Journal
PROTOPLASMA
Volume 235, Issue 1-4, Pages 77-89Publisher
SPRINGER WIEN
DOI: 10.1007/s00709-009-0033-z
Keywords
Fibrillarin; Glycine max; Immunofluorescence; Nucleolar architecture; Nucleolar Christmas trees; Nucleophosmin
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Funding
- University of Lodz [505/393]
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The nucleolar proteins, fibrillarin and nucleophosmin, have been identified immunofluorescently in the root meristematic cells of soybean seedlings under varying experimental conditions: at 25A degrees C (control), chilling at 10A degrees C for 3 h and 4 days and recovery from the chilling stress at 25A degrees C. In each experimental variant, the immunofluorescence signals were present solely at the nucleolar territories. Fluorescent staining for both proteins was mainly in the shape of circular domains that are assumed to correspond to the dense fibrillar component of the nucleoli. The fewest fluorescent domains were observed in the nucleoli of chilled plants, and the highest number was observed in the plants recovered after chilling. This difference in the number of circular domains in the nucleoli of each variant may indicate various levels of these proteins in each variant. Both the number of circular domains and the level of these nucleolar proteins changed with changes in the transcriptional activity of the nucleoli, with the more metabolically active cell having higher numbers of active areas in the nucleolus and higher levels of nucleolar proteins, and conversely. Electron microscopic studies revealed differences in the ultrastructure of the nucleoli in all experimental variants and confirmed that the number of fibrillar centres surrounded by dense fibrillar component was the lowest in the nucleoli of chilled plants, and the highest in the nucleoli of recovered seedlings.
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