메뉴 건너뛰기




Volumn 254, Issue 1, 2000, Pages 143-152

The polyubiquitin gene is essential for meiosis in fission yeast

Author keywords

Centromere; Fission yeast; Meiosis; Polyubiquitin gene; Spindle pole body; Ubiquitin

Indexed keywords

MESSENGER RNA; POLYUBIQUITIN;

EID: 0034627766     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4728     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0023959560 scopus 로고
    • Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast
    • Tanaka K., Matsumoto K., Toh-e A. Dual regulation of the expression of the polyubiquitin gene by cyclic AMP and heat shock in yeast. EMBO J. 7:1988;495-502.
    • (1988) EMBO J. , vol.7 , pp. 495-502
    • Tanaka, K.1    Matsumoto, K.2    Toh-E, A.3
  • 2
    • 0023971055 scopus 로고
    • Expression of the yeast UBI4 gene increases in response to DNA-damaging agents and in meiosis
    • Treger J. M., Heichman K. A., McEntee K. Expression of the yeast UBI4 gene increases in response to DNA-damaging agents and in meiosis. Mol. Cell. Biol. 8:1988;1132-1136.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1132-1136
    • Treger, J.M.1    Heichman, K.A.2    McEntee, K.3
  • 3
    • 0030614559 scopus 로고    scopus 로고
    • UBI4, the polyubiquitin gene of Saccharomyces cerevisiae, is a heat shock gene that is also subject to catabolite derepression control
    • Watt R., Piper P. W. UBI4, the polyubiquitin gene of Saccharomyces cerevisiae, is a heat shock gene that is also subject to catabolite derepression control. Mol. Gen. Genet. 253:1997;439-447.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 439-447
    • Watt, R.1    Piper, P.W.2
  • 4
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley D., Ozkaynak E., Varshavsky A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell. 48:1987;1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Ozkaynak, E.2    Varshavsky, A.3
  • 5
    • 0023336183 scopus 로고
    • The yeast ubiquitin genes: A family of natural gene fusions
    • Ozkaynak E., Finley D., Solomon M. J., Varshavsky A. The yeast ubiquitin genes: A family of natural gene fusions. EMBO J. 6:1987;1429-1439.
    • (1987) EMBO J. , vol.6 , pp. 1429-1439
    • Ozkaynak, E.1    Finley, D.2    Solomon, M.J.3    Varshavsky, A.4
  • 6
    • 0028848152 scopus 로고
    • The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27a and L40
    • Chan Y. L., Suzuki K., Wool I. G. The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27a and L40. Biochem. Biophys. Res. Commun. 215:1995;682-690.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 682-690
    • Chan, Y.L.1    Suzuki, K.2    Wool, I.G.3
  • 8
    • 0025081530 scopus 로고
    • Activation of polyubiquitin gene expression during developmentally programmed cell death
    • Schwartz L., Myer A., Kosz L., Engelstein M., Maier C. Activation of polyubiquitin gene expression during developmentally programmed cell death. Neuron. 5:1990;411-419.
    • (1990) Neuron , vol.5 , pp. 411-419
    • Schwartz, L.1    Myer, A.2    Kosz, L.3    Engelstein, M.4    Maier, C.5
  • 9
    • 0027377272 scopus 로고
    • Cloning of the polyubiquitin cDNA from the marine sponge Geodia cydonium and its preferential expression during reaggregation of cells
    • Pfeifer K., Frank W., Schroder H. C., Gamulin V., Rinkevich B., Batel R., Muller I. M., Muller W. E. Cloning of the polyubiquitin cDNA from the marine sponge Geodia cydonium and its preferential expression during reaggregation of cells. J. Cell Sci. 106:1993;545-553.
    • (1993) J. Cell Sci. , vol.106 , pp. 545-553
    • Pfeifer, K.1    Frank, W.2    Schroder, H.C.3    Gamulin, V.4    Rinkevich, B.5    Batel, R.6    Muller, I.M.7    Muller, W.E.8
  • 10
    • 0025327472 scopus 로고
    • Methylation of chick UbI and UbII polyubiquitin genes and their different expression during spermatogenesis
    • Rocamora N., Agell N. Methylation of chick UbI and UbII polyubiquitin genes and their different expression during spermatogenesis. Biochem. J. 267:1990;821-829.
    • (1990) Biochem. J. , vol.267 , pp. 821-829
    • Rocamora, N.1    Agell, N.2
  • 11
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser M. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:1996;405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 13
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino J. S., Weissman A. M. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Dev. Biol. 14:1998;19-57.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 14
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: On protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 15
    • 0026025891 scopus 로고
    • Molecular genetic analysis of the fission yeast Schizosaccharomyces pombe
    • Moreno S., Klar A., Nurse P. Molecular genetic analysis of the fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:1991;795-823.
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 16
    • 0030897588 scopus 로고    scopus 로고
    • Sexual co-flocculation by heterothallic cells of the fission yeast Schizosaccharomyces pombe modulated by medium constituents
    • Miyata M., Doi H., Miyata H., Jonson B. F. Sexual co-flocculation by heterothallic cells of the fission yeast Schizosaccharomyces pombe modulated by medium constituents. Antonie Leeuwenhoek. 71:1997;207-215.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 207-215
    • Miyata, M.1    Doi, H.2    Miyata, H.3    Jonson, B.F.4
  • 17
    • 0016297403 scopus 로고
    • Premeiotic DNA synthesis in fission yeast
    • Egel R., Egel-Mitani M. Premeiotic DNA synthesis in fission yeast. Exp. Cell Res. 88:1974;127-134.
    • (1974) Exp. Cell Res. , vol.88 , pp. 127-134
    • Egel, R.1    Egel-Mitani, M.2
  • 18
    • 0025123810 scopus 로고
    • High-frequency transformation method and library transduction vectors for cloning mammalian cDNA by trans-complementation of Schizosaccharomyces pombe
    • Okazaki K., Okazaki N., Kume K., Jinno S., Tanaka K., Okayama H. High-frequency transformation method and library transduction vectors for cloning mammalian cDNA by trans-complementation of Schizosaccharomyces pombe. Nucleic Acids Res. 18:1990;6485-6489.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6485-6489
    • Okazaki, K.1    Okazaki, N.2    Kume, K.3    Jinno, S.4    Tanaka, K.5    Okayama, H.6
  • 19
    • 0029591828 scopus 로고
    • Fission yeast sta mutations that stabilize an unstable minichromosome are novel cdc2-interacting suppressors and are involved in regulation of spindle dynamics
    • Murakami S., Niwa O. Fission yeast sta mutations that stabilize an unstable minichromosome are novel cdc2-interacting suppressors and are involved in regulation of spindle dynamics. Mol. Gen. Genet. 249:1995;391-399.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 391-399
    • Murakami, S.1    Niwa, O.2
  • 21
    • 0032053785 scopus 로고    scopus 로고
    • The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control
    • Bridge A. J., Morphew M., Bartlett R., Hagan I. M. The fission yeast SPB component Cut12 links bipolar spindle formation to mitotic control. Genes Dev. 12:1998;927-942.
    • (1998) Genes Dev. , vol.12 , pp. 927-942
    • Bridge, A.J.1    Morphew, M.2    Bartlett, R.3    Hagan, I.M.4
  • 22
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods A., Sherwin T., Sasse R., MacRae T. H., Baines A. J., Gull K. Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J. Cell Sci. 93:1989;491-500.
    • (1989) J. Cell Sci. , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 23
    • 0029029742 scopus 로고
    • + associates with the fission yeast spindle pole body and is essential for viability
    • + associates with the fission yeast spindle pole body and is essential for viability. J. Cell Biol. 129:1995;1033-1047.
    • (1995) J. Cell Biol. , vol.129 , pp. 1033-1047
    • Hagan, I.1    Yanagida, M.2
  • 24
    • 0031025531 scopus 로고    scopus 로고
    • Meiotic nuclear reorganization: Switching the position of centromeres and telomeres in the fission yeast Schizosaccharomyces pombe
    • Chikashige Y., Ding D.-Q., Imai Y., Yamamoto M., Haraguchi T., Hiraoka Y. Meiotic nuclear reorganization: switching the position of centromeres and telomeres in the fission yeast Schizosaccharomyces pombe. EMBO J. 16:1997;193-202.
    • (1997) EMBO J. , vol.16 , pp. 193-202
    • Chikashige, Y.1    Ding, D.-Q.2    Imai, Y.3    Yamamoto, M.4    Haraguchi, T.5    Hiraoka, Y.6
  • 25
    • 0031972489 scopus 로고    scopus 로고
    • Mapping three-dimensional chromosome architecture in situ
    • Dernburg A. F., Sedat J. W. Mapping three-dimensional chromosome architecture in situ. Methods Cell Biol. 53:1998;187-233.
    • (1998) Methods Cell Biol. , vol.53 , pp. 187-233
    • Dernburg, A.F.1    Sedat, J.W.2
  • 26
    • 0024360820 scopus 로고
    • Composite motifs and repeat symmetry in S. pombe centromeres: Direct analysis by integration of NotI restriction site
    • Chikashige Y., Kinoshita N., Nakaseko Y., Matsumoto T., Murakami S., Niwa O., Yanagida M. Composite motifs and repeat symmetry in S. pombe centromeres: direct analysis by integration of NotI restriction site. Cell. 57:1989;739-751.
    • (1989) Cell , vol.57 , pp. 739-751
    • Chikashige, Y.1    Kinoshita, N.2    Nakaseko, Y.3    Matsumoto, T.4    Murakami, S.5    Niwa, O.6    Yanagida, M.7
  • 28
    • 0027170369 scopus 로고
    • Nonurea sodium dodecyl sulfate-polyacrylamide gel electrophoresis with high-molarity buffers for the separation of proteins and peptides
    • Okajima T., Tanabe T., Yasuda T. Nonurea sodium dodecyl sulfate-polyacrylamide gel electrophoresis with high-molarity buffers for the separation of proteins and peptides. Anal. Biochem. 211:1993;293-300.
    • (1993) Anal. Biochem. , vol.211 , pp. 293-300
    • Okajima, T.1    Tanabe, T.2    Yasuda, T.3
  • 29
    • 0021929124 scopus 로고
    • Mutants of Schizosaccharomyces pombe which sporulate in the haploid state
    • Iino Y., Yamamoto M. Mutants of Schizosaccharomyces pombe which sporulate in the haploid state. Mol. Gen. Genet. 198:1985;416-421.
    • (1985) Mol. Gen. Genet. , vol.198 , pp. 416-421
    • Iino, Y.1    Yamamoto, M.2
  • 30
    • 0021818797 scopus 로고
    • Characterization of meiosis-deficient mutants by electron microscopy and mapping of four essential genes in the fission yeast Schizosaccharomyces pombe
    • Shimoda C., Hirata A., Kishida M., Hashida T., Tanaka K. Characterization of meiosis-deficient mutants by electron microscopy and mapping of four essential genes in the fission yeast Schizosaccharomyces pombe. Mol. Gen. Genet. 200:1985;252-257.
    • (1985) Mol. Gen. Genet. , vol.200 , pp. 252-257
    • Shimoda, C.1    Hirata, A.2    Kishida, M.3    Hashida, T.4    Tanaka, K.5
  • 31
    • 0029973094 scopus 로고    scopus 로고
    • Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells
    • Jacobson A., Peltz S. W. Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells. Annu. Rev. Biochem. 65:1996;693-739.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 693-739
    • Jacobson, A.1    Peltz, S.W.2
  • 32
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transportors and channels
    • Hicke L. Gettin' down with ubiquitin: Turning off cell-surface receptors, transportors and channels. Trends Cell Biol. 9:1999;107-112.
    • (1999) Trends Cell Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 33
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan J., Haguenauer-Tsapis R. Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16:1997;5847-5854.
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.1    Haguenauer-Tsapis, R.2
  • 34
    • 0033048856 scopus 로고    scopus 로고
    • 4-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains
    • 4-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. J. Cell Sci. 112:1999;1375-1383.
    • (1999) J. Cell Sci. , vol.112 , pp. 1375-1383
    • Springael, J.-Y.1    Galan, J.-M.2    Haguenauer-Tsapis, R.3    Andre, B.4
  • 35
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason T., Ellison M. J. Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol. 14:1994;7876-7883.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 36
    • 0030013594 scopus 로고    scopus 로고
    • Cut2 proteolysis required for sister-chromatid separation in fission yeast
    • Funabiki H., Yamano H., Kumada K., Nagao K., Hunt T., Yanagida M. Cut2 proteolysis required for sister-chromatid separation in fission yeast. Nature. 381:1996;438-441.
    • (1996) Nature , vol.381 , pp. 438-441
    • Funabiki, H.1    Yamano, H.2    Kumada, K.3    Nagao, K.4    Hunt, T.5    Yanagida, M.6
  • 37
    • 0029790893 scopus 로고    scopus 로고
    • The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe
    • Yamano H., Gannon J., Hunt T. The role of proteolysis in cell cycle progression in Schizosaccharomyces pombe. EMBO J. 15:1996;5268-5279.
    • (1996) EMBO J. , vol.15 , pp. 5268-5279
    • Yamano, H.1    Gannon, J.2    Hunt, T.3
  • 38
    • 0030883687 scopus 로고    scopus 로고
    • The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds
    • Ding R., West R. R., Morphew M., Oakley B. R., McIntosh J. R. The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds. Mol. Biol. Cell. 8:1997;1461-1479.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1461-1479
    • Ding, R.1    West, R.R.2    Morphew, M.3    Oakley, B.R.4    McIntosh, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.