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Mol. Cells 2009; 28(5): 407-415

Published online November 18, 2009

https://doi.org/10.1007/s10059-009-0169-x

© The Korean Society for Molecular and Cellular Biology

Sirtuin/Sir2 Phylogeny, EvolutionaryConsiderations and Structural Conservation

Sebastian Greiss, and Anton Gartner

Received: October 29, 2009; Accepted: November 3, 2009

Abstract

The sirtuins are a protein family named after the first identified member, S. cerevisiae Sir2p. Sirtuins are protein deacetylases whose activity is dependent on NAD+ as a cosubstrate. They are structurally defined by two central domains that together form a highly conserved catalytic center, which catalyzes the transfer of an acetyl moiety from acetyllysine to NAD+, yielding nicotinamide, the unique metabolite O-acetyl-ADP-ribose and deacetylated lysine. One or more sirtuins are present in virtually all species from bacteria to mammals. Here we describe a phylogenetic analysis of sirtuins. Based on their phylogenetic relationship, sirtuins can be grouped into over a dozen classes and subclasses. Humans, like most vertebrates, have seven sirtuins: SIRT1-SIRT7. These function in diverse cellular pathways, regulating transcriptional repression, aging, metabolism, DNA damage responses and apoptosis. We show that these seven sirtuins arose early during animal evolution. Con-served residues cluster around the catalytic center of known sirtuin family members.

Keywords , evolution, molecular phylogeny, SIR2, sirtuin

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Mol. Cells 2009; 28(5): 407-415

Published online November 30, 2009 https://doi.org/10.1007/s10059-009-0169-x

Copyright © The Korean Society for Molecular and Cellular Biology.

Sirtuin/Sir2 Phylogeny, EvolutionaryConsiderations and Structural Conservation

Sebastian Greiss, and Anton Gartner

Received: October 29, 2009; Accepted: November 3, 2009

Abstract

The sirtuins are a protein family named after the first identified member, S. cerevisiae Sir2p. Sirtuins are protein deacetylases whose activity is dependent on NAD+ as a cosubstrate. They are structurally defined by two central domains that together form a highly conserved catalytic center, which catalyzes the transfer of an acetyl moiety from acetyllysine to NAD+, yielding nicotinamide, the unique metabolite O-acetyl-ADP-ribose and deacetylated lysine. One or more sirtuins are present in virtually all species from bacteria to mammals. Here we describe a phylogenetic analysis of sirtuins. Based on their phylogenetic relationship, sirtuins can be grouped into over a dozen classes and subclasses. Humans, like most vertebrates, have seven sirtuins: SIRT1-SIRT7. These function in diverse cellular pathways, regulating transcriptional repression, aging, metabolism, DNA damage responses and apoptosis. We show that these seven sirtuins arose early during animal evolution. Con-served residues cluster around the catalytic center of known sirtuin family members.

Keywords: , evolution, molecular phylogeny, SIR2, sirtuin

Mol. Cells
Sep 30, 2023 Vol.46 No.9, pp. 527~572
COVER PICTURE
Chronic obstructive pulmonary disease (COPD) is marked by airspace enlargement (emphysema) and small airway fibrosis, leading to airflow obstruction and eventual respiratory failure. Shown is a microphotograph of hematoxylin and eosin (H&E)-stained histological sections of the enlarged alveoli as an indicator of emphysema. Piao et al. (pp. 558-572) demonstrate that recombinant human hyaluronan and proteoglycan link protein 1 (rhHAPLN1) significantly reduces the extended airspaces of the emphysematous alveoli by increasing the levels of TGF-β receptor I and SIRT1/6, as a previously unrecognized mechanism in human alveolar epithelial cells, and consequently mitigates COPD.

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