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  • 1
    ISSN: 1432-2048
    Keywords: Avena (phytochrome) ; Monoclonal antibodies (phytochrome) ; Phytochrome (sequestering)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The kinetics of the intracellular redistribution of phytochrome (sequestering) in Avena sativa L. coleoptiles following a brief, saturating actinic pulse of red (R) light have been determined. Immunocytochemical labelling of phytochrome with monoclonal antibodies showed that at 22°C sequestering can occur within 1–2 s from the onset of R irradiation and is dependent upon the continued presence of the far-red-absorbing form of phytochrome (Pfr). The initial rate, but not the final extent, of sequestering is reduced by lowering the temperature of the tissue to 1°C. Sequestering at 22°C appears to involve two distinct stages: (1) a rapid association of Pfr with putative binding sites initiates the sequestered condition, following which (2) these sites of sequestered phytochrome appear to aggregate. Neither of these two processes was affected by the cytoskeletal inhibitors colchicine or cytochalasin B. Phytochrome sequestering therefore resembles R-light-induced phytochrome pelletability with respect to kinetics, temperature sensitivity, and dependence upon the continued presence of Pfr in the cell.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Protoplasma 171 (1992), S. 85-88 
    ISSN: 1615-6102
    Keywords: Ca2+-dependent protein kinase ; Chara ; Cytoplasmic streaming ; Myosin light chain ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ca2+-dependent protein kinase (CDPK) has been proposed to mediate inhibition by Ca2+ of cytoplasmic streaming in the green algaChara. We have identified the in vivo substrate(s) of CDPK inChara by using vacuolar perfusion of individual internodal cells with [γ-32P]ATP. Phosphorylation of several polypeptides is enhanced when perfusions are performed at 10−4M free Ca2+ compared to 〈10−9M free Ca2+. The Ca2+-stimulated phosphorylation of these proteins is inhibited by the presence of a monoclonal antibody to soybean CDPK. One of these proteins is 16 to 18kDa and is recognized by an antibody against gizzard myosin light chains. These results demonstrate that inChara, several polypeptides are phophorylated by CDPK and one of these proteins has been tentatively identified as a myosin light chain. These observations support the hypothesis that Ca2+-regulated phosphorylation of myosin is involved in the regulation of cytoplasmic streaming.
    Type of Medium: Electronic Resource
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