A STRESS-INDUCED PROTEIN ASSOCIATED WITH THE GIRDLE BAND REGION OF THE DIATOM THALASSIOSIRA PSEUDONANA (BACILLARIOPHYTA)

We report the characterization of a cell-surface protein isolated from the centric diatom Thalassiosira pseudonana Hasle and Heimdal. This protein has an apparent molecular weight of 150 kDa, is highly acidic, and is intimately associated with the cell wall. Although originally identified in cells e...

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Bibliographic Details
Published in:Journal of phycology 2005-06, Vol.41 (3), p.577-589
Main Authors: Davis, Aubrey K., Hildebrand, Mark, Palenik, Brian
Format: Article
Language:English
Subjects:
Bacillariophyta
cell cycle
cell surface
chitin binding domains
copper
diatom
girdle band
iron
Marine
silicon
stress
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Summary:We report the characterization of a cell-surface protein isolated from the centric diatom Thalassiosira pseudonana Hasle and Heimdal. This protein has an apparent molecular weight of 150 kDa, is highly acidic, and is intimately associated with the cell wall. Although originally identified in cells experiencing copper toxicity, it is also induced by silicon and iron limitation but not by phosphate or nitrate limitation. Using immunofluorescence techniques, the 150-kDa protein was localized to the girdle band region and covered the elongated girdle band region of morphologically aberrant cells suffering from copper toxicity. Although having biochemical similarities to girdle band associated proteins identified in pennate diatoms known as pleuralins, the 150-kDa protein is not a sequence homolog and is predicted to have a number of unique features, such as chitin binding domains and a possible RGD cell attachment motif. Results presented here suggest that this protein is normally cell cycle regulated and may be involved in stabilizing cells during the division process.
ISSN:0022-3646
1529-8817
DOI:10.1111/j.1529-8817.2005.00076.x