Unknown

Dataset Information

0

Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo-tomography.


ABSTRACT: We employed electron cryo-tomography to visualize cytosolic ribosomes on the surface of mitochondria. Translation-arrested ribosomes reveal the clustered organization of the TOM complex, corroborating earlier reports of localized translation. Ribosomes are shown to interact specifically with the TOM complex, and nascent chain binding is crucial for ribosome recruitment and stabilization. Ribosomes are bound to the membrane in discrete clusters, often in the vicinity of the crista junctions. This interaction highlights how protein synthesis may be coupled with transport. Our work provides unique insights into the spatial organization of cytosolic ribosomes on mitochondria.

SUBMITTER: Gold VA 

PROVIDER: S-EPMC5623831 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Visualization of cytosolic ribosomes on the surface of mitochondria by electron cryo-tomography.

Gold Vicki Am VA   Chroscicki Piotr P   Bragoszewski Piotr P   Chacinska Agnieszka A  

EMBO reports 20170821 10


We employed electron cryo-tomography to visualize cytosolic ribosomes on the surface of mitochondria. Translation-arrested ribosomes reveal the clustered organization of the TOM complex, corroborating earlier reports of localized translation. Ribosomes are shown to interact specifically with the TOM complex, and nascent chain binding is crucial for ribosome recruitment and stabilization. Ribosomes are bound to the membrane in discrete clusters, often in the vicinity of the crista junctions. This  ...[more]

Similar Datasets

| S-EPMC4828066 | biostudies-literature
| S-EPMC4898762 | biostudies-literature
| S-EPMC4660369 | biostudies-literature
| S-EPMC6160218 | biostudies-literature
| EMPIAR-10985 | biostudies-other
| S-EPMC3217200 | biostudies-literature
| S-EPMC8153238 | biostudies-literature
| S-EPMC6175578 | biostudies-literature
| S-EPMC2976456 | biostudies-literature
| EMPIAR-10987 | biostudies-other