The so far unexplored H. Orientalis cv. Olympicus exhibits a unique pattern of flower senescence, involving re-greening of creamy white petaloid sepals at the later stages. The greenish sepals become photosynthetically competent immediately after pollination and persist until the seeds are set. After the seed set, the entire (green) flower abscises from the plant. Flower development of Helleborus orientalis cv. Olympicus growing in the open was divided into six stages (I-VI) from tight bud stage to the senescent stage. The average life span of an individual flower after it is fully open is about 6 days. Membrane permeability of sepal tissues estimated as electrical conductivity of leachates increased during senescence. The content of sugars and soluble proteins in the sepal tissues increased during flower opening and declined thereafter during senescence. The protease activity increased as the flower progressed towards senescence. From the present study, it becomes evident that decline in the sugar status and elevation in specific protease activity leading to degradation of proteins are the important factors regulating development and senescence in H. orientalis flowers. Although the tissue content of soluble proteins registered an overall quantitative decrease but SDS-PAGE of protein extract from sepal tissues suggested a decrease in the expression of high molecular weight proteins and an increase in low molecular weight proteins during flower development and senescence. At this stage it is not known whether the polypeptides that increased during senescence play an important role in the senescence of Helleborus orientalis flowers. The increase in these polypeptides during flower senescence is of particular interest because they may be linked to flower longevity. Understanding the nature of these proteins can provide new insights into the pathways that execute senescence and the post-transcriptional regulation of senescence in this flower system.
Keywords: Flower senescence; Helleborus orientalis; Membrane permeability; Protease activity; SDS-PAGE; α-amino acids.