Paramecium GPI Proteins: Variability of Expression and Localization

In Paramecium primaurelia, the two major classes of cell surface proteins, the surface antigen (SAg) and the surface GPI proteins (SGPs), are linked to the plasma membrane through a glycosylphosphatidylinositol (GPI) anchor. In the present study, we have characterized the expression of the SGPs in s...

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Bibliographic Details
Published in:Protist 2000-08, Vol.151 (2), p.161-169
Main Author: Capdeville, Yvonne
Format: Article
Language:English
Subjects:
Animals
Antigens, Protozoan - biosynthesis
Antigens, Protozoan - isolation & purification
Antigens, Surface - biosynthesis
Antigens, Surface - isolation & purification
Chemical Fractionation
Glycosylphosphatidylinositols - metabolism
GPI protein
GPI proteins
membrane domain segregation
Membrane Proteins - biosynthesis
Membrane Proteins - isolation & purification
Membrane Proteins - metabolism
Paramecium
Paramecium - growth & development
Paramecium - metabolism
PI-PLC
Protozoan Proteins - biosynthesis
Protozoan Proteins - isolation & purification
Protozoan Proteins - metabolism
regulation
surface GPI protein
Temperature
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Summary:In Paramecium primaurelia, the two major classes of cell surface proteins, the surface antigen (SAg) and the surface GPI proteins (SGPs), are linked to the plasma membrane through a glycosylphosphatidylinositol (GPI) anchor. In the present study, we have characterized the expression of the SGPs in several geographical strains of P. primaurelia and P. tetraurelia at different temperatures, 23 °C and 32 °C. The identification of the expressed SGPs was performed on purified cilia, by establishing the SGP SDS-PAGE profiles under four different conditions: with or without their anchoring lipid, cleaved with a Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), and either in a reduced or in an unreduced state. This screening revealed the existence of specific sets of ciliary SGPs, as a function of temperature and the geographical origin of the strains. The SGPs the most abundant at 23 °C and 32 °C displayed a rapid turnover. We also looked for the presence of PI-PLC releasable proteins in purified cortices. In addition to the SAg and SGPs, the cortical fraction was shown to contain other PI-PLC releasable proteins, not found in the ciliary fraction, thus localized exclusively in the interciliary region.
ISSN:1434-4610
1618-0941
DOI:10.1078/1434-4610-00016