Rapid inactivation of the yeast Sec complex selectively blocks transport of post-translationally translocated proteins.

ABSTRACT: The yeast endoplasmic reticulum has three distinct protein translocation channels. The heterotrimeric Sec61 and Ssh1 complexes, which bind translating ribosomes, mediate cotranslational translocation of proteins targeted to the endoplasmic reticulum by the signal recognition particle (SRP) and SRP receptor targeting pathway, whereas the heptameric Sec complex has been proposed to mediate ribosome-independent post-translational translocation of proteins with less hydrophobic signal sequences that escape recognition by the SRP. However, multiple reports have proposed that the Sec complex may function cotranslationally and be involved in translocation or integration of SRP-dependent protein translocation substrates. To provide insight into these conflicting views, we induced expression of the

SUBMITTER: Yi JK 

PROVIDER: S-EPMC8503631 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature