ISSN:
1432-2048
Keywords:
Blue light
;
Coleoptile tip
;
Light receptor (redox dependence)
;
Phosphorylation of proteins
;
Phototropism
;
Zea
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract A blue-light-induced rapid phosphorylation of a 100-kDa protein localized in plasma membranes of phototropically sensitive tips of maize (Zea mays L.) coleoptiles was studied. Since, under in-vivo conditions or in a crude homogenate of tips, cytosolic ATP is the phosphate donor for the light-induced phosphorylation of this protein, a subsequent in-vitro phosphorylation by [32P]ATP is prevented. However, in-vitro irradiation of microsomal membranes isolated from non-irradiated tips followed by a 1-min incubation with [32P]ATP resulted in a strong phosphorylation (labelling) of the 100-kDa plasma-membrane protein. This process was saturated by a 7-s light pulse (200 μmol photons·m−2·s−1). In the absence of [32P]ATP the capacity for in-vitro phosphorylation of the 100-kDa protein after a 30-s light pulse declined slowly within 60 min but could be reconstituted by a new light pulse in the presence of reducing compounds. Moreover, when plasma membranes which had been stored frozen were used, reducing compounds such as NADH, NADPH, ascorbate, glutathione or dithiotreithol enhanced the light-triggered in-vitro phosphorylation. These compounds were unable to elicit or enhance the phosphorylation in the dark. It is suggested that the transfer of (blue-light) excited electrons from the chromophore moiety of the receptor to the target (either the 100-kDa protein or the protein kinase itself) is facilitated when reducing compounds instantly eliminate the positive charge generated at the chromophore. The transferred electrons could finally alter the redox state and-or the conformation of either the 100-kDa protein, rendering it susceptible to the action of a protein kinase, or the protein kinase which would then be capable of phospho-rylating the 100-kDa protein.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00195683
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