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Biochemistry. 2018 Sep 25;57(38):5564-5575. doi: 10.1021/acs.biochem.8b00726. Epub 2018 Sep 14.

MIEF1 Microprotein Regulates Mitochondrial Translation.

Author information

1
Clayton Foundation Laboratories for Peptide Biology , The Salk Institute for Biological Studies , 10010 North Torrey Pines Road , La Jolla , California 92037 , United States.
2
Division of Biological Sciences , University of California, San Diego , 9500 Gilman Drive , La Jolla , California 92093 , United States.
3
Mass Spectrometry Core for Proteomics and Metabolomics , The Salk Institute for Biological Studies , 10010 North Torrey Pines Road , La Jolla , California 92037 , United States.
4
Department of Molecular Medicine , The Scripps Research Institute , 10550 North Torrey Pines Road , La Jolla , California 92037 , United States.

Abstract

Recent technological advances led to the discovery of hundreds to thousands of peptides and small proteins (microproteins) encoded by small open reading frames (smORFs). Characterization of new microproteins demonstrates their role in fundamental biological processes and highlights the value in discovering and characterizing more microproteins. The elucidation of microprotein-protein interactions (MPIs) is useful for determining the biochemical and cellular roles of microproteins. In this study, we characterize the protein interaction partners of mitochondrial elongation factor 1 microprotein (MIEF1-MP) using a proximity labeling strategy that relies on APEX2. MIEF1-MP localizes to the mitochondrial matrix where it interacts with the mitochondrial ribosome (mitoribosome). Functional studies demonstrate that MIEF1-MP regulates mitochondrial translation via its binding to the mitoribosome. Loss of MIEF1-MP decreases the mitochondrial translation rate, while an elevated level of MIEF1-MP increases the translation rate. The identification of MIEF1-MP reveals a new gene involved in this process.

PMID:
30215512
PMCID:
PMC6443411
DOI:
10.1021/acs.biochem.8b00726
[Indexed for MEDLINE]
Free PMC Article

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