Phylointeractomics reconstructs functional evolution of protein binding
Dennis Kappei,
Marion Scheibe,
Maciej Paszkowski-Rogacz,
Alina Bluhm,
Toni Ingolf Gossmann,
Sabrina Dietz,
Mario Dejung,
Holger Herlyn,
Frank Buchholz (),
Matthias Mann () and
Falk Butter ()
Additional contact information
Dennis Kappei: Cancer Science Institute of Singapore, National University of Singapore
Marion Scheibe: Institute of Molecular Biology (IMB) gGmbH
Maciej Paszkowski-Rogacz: Medical Systems Biology, UCC, University Hospital and Medical Faculty Carl Gustav Carus, TU Dresden
Alina Bluhm: Institute of Molecular Biology (IMB) gGmbH
Toni Ingolf Gossmann: University of Sheffield, Western Bank, Sheffield S10 2TN, UK
Sabrina Dietz: Institute of Molecular Biology (IMB) gGmbH
Mario Dejung: Institute of Molecular Biology (IMB) gGmbH
Holger Herlyn: Institute of Anthropology, University of Mainz
Frank Buchholz: Medical Systems Biology, UCC, University Hospital and Medical Faculty Carl Gustav Carus, TU Dresden
Matthias Mann: Max Planck Institute of Biochemistry
Falk Butter: Institute of Molecular Biology (IMB) gGmbH
Nature Communications, 2017, vol. 8, issue 1, 1-9
Abstract:
Abstract Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functional evolution. For instance, we show that TERF1 evolved as a telomere-binding protein in the common stem lineage of marsupial and placental mammals. Phylointeractomics is a versatile and scalable approach to investigate evolutionary changes in protein function and thus can provide experimental evidence for phylogenomic relationships.
Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (3)
Downloads: (external link)
https://www.nature.com/articles/ncomms14334 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14334
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/ncomms14334
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().