Characterization of the cilia and ciliary membrane proteins of wild-type Paramecium tetraurelia and a pawn mutant.

Cilia and ciliary membranes were isolated from axenically grown, wild-type Paramecium tetraurelia strain 51s and from the extreme pawn mutant strain, d495, derived from this parental strain. Over 60 protein bands having molecular weights of 15 to greater than 300 kdaltons were detected by Coomassie Blue staining of whole cilia proteins separated by one-dimensional SDS polyacrylamide gel electrophoresis. About 30 of these protein bands were visible in Coomassie Blue-stained membrane separations. About 60 bands were detected by silver staining of one-dimensional gels of membrane proteins. Differences between Coomassie Blue-stained separations of wild-type and pawn mutant strain d495 membrane proteins were seen in the quantity of a band present at 43 kdaltons. Radioiodination of cell surface proteins labeled approximately 15 protein bands in both wild-type and mutant cilia. The major axonemal proteins were unlabeled. Six membrane glycoproteins were identified by staining one-dimensional separations with iodinated concanavalin A and lentil lectin, two lectins that specifically bind both glucose and mannose residues. Two major neutral sugar species present in an acid hydrolysate of the cilia preparation were tentatively identified as glucose and mannose by gas chromatography of the alditol acetate derivatives.