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1996 Fiscal Year Final Research Report Summary

Mechanisms of cell division with protein phosphorylation.

Research Project

Project/Area Number 06454138
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Applied molecular and cellular biology
Research InstitutionHIROSHIMA UNIVERSITY

Principal Investigator

IKEGAMI Susumu  Hiroshima University, Dept.Applied Biochemistry, Professor, 生物生産学部, 教授 (80011980)

Co-Investigator(Kenkyū-buntansha) SHIODA Masaki  Kumamoto University, Dept Biological Sciences, Professor, 理学部, 教授 (80134526)
HOSOYA Hiroshi  Hiroshima University, Dept.Biological Sciences, Professor, 理学部, 教授 (90183102)
Project Period (FY) 1994 – 1996
KeywordsMyosin / Phosphorylation / P1 / NAAP / cdc2 kinase / Cyclin B
Research Abstract

Hosoya and his colleagues discovered that phosphorylated myosin is present in the contractile ring. This is a very importand discovery for the understanding of the mechanism of cell division. They also discovered the enzyme that selectively phosphorylates the light chain of myosin.
Shioda and his colleagues discovered a novel protein, P1, which regulates the initiation of DNA replication. P1, which is inactive in its unphosphorylated form, becomes active by phosphorylation. The enzyme responsible for the phosphorylation is found to be a DNA-dependent kinase.
Ikegami and his colleagues discovered a novel nucleic-acid associated protein designated as NAAP which was isolated from starfish oocytes. Oligonucleotides derived from the partial amino acid sequences of NAAP were used to clone NAAPcDNA and the entire cDNA sequence was determined. The transcript encoding NAAP was present only in growing oocytes but not in full-grown oocytes, embryos and adult tissues. The NAAP protein localized in the germinal vesicle of the full-grown oocyte and dispersed diffusely after germinal vesicle breakdown at the onset of meiosis. During oocyte maturation, NAAP changed the moleclar form in a cell-cycle dependent manner. It was found that Ser 145 of NAAP,which was unphosphorylated at the germinal vesicle stage, was phosphorylated during the M phase of meiosis.

  • Research Products

    (8 results)

All Other

All Publications (8 results)

  • [Publications] Shimizu,T: "A covalently on osslinked histone." Nature. 380. 32 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Uno,M: "Callyspongins A and B : Novel polyacelylene sulfates from the manine sponge." J.Natl.Prod.(Lloglia). 59. 1146-1148 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Ohta,S.: "Hipposrngic acid A : an unusuel triterpencic acid from a sponge." Tetrahedron letters. 37. 7765-7766 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Ohta,S.: "Rhonaloic acid A : A novel ncrseterteryene from a marine sponge" Tetrahedron Letters. 37. 2265-2266 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Ohta, S., Uno, M., Yoshimura, M., Hiraga, Y., and Ikegami, S.: "Rhopaloic acid A : A novel norsesterterpene from a marine sponge, Rhopaloeides sp., which inhibits gastrulation of starfish embryos." Tetrahedron Lett.37. 2265-2266 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Ohta, S., M.Uno, Tokumasu, M., Hiraga, Y.and Ikegami, S.: "Hippospongic acid A : an unusual triterpenoic acid from a marine sponge, Hippospongia sp., which inhibits gastrulation of starfish embryos." Tetrahedron Lett.37. 7765-7766 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Shimizu, T., Hozumi, K., Horiike, S., Nunomura, K., Ikegami, S,.Takao, T., and Shimonishi, Y.: "A covalently crosslinked histone." Nature. 380. 32 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Uno, M., Ohta, S., Ohta, E., and Ikegami, S.: "Callyspongins A and B : Novel polyacetylene sulfates from the marine sponge, Callyspongia truncata, that inhibit fertilization of starfish gametes." J.Natl.Prod.(Lloydia). 59. 1146-1148 (1996)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1999-03-09  

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