Architecture and function of IFT complex proteins in ciliogenesis - PubMed (original) (raw)

(a) Schematic representations of the primary structures of the 20 C. reinhardtii IFT proteins identified to date. Predicted secondary structure elements and domains/motifs identified using bioinformatics are indicated according to the legend. For IFT25, IFT27 and the N-terminal domain of IFT54, the available crystal and NMR structures where used to identify domains and derive the secondary structure. For subunits with no 3D structure determined, the secondary structure was predicted using the PSIPRED algorithm (Jones, 1999). Tetratricopeptide repeats (TPR) were predicted using the algorithms TPRpred (

http://toolkit.tuebingen.mpg.de/tprpred

) and REP (

http://www.embl.de/andrade/papers/rep/search.html

). The program REP was also used to predict WD40 repeats. Coiled coils were identified using COILS (Lupas et al., 1991;

http://toolkit.tuebingen.mpg.de/pcoils

) and Calponin-homology (CH) domains were identified using the HHPred algorithm (Soding et al., 2005;

http://toolkit.tuebingen.mpg.de/hhpred

) for IFT81 and IFT57. The CH domain of IFT54 was identified based on the determined NMR structure of this domain (PDB code 2EQO). (b) Simplified interaction map of IFT proteins and associated factors (see text for details). Direct interactions are indicated with solid lines and potential interactions with dashed lines. Abbreviation for the organisms in which the interactions have been reported are as follows: Cr, Chlamydomonas reinhardtii; Ce, Caenorhabditis elegans; Hs, Homo sapiens, Dr, Danio rerio; Mm, Mus musculus.