ArticleMolecular and cellular biology2011
The duplicated deacetylases Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- The deacetylase Sir2 is the primary sensor driving transcriptional changes in response to low NAD+ in the yeast Kluyveromyces lactis.Genetics · 2026Article
- Article
- A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs.The Journal of biological chemistry · 2019Article
- Sirtuins in the phylum Basidiomycota: A role in virulence in Cryptococcus neoformans.Scientific reports · 2017Article
- HST1 increases replicative lifespan of a sir2Δ mutant in the absence of PDE2 in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2017Article
- Article
- Sporadic Gene Loss After Duplication Is Associated with Functional Divergence of Sirtuin Deacetylases Among Candida Yeast Species.G3 (Bethesda, Md.) · 2016Article
- Chromosome-wide histone deacetylation by sirtuins prevents hyperactivation of DNA damage-induced signaling upon replicative stress.Nucleic acids research · 2016Article
- Evolution and Functional Trajectory of Sir1 in Gene Silencing.Molecular and cellular biology · 2016Article
- The deacetylase Sir2 from the yeast Clavispora lusitaniae lacks the evolutionarily conserved capacity to generate subtelomeric heterochromatin.PLoS genetics · 2013Article
- Alternative splicing and subfunctionalization generates functional diversity in fungal proteomes.PLoS genetics · 2013Article
- Natural genetic variation in yeast longevity.Genome research · 2012Article
- Biotinylation of lysine method identifies acetylated histone H3 lysine 79 in Saccharomyces cerevisiae as a substrate for Sir2.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The Sum1/Ndt80 transcriptional switch and commitment to meiosis in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2012Review
- Reinventing heterochromatin in budding yeasts: Sir2 and the origin recognition complex take center stage.Eukaryotic cell · 2011Review
- Degradation of mRNAs that lack a stop codon: a decade of nonstop progress.Wiley interdisciplinary reviews. RNAReview
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2 authors at 1 institution in 1 country.
Funding
Abstract
Protein families are generated by successive rounds of gene duplication and subsequent diversification. However, the paths by which duplicated genes acquire distinct functions are not well characterized. We focused on a pair of duplicated deacetylases from Saccharomyces cerevisiae, Sir2 and Hst1, that subfunctionalized after duplication. As a proxy for the ancestral, nonduplicated deacetylase, we studied Sir2 from another yeast, Kluyveromyces lactis. We compared the interaction domains of these deacetylases for the Sir transcriptional silencing complex, which acts with ScSir2, and the Sum1 repressor, which acts with ScHst1, and found that these interaction domains have been retained over the course of evolution and can be disrupted by simple amino acid substitutions. Therefore, Sir2 and Hst1 subfunctionalized by acquiring complementary inactivating mutations in these interaction domains.
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