AtTPR7 as part of the Arabidopsis Sec post-translocon.

The secretory system in eukaryotic organisms ensures targeting of proteins to their place of function after they entered the endoplasmic reticulum either co- or post-translationally. Thereby proteins are translocated through the Sec translocon into the endoplasmic reticulum. In the Arabidopsis genome homologs for the three major components of the Sec translocon, the central pore Sec61α and the auxiliary proteins Sec62 and Sec63 are present. Phylogenetic analyses show Sec61α to be the most conserved subunit within the Sec translocon whereas Sec62 and Sec63 show less homology but contain the same functional domains among all organisms. We recently characterized a novel tetratricopeptide repeat domain containing protein, AtTPR7, as part of the Arabidopsis Sec translocon which is probably involved in chaperone assisted post-translational import. In this study we investigated the interaction of AtTPR7 with Sec62 as well as the cytosolic chaperones HSP70 and HSP90 not only in vitro but also in vivo to further strengthen the hypothesis of AtTPR7 being a chaperone docking protein of the Sec translocon for secretory preproteins in Arabidopsis.

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