Characterization of a molecular chaperone present in the eukaryotic flagellum.
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.
Shapiro
Jessica
J
Department of Biology, Haverford College, 370 Lancaster Ave., Haverford, Pennsylvania 19041, USA.
Ingram
Jessica
J
Johnson
Karl A
KA
D020418:Algal Proteins; D000818:Animals; D016825:Chlamydomonas reinhardtii / Q000502:physiology*; D005407:Flagella / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D018832:Molecular Chaperones; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D016053:RNA, Protozoan / Q000235:genetics / Q000378:metabolism
D020418:Algal Proteins; D018840:HSP70 Heat-Shock Proteins; C088230:KHP1 protein, Chlamydomonas; D008869:Microtubule-Associated Proteins; D018832:Molecular Chaperones; D015800:Protozoan Proteins; D012333:RNA, Messenger; D016053:RNA, Protozoan