Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora.

@article{Tucker2010BiologicallyAI,
  title={Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora.},
  author={Alex C. Tucker and Jorge C Escalante-Semerena},
  journal={Journal of bacteriology},
  year={2010},
  volume={192 23},
  pages={6200-8}
}
Sirtuins are NAD(+)-dependent protein deacylases that are conserved in all domains of life and are involved in diverse cellular processes, including control of gene expression and central metabolism. Eukaryotic sirtuins have N-terminal extensions that have been linked to protein multimerization and cellular localization. Here the first evidence of sirtuin isoforms in bacteria is reported. The enterobacterium Salmonella enterica synthesizes two isoforms of CobB sirtuin, a shorter 236-amino-acid… CONTINUE READING

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