Journal
BIOCHEMISTRY
Volume 57, Issue 38, Pages 5564-5575Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.8b00726
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Funding
- Timken Sturgis Foundation Award
- Salk Women in Science Fellowship
- Pioneer Fellowship
- NIH Fellowship [GM123685]
- Mass Spectrometry Core of the Salk Institute
- NIH-NCI CCSG [P30 014195]
- Helmsley Center for Genomic Medicine
- National Institutes of Health
- National Cancer Institute Cancer Center Support grants [P30 (CA014195), R01 (GM102491), P41 (GM103533), R01 (MH067880)]
- Leona M. and Harry B. Helmsley Charitable Trust [2012-PG-MED002]
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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.
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