Phosphorylation of a protein (pp56) is related to the regeneration of rice cultured suspension cells.
Short-term cultured suspension cells of rice (Oryza sativa L.) are capable of regeneration, but not in long-term culture. For clarification of the mechanism of regeneration, protein phosphorylation in short-term and long-term cultured suspension cells was compared by two dimensional-polyacrylamide gel electrophoresis. A 56 kDa protein having an isoelectric point of 4.5 was phosphorylated in vitro in short-term cultured suspension cells, but was not phosphorylated after regeneration. This protein in long-term cultured suspension cells remained phosphorylated after transfer to the regeneration medium. However, using an antibody raised against this protein from short-term cultured suspension cells, it was always detected in long-term and short-term cultured suspension cells after transfer to the regeneration medium. The partial amino acid sequence of the HPLC-purified protein showed homology to a calcium-binding protein from maize. The phosphorylation of the 56 kDa protein (pp56) appears to be associated with the regeneration of cultured rice cells.
Department of Molecular Biology, National Institute of Agrobiological Resources, Ibaraki, Japan.
S
S
Komatsu
T
T
Masuda
K
K
Abe
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D015180:Electrophoresis, Gel, Two-Dimensional; D008969:Molecular Sequence Data; D012275:Oryza / Q000166:cytology / Q000378:metabolism*; D010766:Phosphorylation; D010940:Plant Proteins / Q000032:analysis*; D011817:Rabbits; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins