SirT3 is a nuclear NAD + -dependent histone deacetylase that translocates to the mitochondria upon cellular stress
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Implication
Experimental study reveals SirT3 deacetylates histone H4-K16 in human cell nuclei and relocates to mitochondria under stress, suggesting a dual-compartment response to cellular damage.
Key Points
- To characterize the subcellular localization, enzymatic targets, and stress-dependent trafficking of human SirT3.
- Evaluated the deacetylase activity of full-length (~44 kDa) and N-terminally processed human SirT3 against histone targets in vitro and in vivo.
- Tracked the subcellular distribution of SirT3 under baseline growth conditions and cellular stress (etoposide, UV-irradiation, and protein overexpression) using an N-terminus-specific antibody.
- SirT3 resides in both the nucleus and the mitochondria under normal growth conditions in human cells.
- Both full-length and processed SirT3 specifically deacetylate histone H4-K16 in vitro and in vivo upon gene recruitment.
- Cellular stress triggered by UV irradiation, etoposide-induced DNA damage, or SirT3 overexpression induces the translocation of SirT3 from the nucleus to the mitochondria.
Cite This Study
Scher et al. (2007) studied this question.