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Rapid Isolation of the Mitoribosome from HEK Cells
Published on: October 4, 2018
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Human GTPBP10 is required for mitoribosome maturation
Priyanka Maiti1, Hyun-Jung Kim2, Ya-Ting Tu2
1Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Nucleic Acids Research
|October 16, 2018
Summary
GTPBP10 is crucial for mitochondrial ribosome assembly, ensuring proper large subunit maturation and coordinating subunit accumulation for effective protein synthesis.
Area of Science:
- Mitochondrial biology
- Molecular cell biology
- Ribosome biogenesis
Background:
- Mitochondrial ribosome (mitoribosome) biogenesis is essential for cellular respiration.
- Mitoribosome assembly factors are localized to RNA granules near mitochondrial DNA.
- The roles of specific GTPases in mitoribosome assembly are not fully understood.
Purpose of the Study:
- To investigate the function of GTPBP10, a small GTPase, in mitoribosome biogenesis.
- To determine the impact of GTPBP10 deficiency on mitochondrial protein synthesis.
Main Methods:
- Proteomic analysis of RNA granules.
- Gene-editing (CRISPR/Cas9) to create GTPBP10 knockout HEK293T cells.
- Biochemical assays including co-sedimentation, rRNA interaction studies, and crosslinking.
Main Results:
- GTPBP10 is a mitochondrial protein essential for mitoribosome assembly.
- GTPBP10 deficiency leads to reduced large (mtLSU) and small (mtSSU) mitoribosome subunits and absence of 55S monosomes.
- GTPBP10 interacts with 16S rRNA and mtLSU proteins, and is indirectly required for rRNA precursor processing.
Conclusions:
- GTPBP10 is a key factor for mtLSU maturation and coordinates mtSSU and mtLSU accumulation.
- GTPBP10 acts as a quality control checkpoint during mtLSU assembly, preventing premature subunit joining.
- GTPBP10 is indispensable for mitochondrial protein synthesis.
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