Physiological and mutational protein variations in the ciliary membrane of Paramecium.
The proteins in the ciliary membrane of wild-type and mutant Paramecium tetraurelia are examined with SDS and IEF gels. Over 80% of the proteins in the ciliary membrane belong to two groups: the immobilization antigen (I-Ag), which is a 220-280 kD surface protein, and a set of at least four integral proteins slightly over 40 kD (the 40 k), most of which focus near pH 4.0 (the acidic 40 k). Variations of the I-Ag in its apparent molecular weight appear spontaneously in different clones of the same strain and can be triggered by changing the culture temperatures. We discovered that the members of the acidic 40 k family also vary in their relative proportion. Furthermore, the variations in I-Ag and those in acidic 40 k are tightly coupled. The concerted changes suggest a co-regulation in the synthesis of these proteins. The ciliary membranes of 20 mutants of 11 complementation groups known for their behavioral and electrophysiological defects are examined. Coupled variations of I-Ag and acidic 40 k among clones, similar to those of the wild type, are seen. Besides the I-Ag and the acidic 40 k, this membrane has over 60 other species of proteins, most of which are invariant. Shifts in the isoelectric points of two of these minor proteins have been correlated with two different mutations, 'fast-2' and 'paranoiac A'. No electrophoretic shifts can be correlated with the 'pawn B' mutation as found by Merkel et al. [35].
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002923:Cilia / Q000378:metabolism*; D005796:Genes; D008565:Membrane Proteins / Q000235:genetics* / Q000302:isolation & purification; D008970:Molecular Weight; D009154:Mutation; D010247:Paramecium / Q000235:genetics*; D013045:Species Specificity
D008565:Membrane Proteins