Subunit interactions and organization of the Chlamydomonas reinhardtii intraflagellar transport complex A proteins.

ABSTRACT: Chlamydomonas reinhardtii intraflagellar transport (IFT) particles can be biochemically resolved into two smaller assemblies, complexes A and B, that contain up to six and 15 protein subunits, respectively. We provide here the proteomic and immunological analyses that verify the identity of all six Chlamydomonas A proteins. Using sucrose density gradient centrifugation and antibody pulldowns, we show that all six A subunits are associated in a 16 S complex in both the cell bodies and flagella. A significant fraction of the cell body IFT43, however, exhibits a much slower sedimentation of ∼2 S and is not associated with the IFT A complex. To identify interactions between the six A proteins, we combined exhaustive yeast-based two-hybrid analysis, heterologous recombinant protein expression i

SUBMITTER: Behal RH 

PROVIDER: S-EPMC3320918 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature