
    • 0033199914 scopus 로고    scopus 로고
    • A novel member of the cyclin-dependent kinase family in Paramecium tetraurelia
    • Zhang H., Berger J.D. A novel member of the cyclin-dependent kinase family in Paramecium tetraurelia. J. Eukaryot. Microbiol. 46:1999;482-491.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 482-491
    • Zhang, H.1    Berger, J.D.2
  • 14
    • 0026767479 scopus 로고
    • Efficient mass transformation of Tetrahymena thermophila by electroporation of conjugants
    • Gaertig J., Gorovsky M.A. Efficient mass transformation of Tetrahymena thermophila by electroporation of conjugants. Proc. Natl. Acad. Sci. U. S. A. 89:1992;9196-9200.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 9196-9200
    • Gaertig, J.1    Gorovsky, M.A.2
  • 15
    • 0022490466 scopus 로고
    • Transformation of Tetrahymena thermophila by microinjection of ribosomal RNA genes
    • Tondravi M., Yao M.-C. Transformation of Tetrahymena thermophila by microinjection of ribosomal RNA genes. Proc. Natl. Acad. Sci. U. S. A. 83:1986;4369-4373.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 4369-4373
    • Tondravi, M.1    Yao, M.-C.2
  • 17
    • 0001939094 scopus 로고
    • RACE: Rapid amplification of cDNA ends
    • J.J. Snincky, & T.J. White. San Diego, CA: Academic Press
    • Frohman M.A. RACE: rapid amplification of cDNA ends. Snincky J.J., White T.J. PCR Protocols. 1990;28-38 Academic Press, San Diego, CA.
    • (1990) PCR Protocols , pp. 28-38
    • Frohman, M.A.1
  • 18
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0030793697 scopus 로고    scopus 로고
    • HSP70 and HSP90 homologs are associated with tubulin in heter-oligomeric complexes, cilia and the cortex of Tetrahymena
    • Williams N.E., Nelsen E.M. HSP70 and HSP90 homologs are associated with tubulin in heter-oligomeric complexes, cilia and the cortex of Tetrahymena. J. Cell Sci. 110:1997;1665-1672.
    • (1997) J. Cell Sci. , vol.110 , pp. 1665-1672
    • Williams, N.E.1    Nelsen, E.M.2
  • 21
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei Y., Yu L., Browen J., Gorovsky M., Allis C.D. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell. 97:1999;99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Browen, J.3    Gorovsky, M.4    Allis, C.D.5
  • 22
    • 0031000539 scopus 로고    scopus 로고
    • A cdc2-related kinase is associated with macronuclear DNA synthesis in Paramecium tetraurelia
    • Tang L., Adl M.S., Berger J.D. A cdc2-related kinase is associated with macronuclear DNA synthesis in Paramecium tetraurelia. J. Eukaryot. Microbiol. 44:1997;269-275.
    • (1997) J. Eukaryot. Microbiol. , vol.44 , pp. 269-275
    • Tang, L.1    Adl, M.S.2    Berger, J.D.3
  • 23
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 241:1988;42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 24
    • 0022573987 scopus 로고
    • The fission yeast cell cycle control gene cdc2; Isolation of a sequence Suc1 that suppresses cdc2 mutant function
    • Hayles J., Beach D.H., Durkacz B., Nurse P.M. The fission yeast cell cycle control gene cdc2; isolation of a sequence Suc1 that suppresses cdc2 mutant function. Mol. Gen. Genet. 202:1986;291-293.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 291-293
    • Hayles, J.1    Beach, D.H.2    Durkacz, B.3    Nurse, P.M.4
  • 25
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen X., Yu L., Weir J.W., Gorovsky M.A. Linker histones are not essential and affect chromatin condensation in vivo. Cell. 82:1995;47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 26
    • 0000768631 scopus 로고
    • Induction of synchronous cell division in mass cultures of Tetrahymena pyriformis
    • Scherbaum O., Zeuthen E. Induction of synchronous cell division in mass cultures of Tetrahymena pyriformis. Exp. Cell Res. 6:1954;221-227.
    • (1954) Exp. Cell Res. , vol.6 , pp. 221-227
    • Scherbaum, O.1    Zeuthen, E.2
  • 27
    • 0001645580 scopus 로고
    • The arrest of mitosis and stomatogenesis during temperature induction of synchronous division in Tetrahymena pyriformis, mating type I, variety I
    • Holz G.G., Scherbaum O.H., Williams N.E. The arrest of mitosis and stomatogenesis during temperature induction of synchronous division in Tetrahymena pyriformis, mating type I, variety I. Exp. Cell Res. 13:1957;618-621.
    • (1957) Exp. Cell Res. , vol.13 , pp. 618-621
    • Holz, G.G.1    Scherbaum, O.H.2    Williams, N.E.3
  • 28
    • 0017141942 scopus 로고
    • Causal relations among cell cycle processes in Tetrahymena pyriformis: An analysis employing temperature-sensitive mutants
    • Frankel J., Jenkins L.M., DeBault L.E. Causal relations among cell cycle processes in Tetrahymena pyriformis: an analysis employing temperature-sensitive mutants. J. Cell Biol. 71:1976;242-260.
    • (1976) J. Cell Biol. , vol.71 , pp. 242-260
    • Frankel, J.1    Jenkins, L.M.2    DeBault, L.E.3
  • 29
    • 0017380826 scopus 로고
    • Mutations affecting cell division in Tetrahymena pyriformis, syngen 1: II. Phenotypes of single and double homozygotes
    • Frankel J., Nelsen E.M., Jenkins L.M. Mutations affecting cell division in Tetrahymena pyriformis, syngen 1: II. Phenotypes of single and double homozygotes. Dev. Biol. 58:1977;255-275.
    • (1977) Dev. Biol. , vol.58 , pp. 255-275
    • Frankel, J.1    Nelsen, E.M.2    Jenkins, L.M.3
  • 30
    • 0025826675 scopus 로고
    • A cdc2-like kinase phosphorylates histone H1 in the amitotic macronucleus of Tetrahymena
    • Roth S.Y., Collini M.P., Draetta G., Beach D., Allis C.D. A cdc2-like kinase phosphorylates histone H1 in the amitotic macronucleus of Tetrahymena. EMBO J. 10:1991;2069-2075.
    • (1991) EMBO J. , vol.10 , pp. 2069-2075
    • Roth, S.Y.1    Collini, M.P.2    Draetta, G.3    Beach, D.4    Allis, C.D.5
  • 31
    • 0026351534 scopus 로고
    • Is cyclin Zeuthen's "division protein"?
    • Williams N.E., Macey M.G. Is cyclin Zeuthen's "division protein"? Exp. Cell Res. 197:1991;137-139.
    • (1991) Exp. Cell Res. , vol.197 , pp. 137-139
    • Williams, N.E.1    Macey, M.G.2
  • 32
    • 0025163611 scopus 로고
    • The formation of basal body domains in the membrane skeleton of Tetrahymena
    • Williams N.E., Honts J.E., Kaczanowska J. The formation of basal body domains in the membrane skeleton of Tetrahymena. Development. 109:1990;935-942.
    • (1990) Development , vol.109 , pp. 935-942
    • Williams, N.E.1    Honts, J.E.2    Kaczanowska, J.3
  • 33
    • 0033989699 scopus 로고    scopus 로고
    • Cell biology of Tetrahymena thermophila
    • D. Asai, & J.D. Forney. San Diego, CA: Academic Press
    • Frankel J. Cell biology of Tetrahymena thermophila. Asai D., Forney J.D. Methods in Cell Biology. vol. 62:1999;28-125 Academic Press, San Diego, CA.
    • (1999) Methods in Cell Biology , vol.62 , pp. 28-125
    • Frankel, J.1
  • 34
    • 0024786266 scopus 로고
    • cdc2 is located in both nucleus and cytoplasm; Part is centrosomally associated at G2/M and enters vesicles at anaphase
    • cdc2 is located in both nucleus and cytoplasm; part is centrosomally associated at G2/M and enters vesicles at anaphase. EMBO J. 8:1989;3985-3995.
    • (1989) EMBO J. , vol.8 , pp. 3985-3995
    • Bailly, E.1    Doree, M.2    Nurse, P.3    Bornens, M.4
  • 35
    • 0026603096 scopus 로고
    • Cytoplasmic accumulation of cyclin B1 in human cells: Association with a detergent-resistant compartment and with the centrosome
    • Bailly E., Pines J., Hunter T., Bornens M. Cytoplasmic accumulation of cyclin B1 in human cells: association with a detergent-resistant compartment and with the centrosome. J. Cell Sci. 101:1992;529-545.
    • (1992) J. Cell Sci. , vol.101 , pp. 529-545
    • Bailly, E.1    Pines, J.2    Hunter, T.3    Bornens, M.4
  • 36
    • 0033525007 scopus 로고    scopus 로고
    • Requirement of Cdk2-Cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts
    • Hinchcliffe E.H., Li C., Thompson E.A., Maller J.L., Sluder G. Requirement of Cdk2-Cyclin E activity for repeated centrosome reproduction in Xenopus egg extracts. Science. 283:1999;851-854.
    • (1999) Science , vol.283 , pp. 851-854
    • Hinchcliffe, E.H.1    Li, C.2    Thompson, E.A.3    Maller, J.L.4    Sluder, G.5
  • 39
    • 0033179053 scopus 로고    scopus 로고
    • Molecular subdivision of the cortex of dividing Tetrahymena is coupled with the formation of the fission zone
    • Kaczanowska J., Joachimiak E., Buzanska L., Krawczynska W., Wheatley D., Kaczanowski A. Molecular subdivision of the cortex of dividing Tetrahymena is coupled with the formation of the fission zone. Dev. Biol. 212:1999;150-164.
    • (1999) Dev. Biol. , vol.212 , pp. 150-164
    • Kaczanowska, J.1    Joachimiak, E.2    Buzanska, L.3    Krawczynska, W.4    Wheatley, D.5    Kaczanowski, A.6
  • 40
    • 0027022457 scopus 로고
    • Protein phosphorylation and the regulation of basal body microtubule organizing centers in Tetrahymena
    • Huelsman D.A., Gitz D.L., Pennock D.G. Protein phosphorylation and the regulation of basal body microtubule organizing centers in Tetrahymena. Cytobios. 71:1992;37-50.
    • (1992) Cytobios , vol.71 , pp. 37-50
    • Huelsman, D.A.1    Gitz, D.L.2    Pennock, D.G.3
  • 41
    • 0023078725 scopus 로고
    • Protein phosphorylation and dynamics of cytoskeletal structures associated with basal bodies in Paramecium
    • Keryer G., Davis F.M., Rao P.N., Beisson J. Protein phosphorylation and dynamics of cytoskeletal structures associated with basal bodies in Paramecium. Cell Motil. Cytoskelet. 8:1987;44-54.
    • (1987) Cell Motil. Cytoskelet. , vol.8 , pp. 44-54
    • Keryer, G.1    Davis, F.M.2    Rao, P.N.3    Beisson, J.4
  • 42
    • 0026043342 scopus 로고
    • Cortical morphogenesis in Paramecium: A transcellular wave of protein phosphorylation involved in ciliary rootlet disassembly
    • Sperling L., Keryer G., Ruiz F., Beisson J. Cortical morphogenesis in Paramecium: a transcellular wave of protein phosphorylation involved in ciliary rootlet disassembly. Dev. Biol. 148:1991;205-218.
    • (1991) Dev. Biol. , vol.148 , pp. 205-218
    • Sperling, L.1    Keryer, G.2    Ruiz, F.3    Beisson, J.4
  • 43
    • 0016337102 scopus 로고
    • Molecular basis of control of mitosis cell division in eukaryotes
    • Bradbury E.M., Inglis R.J., Matthews H.R., Langan T.A. Molecular basis of control of mitosis cell division in eukaryotes. Nature. 249:1974;553-555.
    • (1974) Nature , vol.249 , pp. 553-555
    • Bradbury, E.M.1    Inglis, R.J.2    Matthews, H.R.3    Langan, T.A.4
  • 44
    • 0026545414 scopus 로고
    • Chromatin condensation: Does histone H1 dephosphorylation play a role?
    • Roth S.Y., Allis C.D. Chromatin condensation: does histone H1 dephosphorylation play a role? Trends Biochem. Sci. 17:1992;93-98.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 93-98
    • Roth, S.Y.1    Allis, C.D.2
  • 45
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D., Thompson J., Gibson T. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.