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Stress-Dependent Regulation of FOXO Transcription Factors by the SIRT1 Deacetylase
One way in which members of the Sir2 family of proteins may increase organismal longevity is by tipping FOXO-dependent responses away from apoptosis and toward stress resistance.
RAG-2-deficient mice lack mature lymphocytes owing to inability to initiate V(D)J rearrangement
Loss of RAG-2 function in vivo results in total inability to initiate V(D)J rearrangement, leading to a novel severe combined immune deficient (SCID) phenotype.
SIRT4 Inhibits Glutamate Dehydrogenase and Opposes the Effects of Calorie Restriction in Pancreatic β Cells
It is shown that SIRT4 functions in beta cell mitochondria to repress the activity of GDH by ADP-ribosylation, thereby downregulating insulin secretion in response to amino acids, effects that are alleviated during CR.
SIRT1 Regulates Circadian Clock Gene Expression through PER2 Deacetylation
It is shown that SIRT1, an NAD(+)-dependent protein deacetylase, is required for high-magnitude circadian transcription of several core clock genes, including Bmal1, Rorgamma, Per2, and Cry1.
An early haematopoietic defect in mice lacking the transcription factor GATA-2
It is demonstrated that the transcription factor GATA-2 plays a critical role in haematopoiesis, particularly of an adult type, and proposed that it regulates genes controlling growth factor responsiveness or the proliferative capacity of early haem atopoietic cells.
Efficient in vivo manipulation of mouse genomic sequences at the zygote stage.
A transgenic mouse line carrying the cre transgene under the control of the adenovirus EIIa promoter that targets expression of the Cre recombinase to the early mouse embryo is described and loxP-flanked DNA sequences are efficiently deleted.
A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy
The results suggest that the Sirt1 deacetylase is an important in vivo regulator of autophagy and provide a link between sirtuin function and the overall cellular response to limited nutrients.
Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α
SIRT1 is identified as a functional regulator of PGC‐1α that induces a metabolic gene transcription program of mitochondrial fatty acid oxidation in response to low glucose concentrations and has implications for understanding selective nutrient adaptation and how it might impact lifespan or metabolic diseases such as obesity and diabetes.
Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine Acetylation
It is demonstrated that SIRT3 has evolved to control reversible lysine acetylation in this organelle and is shown to be a soluble mitochondrial protein.
SIRT 3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
Sirtuins are NAD-dependent protein deacetylases. They mediate adaptive responses to a variety of stresses, including calorie restriction and metabolic stress. Sirtuin 3 (SIRT3) is localized in the