Characterization of a molecular chaperone present in the eukaryotic flagellum

Eukaryot Cell. 2005 Sep;4(9):1591-4. doi: 10.1128/EC.4.9.1591-1594.2005.

Abstract

Chlamydomonas flagella contain a molecular chaperone now identified as HSP70A, a major cytoplasmic isoform. HSP70A synthesis is upregulated by deflagellation, and its distribution in the flagellum overlaps with the IFT kinesin-II motor FLA10. HSP70A may chaperone flagellar proteins during transport, participating in the assembly and maintenance of the flagellum.

Publication types

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

MeSH terms

  • Animals
  • Chlamydomonas reinhardtii / physiology*
  • Flagella / metabolism*
  • HSP70 Heat-Shock Proteins / genetics
  • HSP70 Heat-Shock Proteins / metabolism*
  • Microtubule-Associated Proteins / metabolism
  • Molecular Chaperones*
  • Protein Transport
  • Protozoan Proteins / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Protozoan / genetics
  • RNA, Protozoan / metabolism

Substances

  • HSP70 Heat-Shock Proteins
  • KHP1 protein, Chlamydomonas
  • Microtubule-Associated Proteins
  • Molecular Chaperones
  • Protozoan Proteins
  • RNA, Messenger
  • RNA, Protozoan