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Related Concept Videos

Synteny and Evolution02:31

Synteny and Evolution

John H. Renwick first coined the term “synteny” in 1971, which refers to the genes present on the same chromosomes, even if they are not genetically linked. The species with common ancestry tend to show conserved syntenic regions. Therefore, the concept of synteny is nowadays used to describe the evolutionary relationship between species.
Around 80 million years ago, the human and mice lineages diverged from the common ancestor. During the course of evolution, the ancestral chromosome underwent...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
Although the genome of each species varies greatly from each other, a few sequences are highly conserved. Such conserved DNA...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conservation of Protein Domains02:26

Conservation of Protein Domains

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Related Experiment Video

Updated: Jun 18, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Sirtuin/Sir2 phylogeny, evolutionary considerations and structural conservation.

Sebastian Greiss1, Anton Gartner

  • 1Wellcome Trust Centre for Gene Regulation and Expression, University of Dundee, Dundee DD1 5EH, UK.

Molecules and Cells
|November 26, 2009
PubMed
Summary

Sirtuins are NAD(+)-dependent protein deacetylases found in all species. A phylogenetic analysis reveals conserved structures and functions across diverse sirtuin classes, including the seven found in humans.

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Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Sirtuins are a conserved protein family functioning as NAD(+)-dependent deacetylases.
  • Their catalytic activity involves transferring acetyl groups to NAD(+), producing unique metabolites.
  • Sirtuins are present across diverse species, from bacteria to mammals.

Purpose of the Study:

  • To perform a phylogenetic analysis of the sirtuin protein family.
  • To understand the evolutionary relationships and conserved structural features of sirtuins.
  • To investigate the origins and functional diversity of human sirtuins (SIRT1-SIRT7).

Main Methods:

  • Phylogenetic analysis of sirtuin protein sequences.
  • Identification of conserved residues within the catalytic center.
  • Comparative analysis across different species and sirtuin classes.

Main Results:

  • Sirtuins can be classified into over a dozen phylogenetic groups and subclasses.
  • Humans possess seven sirtuins (SIRT1-SIRT7) that emerged early in animal evolution.
  • Conserved residues are clustered around the catalytic center in known sirtuin members.

Conclusions:

  • The sirtuin family exhibits deep evolutionary conservation in structure and function.
  • Human sirtuins play critical roles in diverse cellular processes including aging and metabolism.
  • Phylogenetic insights aid in understanding sirtuin function and evolution.