Evidence map›Paper›PMID 21949823›Full record

ArticlePloS one2011

Differences in the number of intrinsically disordered regions between yeast duplicated proteins, and their relationship with functional divergence.

Floriane Montanari, Denis C Shields, Nora Khaldi

Abstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Evolution of intrinsic disorder in eukaryotic proteins.Cellular and molecular life sciences : CMLS · 2017
    Review
  5. Intrinsic protein disorder reduces small-scale gene duplicability.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017
    Article
  6. Article
  7. Article
4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Floriane MontanariUCD Conway Institute of Biomolecular and Biomedical Research, School of Medicine and Medical Sciences, and UCD Complex and Adaptive Systems Laboratory, University College Dublin, Dublin, Republic of Ireland.
Denis C Shields
Nora Khaldi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIntrinsically disordered regions are enriched in short interaction motifs that play a critical role in many protein-protein interactions. Since new short interaction motifs may easily evolve, they have the potential to rapidly change protein interactions and cellular signaling. In this work we examined the dynamics of gain and loss of intrinsically disordered regions in duplicated proteins to inspect if changes after genome duplication can create functional divergence. For this purpose we used Saccharomyces cerevisiae and the outgroup species Lachancea kluyveri. PRINCIPAL

findingsWe find that genes duplicated as part of a genome duplication (ohnologs) are significantly more intrinsically disordered than singletons (p<2.2(e)-16, Wilcoxon), reflecting a preference for retaining intrinsically disordered proteins in duplicate. In addition, there have been marked changes in the extent of intrinsic disorder following duplication. A large number of duplicated genes have more intrinsic disorder than their L. kluyveri ortholog (29% for duplicates versus 25% for singletons) and an even greater number have less intrinsic disorder than the L. kluyveri ortholog (37% for duplicates versus 25% for singletons). Finally, we show that the number of physical interactions is significantly greater in the more intrinsically disordered ohnolog of a pair (p = 0.003, Wilcoxon).

conclusionThis work shows that intrinsic disorder gain and loss in a protein is a mechanism by which a genome can also diverge and innovate. The higher number of interactors for proteins that have gained intrinsic disorder compared with their duplicates may reflect the acquisition of new interaction partners or new functional roles.

Indexed as

Gene DuplicationGenes, DuplicateGenetic VariationAmino Acid SequenceComputational BiologyEvolution, MolecularGenome, FungalMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSaccharomyces cerevisiae Proteins

Identifiers

PMID21949823
PMCPMC3174238

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.