Dynein motors of the Chlamydomonas flagellum.
Chlamydomonas is a biflagellate unicellular green alga that has proven especially amenable for the analysis of microtubule (MT)-based molecular motors, notably dyneins. These enzymes form the inner and outer arms of the flagellum and are also required for intraflagellar transport. Dyneins have masses of approximately 1-2 MDa and consist of up to 15 different polypeptides. Nucleotide binding/hydrolysis and MT motor activity are associated with the heavy chains, and we detail here our current model for the substructural organization of these approximately 520-kDa proteins. The remaining polypeptides play a variety of roles in dynein function, including attachment of the motor to cargo, regulation of motor activity in response to specific inputs, and their necessity for the assembly and/or stability of the entire complex. The combination of genetic, physiological, structural, and biochemical approaches has made the Chlamydomonas flagellum a very powerful model system in which to dissect the function of these fascinating molecular motors.
DiBella
L M
LM
Department of Biochemistry, University of Connecticut Health Center, Farmington 06032, USA.
King
S M
SM
D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport; D002118:Calcium / Q000378:metabolism; D002696:Chlamydomonas / Q000166:cytology / Q000201:enzymology* / Q000235:genetics; D004398:Dyneins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005407:Flagella / Q000201:enzymology* / Q000378:metabolism; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D007527:Isoenzymes; D046911:Macromolecular Substances; D020409:Molecular Motor Proteins; D004398:Dyneins; D002118:Calcium