| 2010 |
NOA1 (knockout mice and in vitro assays) is required for mitochondrial protein synthesis; NOA1-deficient cells show deficient mitochondrial protein synthesis, global OXPHOS defect, and anomalous sedimentation of mitochondrial ribosomal subunits consistent with a defect in mitochondrial ribosome assembly. In vitro, intrinsic NOA1 GTPase activity was stimulated by bacterial ribosomal constituents. |
Knockout mouse generation, sucrose gradient centrifugation of mitochondrial ribosomal subunits, Western blotting, in vitro GTPase activity assay with ribosomal constituents |
Molecular biology of the cell |
High |
21118999
|
| 2012 |
Human C4orf14 (NOA1) co-purifies with the small 28S mitochondrial ribosomal subunit and co-fractionates with it on sucrose gradients. Gene silencing specifically reduced components of the small subunit and decreased mitochondrial protein synthesis. The GTPase activity of C4orf14 and bound GTP were both critical for interaction with the 28S subunit. C4orf14 also associates with mitochondrial nucleoids and binds DNA in vitro; its silencing caused mitochondrial DNA depletion. |
Co-purification of recombinant C4orf14 from human cells, sucrose gradient fractionation, gene silencing (siRNA), in vitro DNA binding assay, immunoprecipitation with mitochondrial translation factors |
Nucleic acids research |
High |
22447445
|
| 2008 |
hNOA1 is peripherally associated with the inner mitochondrial membrane facing the matrix. By immunoprecipitation-mass spectrometry, endogenous hNOA1 interacts with Complex I of the electron transport chain and with DAP3 (death-associated protein 3). Knockdown of hNOA1 reduces mitochondrial O2 consumption ~20% in a Complex I-dependent manner and renders cells more resistant to apoptotic stimuli (gamma-interferon and staurosporine). |
Immunofluorescence, immunoelectron microscopy, mitochondrial subfractionation, immunoprecipitation-mass spectrometry, siRNA knockdown with O2 consumption assay and apoptosis assay |
The Journal of biological chemistry |
High |
19103604
|
| 2011 |
Mouse NOA1 (mNOA1) localizes predominantly in the mitochondrial matrix and interacts with several high-molecular-mass complexes, most notably Complex IV of the respiratory chain and the prohibitin complex. Knockdown of mNOA1 impaired enzyme activity of complexes I+III, resulting in oxidative stress and cell death. mNOA1 is transcriptionally regulated in an oxygen-sensitive manner. |
Mitochondrial fractionation, blue-native PAGE/interaction analysis, siRNA knockdown with enzyme activity assays and oxidative stress measurements |
The Journal of biological chemistry |
Medium |
21771794
|
| 2013 |
NOA1 binds specifically to oligonucleotides that fold into G-quadruplex structures (identified by SELEX), and binding of G-quadruplex oligonucleotides stimulates the GTPase activity of NOA1, establishing a regulatory link between G-quadruplex-containing RNAs and NOA1 GTPase function. |
SELEX with recombinant wildtype NOA1 and GTPase mutant NOA1-K353R, GTPase activity assay with G-quadruplex oligonucleotides |
Biochimica et biophysica acta |
Medium |
23933583
|
| 2014 |
Newly translated NOA1 is first imported into the nucleus (localizing to the nucleolus where it interacts with UBF1) before nuclear export (via a CRM1/leptomycin-B-sensitive NES) and subsequent import into mitochondria. Mutation of the nuclear localization signal (NLS) prevented both nuclear and mitochondrial import; deletion of the N-terminal mitochondrial targeting sequence (MTS) caused nuclear accumulation and increased caspase-dependent apoptosis. NOA1 is also a substrate of the mitochondrial matrix protease complex ClpXP. |
Live cell imaging/immunofluorescence of NLS/NES/MTS mutants, leptomycin-B inhibition, ClpXP substrate assay, co-immunoprecipitation with UBF1 |
PloS one |
Medium |
25072814
|
| 2012 |
Yeast Mtg3 (NOA1 ortholog) is required for assembly of the mitochondrial 30S (small) ribosomal subunit but not the 54S (large) subunit. Mutations in MTG3 cause accumulation of a 15S rRNA precursor with an 80-nucleotide 5' extension. Overexpression of Mrpl4p (a 54S constituent at the peptide exit site) partially rescues the respiratory deficiency of mtg3 null mutants, accompanied by increased processed 15S rRNA, suggesting Mtg3p and Mrpl4p jointly regulate small subunit assembly by modulating 15S rRNA processing. |
Genetic screen, sucrose gradient sedimentation, immunoblotting with subunit-specific antibodies, Northern blot for rRNA precursors, genetic rescue by overexpression |
The Journal of biological chemistry |
High |
22621929
|
| 2024 |
The C-terminal domain of yeast Mtg3 (NOA1 ortholog) is required for robust binding to the mitoribosome, as shown by sucrose density gradient analysis. Point mutants that abrogate GTP/GDP binding and GTPase activity compromise protein function in vivo, but surprisingly, mitoribosome association was not compromised in nucleotide-binding/hydrolysis-deficient mutants, supporting a model where Mtg3 binds precursor mitoribosomes through its C-terminus while GTP/GDP cycling drives a conformational change or validates a folding intermediate. |
Sucrose density gradient fractionation, C-terminal deletion mutants, point mutagenesis of GTPase active site, in vivo functional complementation assay |
Biochemical and biophysical research communications |
Medium |
39180962
|
| 2025 |
WTAP regulates m6A methylation of NOA1 mRNA (confirmed by MeRIP-qPCR), and WTAP knockdown leads to mitochondrial damage (smaller mitochondria, compressed intermembrane space, reduced mitochondrial membrane potential), suggesting NOA1 is a downstream effector of WTAP-mediated m6A modification in maintaining mitochondrial integrity. |
MeRIP-qPCR for m6A methylation of NOA1, WTAP conditional knockout, electron microscopy for mitochondrial morphology, mass spectrometry identification of NOA1 as WTAP-related protein |
Journal of Cancer |
Low |
39744575
|