Two-dimensional analysis of flagellar proteins from wild-type and paralyzed mutants of Chlamydomonas reinhardtii.
Flagellar polypeptides of Chlamydomonas reinhardtii were analyzed in two-dimensions by isoelectric focusing and electrophoresis in the presence of sodium dodecyl sulfate. In addition to flagellar tubulin, over 130 polypeptides were resolved and 100 of these were identified as axonemal components in wild-type organisms. Flagella of two nonconditional paralyzed mutants, pf 14 and pf 1, were also analyzed and, at the same time, electron microscopic studies were carried out. pf 14 flagella, which completely lack radial spokes and associated spokeheads, are missing 12 polypeptides. Six of these polypeptides are also missing from pf 1 flagella in which spokes are clearly present but spoke heads appear to be absent.
D002465:Cell Movement; D002696:Chlamydomonas / Q000648:ultrastructure*; D004591:Electrophoresis, Polyacrylamide Gel; D005407:Flagella / Q000648:ultrastructure*; D008854:Microscopy, Electron; D008970:Molecular Weight; D009154:Mutation; D010940:Plant Proteins / Q000302:isolation & purification; D013045:Species Specificity
D010940:Plant Proteins
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