CELL CYCLE-DEPENDENT CHANGE OF PROTEASOME DISTRIBUTION DURING EMBRYONIC-DEVELOPMENT OF THE ASCIDIAN HALOCYNTHIA-RORETZI

被引:63
作者
KAWAHARA, H [1 ]
YOKOSAWA, H [1 ]
机构
[1] HOKKAIDO UNIV,FAC PHARMACEUT SCI,DEPT BIOCHEM,SAPPORO,HOKKAIDO 060,JAPAN
关键词
D O I
10.1016/0012-1606(92)90210-8
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
The proteasome is a multicatalytic proteinase complex composed of nonidentical subunits. By immunocytochemical analysis using monoclonal antibody raised against the egg proteasome, we demonstrate that the proteasome undergoes changes in its subcellular distribution, depending on the cell division cycle during embryonic development of the ascidian Halocynthia roretzi. During interphase, the proteasome is localized in the nucleus, i.e., in the nucleoplasm and along the nuclear membrane. The proteasome disappears from the nucleoplasm in prophase and from the nuclear envelope in prometaphase. During early metaphase, the proteasome is detectable in the chromosomes and, at late stages of metaphase, the immunoreactivity also occurs in the peripheral region of each spindle pole and at the mitotic spindle. In anaphase, however, the staining disappears in the mitotic apparatus. In telophase, the proteasome is again localized in the newly formed nucleus. In addition to the localization in the nucleus and around the mitotic apparatus, the proteasome shows cytoplasmic localization throughout the cell division cycle. Such a change of subcellular distribution of the proteasome is clearly demonstrated in the synchronously dividing blastomeres and also is believed to occur in the postcleavage embryos. These observations suggest that the proteasome may play a key role in the progression of cell division cycle. © 1992.
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页码:27 / 33
页数:7
相关论文
共 25 条
  • [1] IDENTITY OF THE 19S PROSOME PARTICLE WITH THE LARGE MULTIFUNCTIONAL PROTEASE COMPLEX OF MAMMALIAN-CELLS (THE PROTEASOME)
    ARRIGO, AP
    TANAKA, K
    GOLDBERG, AL
    WELCH, WJ
    [J]. NATURE, 1988, 331 (6152) : 192 - 194
  • [2] DESA MFG, 1988, J CELL SCI, V89, P151
  • [3] DRISCOLL J, 1990, J BIOL CHEM, V265, P4789
  • [4] ATP-DEPENDENT INCORPORATION OF 20S PROTEASE INTO THE 26S COMPLEX THAT DEGRADES PROTEINS CONJUGATED TO UBIQUITIN - (PROTEIN BREAKDOWN MULTICATALYTIC PROTEINASE COMPLEX)
    EYTAN, E
    GANOTH, D
    ARMON, T
    HERSHKO, A
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (20) : 7751 - 7755
  • [5] DROSOPHILA SMALL CYTOPLASMIC 19S RIBONUCLEOPROTEIN IS HOMOLOGOUS TO THE RAT MULTICATALYTIC PROTEINASE
    FALKENBURG, PE
    HAASS, C
    KLOETZEL, PM
    NIEDEL, B
    KOPP, F
    KUEHN, L
    DAHLMANN, B
    [J]. NATURE, 1988, 331 (6152) : 190 - 192
  • [6] FUJIWARA T, 1990, J BIOL CHEM, V265, P16604
  • [7] GAUTIER J, 1988, J CELL SCI, V90, P543
  • [8] GLOTZER M, 1991, NATURE, V349, P132, DOI 10.1038/349132a0
  • [9] THE PROS-35 GENE ENCODES THE 35KD PROTEIN SUBUNIT OF DROSOPHILA-MELANOGASTER PROTEASOME
    HAASS, C
    PESOLDHURT, B
    MULTHAUP, G
    BEYREUTHER, K
    KLOETZEL, PM
    [J]. EMBO JOURNAL, 1989, 8 (08) : 2373 - 2379
  • [10] EVIDENCE FOR PARTICIPATION OF SPERM PROTEINASES IN FERTILIZATION OF THE SOLITARY ASCIDIAN, HALOCYNTHIA-RORETZI - EFFECTS OF PROTEASE INHIBITORS
    HOSHI, M
    NUMAKUNAI, T
    SAWADA, H
    [J]. DEVELOPMENTAL BIOLOGY, 1981, 86 (01) : 117 - 121