A flagellar surface glycoprotein mediating cell-substrate interaction in Chlamydomonas.
The Chlamydomonas flagellar surface exhibits interesting adhesive properties that are associated with flagellar surface motility. This dynamic surface property can be exhibited as the binding and movement of small polystyrene microspheres or as the interaction of the flagellar surface with a solid substrate followed by whole cell locomotion, termed "gliding". In order to identify flagellar surface proteins that mediate substrate interaction during flagellar surface motility, two immobilized iodination systems were employed that mimic the conditions for flagellar surface motility: small polystyrene microspheres derivatized with lactoperoxidase, and large glass beads derivatized with Iodogen. Use of these iodination conditions resulted in preferential iodination of a high-molecular-weight glycoprotein with apparent molecular weight of 300,000-350,000. These results suggest this glycoprotein as a major candidate for the surface-exposed adhesive component that directly interacts with the substrate and couples the substrate to a system of force transduction presumed to be located within the flagellum.
D002448:Cell Adhesion; D002696:Chlamydomonas / Q000502:physiology*; D005407:Flagella / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D007455:Iodine / Q000378:metabolism; D008970:Molecular Weight; D014508:Urea / Q000031:analogs & derivatives
D006023:Glycoproteins; C012385:1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril; D014508:Urea; D007455:Iodine