Unknown

Dataset Information

0

Chloroplast Omp85 proteins change orientation during evolution.


ABSTRACT: The majority of outer membrane proteins (OMPs) from gram-negative bacteria and many of mitochondria and chloroplasts are ?-barrels. Insertion and assembly of these proteins are catalyzed by the Omp85 protein family in a seemingly conserved process. All members of this family exhibit a characteristic N-terminal polypeptide-transport-associated (POTRA) and a C-terminal 16-stranded ?-barrel domain. In plants, two phylogenetically distinct and essential Omp85's exist in the chloroplast outer membrane, namely Toc75-III and Toc75-V. Whereas Toc75-V, similar to the mitochondrial Sam50, is thought to possess the original bacterial function, its homolog, Toc75-III, evolved to the pore-forming unit of the TOC translocon for preprotein import. In all current models of OMP biogenesis and preprotein translocation, a topology of Omp85 with the POTRA domain in the periplasm or intermembrane space is assumed. Using self-assembly GFP-based in vivo experiments and in situ topology studies by electron cryotomography, we show that the POTRA domains of both Toc75-III and Toc75-V are exposed to the cytoplasm. This unexpected finding explains many experimental observations and requires a reevaluation of current models of OMP biogenesis and TOC complex function.

SUBMITTER: Sommer MS 

PROVIDER: S-EPMC3158144 | biostudies-other | 2011 Aug

REPOSITORIES: biostudies-other

altmetric image

Publications

Chloroplast Omp85 proteins change orientation during evolution.

Sommer Maik S MS   Daum Bertram B   Gross Lucia E LE   Weis Benjamin L M BL   Mirus Oliver O   Abram Lars L   Maier Uwe-G UG   Kühlbrandt Werner W   Schleiff Enrico E  

Proceedings of the National Academy of Sciences of the United States of America 20110808 33


The majority of outer membrane proteins (OMPs) from gram-negative bacteria and many of mitochondria and chloroplasts are β-barrels. Insertion and assembly of these proteins are catalyzed by the Omp85 protein family in a seemingly conserved process. All members of this family exhibit a characteristic N-terminal polypeptide-transport-associated (POTRA) and a C-terminal 16-stranded β-barrel domain. In plants, two phylogenetically distinct and essential Omp85's exist in the chloroplast outer membran  ...[more]

Similar Datasets

| S-EPMC3720927 | biostudies-literature
| S-EPMC17721 | biostudies-literature
| S-EPMC3405695 | biostudies-literature
| S-EPMC4758235 | biostudies-literature
| S-EPMC24447 | biostudies-literature
| S-EPMC4505566 | biostudies-literature
| S-EPMC5234102 | biostudies-literature
| S-EPMC4192544 | biostudies-literature
| S-EPMC8236006 | biostudies-literature
| S-EPMC7378799 | biostudies-literature