Dynein motors of the Chlamydomonas flagellum

Int Rev Cytol. 2001;210:227-68. doi: 10.1016/s0074-7696(01)10007-0.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Calcium / metabolism
  • Chlamydomonas / cytology
  • Chlamydomonas / enzymology*
  • Chlamydomonas / genetics
  • Dyneins / chemistry
  • Dyneins / genetics
  • Dyneins / metabolism*
  • Flagella / enzymology*
  • Flagella / metabolism
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Macromolecular Substances
  • Molecular Motor Proteins / chemistry
  • Molecular Motor Proteins / metabolism*
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding
  • Protein Structure, Tertiary

Substances

  • Isoenzymes
  • Macromolecular Substances
  • Molecular Motor Proteins
  • Dyneins
  • Calcium