Unknown

Dataset Information

0

CryoEM structure of yeast Arginyltransferase 1 (ATE1)


ABSTRACT:

SUBMITTER: Wei Huang 

PROVIDER: EMPIAR-11590 | biostudies-other |

REPOSITORIES: biostudies-other

altmetric image

Publications

The structural basis of tRNA recognition by arginyl-tRNA-protein transferase.

Abeywansha Thilini T   Huang Wei W   Ye Xuan X   Nawrocki Allison A   Lan Xin X   Jankowsky Eckhard E   Taylor Derek J DJ   Zhang Yi Y  

Nature communications 20230419 1


Arginyl-tRNA-protein transferase 1 (ATE1) is a master regulator of protein homeostasis, stress response, cytoskeleton maintenance, and cell migration. The diverse functions of ATE1 arise from its unique enzymatic activity to covalently attach an arginine onto its protein substrates in a tRNA-dependent manner. However, how ATE1 (and other aminoacyl-tRNA transferases) hijacks tRNA from the highly efficient ribosomal protein synthesis pathways and catalyzes the arginylation reaction remains a myste  ...[more]

Similar Datasets

| S-EPMC5129878 | biostudies-literature
| S-EPMC5893162 | biostudies-literature
| S-EPMC9160021 | biostudies-literature
| S-EPMC8318291 | biostudies-literature
| S-EPMC8769551 | biostudies-literature
| S-EPMC5934336 | biostudies-literature
| S-EPMC5410850 | biostudies-literature
| S-EPMC7608217 | biostudies-literature
| S-EPMC9701221 | biostudies-literature
| S-EPMC8119973 | biostudies-literature