The At1g79010 antibody is directed against the NDUFS8.2 protein (AT1G79010), a nuclear-encoded subunit of Complex I in Arabidopsis thaliana. Complex I (NADH dehydrogenase) is a critical enzyme in the electron transport chain, catalyzing NADH-quinone oxidoreduction .
NDUFS8.2 is essential for the proper assembly and function of Complex I. Mutants deficient in NDUFS8.2 or its homolog NDUFS8.1 (AT1G16700) exhibit severe Complex I defects:
Reduced CI Abundance: Mutants show diminished monomeric Complex I and supercomplex I+III in BN-PAGE assays .
Impaired Activity: Deamino-NADH:Q reductase activity, a marker for Complex I function, is significantly reduced in mutants .
Compensatory Pathways: Increased activity of alternative electron transport chains (e.g., cytochrome c oxidase, AOX) may mitigate energy deficits in mutants .
| Phenotype | Wild Type | Double Mutant (ndufs8.1 ndufs8.2) |
|---|---|---|
| CI Abundance | High | Undetectable |
| Supercomplex I+III | Present | Absent |
| AOX Activity | Low | Markedly increased |
The At1g79010 antibody has been utilized in studies to:
CIAF1 (At1g76060): A LYR-motif protein required for Complex I assembly. Mutants lacking CIAF1 show reduced Complex I abundance and activity, paralleling NDUFS8.2-deficient phenotypes .
Immunodetection: The antibody is used to monitor NDUFS8.2 levels in BN-PAGE and Western blotting to assess assembly defects .
Photoperiod Effects: Mutants with NDUFS8.2 deficiency show altered growth and Complex I activity under varying light conditions, highlighting environmental modulation of mitochondrial function .
While primarily studied in Arabidopsis, NDUFS8.2 homologs exist in other organisms. For example, yeast and fungal LYR proteins (e.g., YALI0D07216g) share functional parallels in Complex I biogenesis .
The antibody shows high specificity to NDUFS8.2 with no reported cross-reactivity to other mitochondrial proteins (e.g., COX II, SDH1-1) in immunoblotting . This specificity is critical for distinguishing Complex I subunits from other respiratory chain components.