Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 9, Pages 5483-5494Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku179
Keywords
-
Categories
Funding
- Medical Health Research Infrastructure Funding of Western Australia
- National Health and Medical Research Council [APP1058442, APP1045677, APP1041582, APP1023460, APP1005030]
- Australian Research Council [FT0991008, FT0991113, DP140104111]
- Dora Lush scholarship from the National Health and Medical Research Council [APP1039101]
- Australian Research Council [FT0991008, FT0991113] Funding Source: Australian Research Council
Ask authors/readers for more resources
Mitochondrial gene expression is predominantly regulated at the post-transcriptional level and mitochondrial ribonucleic acid (RNA)-binding proteins play a key role in RNA metabolism and protein synthesis. The AU-binding homolog of enoyl-coenzyme A (CoA) hydratase (AUH) is a bifunctional protein with RNA-binding activity and a role in leucine catabolism. AUH has a mitochondrial targeting sequence, however, its role in mitochondrial function has not been investigated. Here, we found that AUH localizes to the inner mitochondrial membrane and matrix where it associates with mitochondrial ribosomes and regulates protein synthesis. Decrease or overexpression of the AUH protein in cells causes defects in mitochondrial translation that lead to changes in mitochondrial morphology, decreased mitochondrial RNA stability, biogenesis and respiratory function. Because of its role in leucine metabolism, we investigated the importance of the catalytic activity of AUH and found that it affects the regulation of mitochondrial translation and biogenesis in response to leucine.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available